WO2025257254A1

WO2025257254A1 - Lipases and lipase variants and the use thereof

Info

Publication number: WO2025257254A1
Application number: PCT/EP2025/066263
Authority: WO
Inventors: Sigurd Friis TRUELSEN; Marco Malten; Jesper Vind; Sara Maria LANDVIK; Anders Gunnar SANDSTRÖM; Lars Lehmann Hylling Christensen; Mary Ann Stringer
Original assignee: Novozymes AS
Current assignee: Novozymes AS
Priority date: 2024-06-12
Filing date: 2025-06-11
Publication date: 2025-12-18
Anticipated expiration: 2026-12-12

Abstract

The present invention relates to lipases with a common three-dimensional structure, and variants thereof with an improved half-life improvement factor (HIF). The present invention also relates to polynucleotides encoding the lipases and variants, nucleic acid constructs, vectors, and host cells comprising the polynucleotides, compositions comprising the lipases or variants of the invention, and use of the variants.

Description

LIPASES AND LIPASE VARIANTS AND THE USE THEREOF REFERENCE TO A SEQUENCE LISTING This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference. FIELD OF THE INVENTION The present invention relates to lipases and lipase variants and the use thereof. The present invention also relates to polynucleotides encoding the lipases and lipase variants, nucleic acid constructs, vectors, and host cells comprising the polynucleotides, detergent compositions _{comprising the lipases and variants thereof, and use of the lipases and variants in a cleaning} _{process or in a biodiesel process.} BACKGROUND OF THE INVENTION I_{n the detergent industry, enzymes have been implemented in detergent compositions for} _{many decades. Enzymes used in such compositions include proteases, amylases, lipases} _{cellulases, mannanases as well as other enzymes or mixtures thereof.} _{Lipases are included in detergent or cleaning composition to improve fat removal. Over} the past decades the commercially most successful lipases for cleaning processes are variants _{of the Thermomyces lanuginosus lipase. However, today other lipases see the light of day due to} _{changes in detergent or cleaning compositions and cleaning conditions.} Bertolini et al (Eur. J. Biochem. 228, 863-869 (1995)) discloses Geotrichum candidum lipase I (GCL I). For unsaturated substrates having long fatty acyl chains (linoleic acid and alpha linoleic acid) GCL I show higher specific activity than GCL II, whereas GCL II showed higher specific activity against saturated substrates having short fatty acid chains. Despite the fact that lipases are commercially available, there is still a need for novel lipases and stable lipases. SUMMARY OF THE INVENTION T_{he present invention concerns novel lipases with a common three-dimensional structure} _{(TM-score>0.8), and variants thereof with an improved half-life improvement factor (HIF)} compared to the parent. In the first aspect, the invention relates to (parent) wildtype lipases having: i) a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, especially 1.00, compared to the three-dimensional s_{tructure of the lipase shown in any one of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or} SEQ ID NO: 4, respectively, wherein the three-dimensional structure is calculated using Al- phaFold; and/or ii) a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at l_{east 99%, in particular 100% sequence identity to the amino acid sequence of SEQ ID NO:} _{1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4, respectively; and} iii) lipase activity. T_{he lipases of the invention shown in SEQ ID NOs: 1, 2, 3, and 4, respectively, have improved} _{HIF compared to the Geotrichum candidum lipase I (GCL I) which is shown in SEQ ID NO: 5.} In the second aspect, the invention relates to lipase variants with an improved half-life improvement factor (HIF) compared to the corresponding parent lipases, i.e., SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, and SEQ ID NO: 4, respectively. I_{n an embodiment, the invention relates to variants of a parent lipase of the invention,} wherein the variant comprises: a) one or more mutations at positions corresponding to positions: V_{15, S17, P18, I71, G72, P116, Q117, N122, H125, V351, S352, P353, T354, P390, T391,} A395, G441, I442, P443, V446, S467, P468, L472, W526 of SEQ ID NO: 1, wherein the position numbering is based on the numbering of SEQ ID NO: 1; b_{) one or more mutations, in particular to Glu (E) or Arg (R), on the surface of the lipase} _{in SEQ ID NO: 1 within 5Å (angstrom), preferably within 4Å, more preferably within 3Å, even more} _{preferably within 2Å of the positions corresponding to the positions in a); wherein} i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to SEQ ID NO: , compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 1; and iii) the variant has lipase activity. I_{n an embodiment, the mutation or mutations (is)are (a) substitution(s). In a preferred em-} _{bodiment, the target positions is(are) replaced with/substituted to either an Arg (R) or a Glu (E).} _{In an embodiment, the variant comprises substitutions corresponding to one or more of:} _{V15E,R, S17E,R, P18E,R, I71E,R, G72E,R, P116E,R, Q117E,R, N122E,R, H125E,R, V351E,R,} _{S352E,R, P353E,R, T354E,R, P390E,R, T391E,R, A395E,R, G441E,R, I442E,R, P443E,R,} _{V446E,R, S467E,R, P468E,R, L472E,R, W526E,R, using SEQ ID NO: 1 for numbering.} _{In a preferred embodiment, the variant of the invention comprises one or more mutations} _{corresponding to: V15E, S17E, S17R, P18E, P18R, I71R, G72E, P116R, Q117E, N122R, H125E,} V351E, S352E, P353R, T354E, T354R, P390R, T391R, T391E, A395R, A395E, G441E, I442R, P443E, P443R, V446E, S467E, P468R, P468E, L472E, W526R, D462A+L472E, W526R, T391R, T391E, P116D+P468K, P116R+A395D, G72E+A395K+G512D, G72E+A395K, P443R+S467D, A395K+L472E, T391E+A395D+P468K, Q117E+T391E+P443K, I71K+Q117E+T391E+A395K, wherein the position numbering is based on SEQ ID NO: 1. I_{n an embodiment, the invention relates to variants of a parent lipase of the invention,} wherein the variant comprises: a) one or more mutations at positions corresponding to positions: Y494 or S500 of SEQ ID NO: 2, wherein the position numbering is based on the numbering of SEQ ID NO: 2; and/or _{b) one or more mutations, in particular to Glu (E) or Arg (R), on the surface of the lipase in SEQ} ID NO: 2 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at l_{east 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to} SEQ ID NO: 2, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 2; and iii) the variant has lipase activity. In an embodiment, the variant comprises a substitution corresponding to one or more of: Y494E,R or S500E,R using SEQ ID NO: 2 for numbering. In a preferred embodiment, the variant of the invention comprises one or more mutations corresponding to: Y494E or S500E of SEQ ID NO: 2, wherein the position numbering is based on the numbering of SEQ ID NO: 2. In a preferred embodiment, the mutation or mutations (is)are (a) substitution(s). In a pre- _{ferred embodiment, the target position(s) is(are) replaced with/substituted to either an Arg (R) or} a Glu (E). I_{n an embodiment, the invention relates to variants of a parent lipase of the invention,} wherein the variant comprises: _{a) one or more mutations at positions corresponding to positions: L38, A41, Y76, Q171, Y176,} K212, K308, S325, A371, F374, V514, P515, F517, Y527, K530 of SEQ ID NO: 3, wherein the position numbering is based on the numbering of SEQ ID NO: 3; _{b) one or more mutations, in particular to Glu (E) or Arg (R), on the surface of the lipase in SEQ} ID NO: 3 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within _{2Å of the positions corresponding to the positions in a); wherein} i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at l_{east 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to} SEQ ID NO: 3, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 3; and iii) the variant has lipase activity. In an embodiment, the variant comprises a substitution corresponding to one or more of: _{L38E,R, A41E,R, Y76E,R, Q171E,R, Y176E,R, K212E,R, K308E,R, S325E,R, A371E,R,} _{F374E,R, V514E,R, P515E,R, F517E,R, Y527E,R, K530E,R using SEQ ID NO: 3 for position} numbering. I_{n a preferred embodiment, the variants comprise one or more mutations corresponding} _{to: L38R, A41R, Y76R, Q171R, Q171E, Y176E, K212E, S325E, A371E, F374E, K308E, V514R,} P515E, F517R, Y527E, K530R, A55V+V514R, S489L+P515E of SEQ ID NO: 3, wherein the po- sition numbering is based on the numbering of SEQ ID NO: 3. In a preferred embodiment, the mutation or mutations (is)are (a) substitution(s). In a pre- _{ferred embodiment, the target position(s) is(are) replaced with/substituted to either an Arg (R) or} a Glu (E). I_{n an embodiment, the invention relates to variants of a parent lipase of the invention,} wherein the variant comprises: a) one or more mutations at positions corresponding to positions: P45, S70, L71, P72, L75, I79, K81, V83, N84, L90, K193, L397, I443, Y529 of SEQ ID NO: 4 wherein the position numbering is based on the numbering of SEQ ID NO: 4; _{b) one or more mutations, in particular to Glu (E) or Arg (R), on the surface of the lipase in SEQ} ID NO: 4 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at l_{east 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to} SEQ ID NO: 4, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 4; and iii) the variant has lipase activity. _{In an embodiment, the variant comprises a substitution corresponding to one or more of:} P45E,R, S70E,R, L71E,R, P72E,R, L75E,R, I79E,R, K81E,R, V83E,R, N84E,R, T86E,R, L90E,R, _{K193E,R, L397E,R, I443E,R, Y529E,R using SEQ ID NO: 4 for numbering.} _{In a preferred embodiment, the variant comprises one or more mutations corresponding} _{to: P45R, S70E, S70R, L71R, P72E, L75R, L75E, I79R, K81E, K81R, V83R, N84E, T86R, L90R,} K193E, I443E, Y529E, S70R+P72E+A73V+I79R+K81E+N84E, I79R+K81E+N84E, _{S70R+A73V+L75E+I79R+K81R+N84E, P72E+A73V+K81E+N84E, K81E+N84E,} P72E+A73V+K81R+N84E, P72E+A73V+K81R+N84E+S359G, R437L+I443E of SEQ ID NO: 4, _{wherein the position numbering is based on the numbering of SEQ ID NO: 4.} In a preferred embodiment, the mutation or mutations (is)are (a) substitution(s). In a pre- _{ferred embodiment, the target position(s) is(are) replaced with/substituted to either an Arginine} _{(Arg or R) or a Glutamic acid (Glu or E).} In an embodiment, a lipase of the invention or a lipase variant of the invention has at most 10%, preferably at most 5%, at most 4% at most 3%, at most 2%, at most 1% sequence _{differences relative to SEQ ID NOs: 1, 2, 3, and 4, respectively.} _{A variant of the invention has an improved half-life improvement factor (HIF) compared to} _{the corresponding parent lipase. This is supported in the Examples.} _{In a third aspect, the present invention relates to a polynucleotide encoding a lipase of the} _{first aspect or a lipase variant of the second aspect.} _{In a fourth aspect, the present invention relates to a nucleic acid construct or expression} _{vector comprising a polynucleotide of the third aspect.} _{In a fifth aspect, the present invention relates to a recombinant host cell comprising in its} _{genome a nucleic acid construct or expression vector according to the fourth aspect.} _{In a sixth aspect, the present invention relates to methods for obtaining a lipase variant of} the invention, comprising: (_{a) introducing into a parent lipase according to the invention, one or more mutations at} positions according to the variant of the invention and optionally further introducing one or more _{mutations at at least one, two, three, e.g., at least four, at least five, at least six, at least seven, at} least eight, or nine positions; and (_{b) optionally recovering the lipase variant.} _{In a seventh aspect, the present invention relates to a method of producing a lipase of the} _{first aspect or a lipase variant of the second aspect, comprising (a) cultivating a recombinant host} _{cell of the fifth aspect under conditions suitable for expression of the lipase or lipase variant; and} _{(b) optionally recovering the lipase and lipase variant.} _{In the eighth aspect, the present invention relates to a composition comprising a lipase of} _{the first aspect or a lipase variant of the second aspect.} _{In a ninth aspect, the present invention relates to a method of cleaning an object, com-} _{prising contacting an object with a composition of the eighth aspect under conditions suitable for} cleaning the object. I_{n a tenth aspect, the present invention relates to use of a lipase of the first aspect or a} _{lipase variant of the second aspect or a composition of the eighth aspect in a cleaning process.} In the eleventh aspect, the present invention relates to the use of a lipase of the first aspect or lipase variant of the second aspect or a composition of the eight aspect in a cleaning process, preferably laundry or hard surface cleaning such as hand dishwashing (HDW) or automatic dish- washing (ADW). In the twelfth aspect, the present invention relates to the use of a lipase of the first aspect _{or lipase variant of the second aspect or a composition of the eighth aspect for hydrolyzing a} lipase substrate. BRIEF DESCRIPTION OF THE FIGURES F_{igure 1 shows a multiple alignment of SEQ ID NOs: 1, 2, 3, and 4.} SEQUENCE OVERVIEW S_{EQ ID NO:1 is a lipase derived from Eleutherascus tuberculatus.} APPQVRVKNG TYEGVHSPIF NQDFFLGIPY VRAPVGELRY AVPASLEETW EGKRDAKRYS DVCVGYGSDQ IGFTQSEDCL TLNIVRPSLS SSSSSLLPVA VWIHGGGLYM GSSARPQYNL SNIIHVSQSV GTPIIGVSIN YRLAGLGFLA SEEVVDEGVT NLGLRDQRKA LEWIQENIAF FGGDPRKVTI WGESAGGLSV GAHLVGWGAK DYGLFRSAIA ESGGPAWYSS YQDITYYQPH YNALLTSVGC SPSNNNNSSS SSISTSTLTC LRSVPLSLLN ATLSAQSSIW TFPLIDGDVY HQRPSLSLKS GDFVNVPLLI GANSDEGTSF GEWGVNTDDE FEEFVAEVFP VSPTPAPSPN LTLPNKTVSS LLALYPNSPA HQIPLSFTLP TPAGALGSQY KRVATYAGDM RMIAPRRAVC QAWAAHKTPV YCYRFDTVPA GIPDYVGATH FQEVAWVFYN VDGWGYSPSP FLGKPERYKE LALEMARRWV GFVVGADPNG AGLPYWPDYG NGEGAMVFEG NRSRSWVEKD DYRKEGIRFI NEHADEYRR S_{EQ ID NO:2 is a lipase derived from Rhizoctonia solani.} YPTVEGSNVS WLGVRNATAE FNYDYFFGIP FGQAPVGALR FKPPVAWTPT SSNTVVNATV EGASCEQGTE TDVANVSEDC LNLNIWRPSN ISGKIPVMVW IYGGGFYFGS TVYYPGENLV QTSVELNKPV IYVSINYRTG IYGFPPGQEA AAAGALNLGL KDQRLALEWI QKNIGYFGGD PTKVTLFGNS AGAVSTSYQS TYKGGDIGGV FRAMILESGS PSTVNVPPAN DPVLESVFTF VVNATGCNDS ADKFECVRNA PADVLSQANK DAIVPPAELK GVDQGPVAVG PVLAPGDDFL SKLPSESIHT GEFAKVPFIN GAQLDEGTIF VNGEYPETEE DVINWLISQI PGLYWGINNR TAVEELLKFY PADPAAGSPY NTGAETFGQA AQYKRLTSIV GDLLFQASRR DHLRTATKLG VNTWSYLFTE ALPWDAKYGV YHTGEYAFVL NRVRTWEGMP AGLLALEKPV LDYWLSFVYY LDPNVNRVYG ERPYWPKYGS NATAIHFASN VTLGTDDFRK DGIDFIINSP SIYN S_{EQ ID NO:3 is a lipase derived from Westerdykella sp.} AAPSVDLGYA VYEGSYNASS KVNSFKGVRY AAAPLGNLRW AAPKAPATNR SSPIAATEYP PACPQTGASS ETPPAYGFVS RLGNEDCLFL NVFAPANARN LPVFFWIHGG GYGLFSSSGL DPTEFMSTNG NSFVSVVIQY RLGAFGFLSG EDIKQGGALN AGLLDMNFAL QWVQRYIQKF GGDPARVTIA GESAGGAAVM YQAMAYGGKQ DKVLFNNVIT ASPWIPYQHN YDDQVPTQAY DDFAKAAGCE DASDTLQCLR AADTVVLQNA SAKVSEAGPF GTFAFLPVTD GSFVQKRPTE QLFAKAVKGK RLLSSNLAHE GVPLSPPTAK TLEAFRDYID VTFPNFSEAD KAALEKQYSY AGDGRDTDLS APLFDTTGTS GPTAVNQSVH ATGQQQRVFN VFAEYAFDCP SYWMASAFPQ AWKYQWSAQP AYHGFDLNAL WSKGKTTPGR DVIHAFQKIW GNFITTNNPL ISISDAKGSK NNATVPIGSS GKINWPQWTD SKPMLLSLNF TGGVPVFNEP TENLKYYTYK DPGVTNHFKV ADARNWEGGR GNRCDWWKKQ AAKVPY S_{EQ ID NO:4 is a lipase derived from Phlebiodontia subochracea} AAPTVTLDKG VFTGINNAST QTNKFLGIPY AQPPVGNLRF NLPAPNSPYA GTYNATAFGF SCVGSGNGPS LPANLPPSIV KIVNETFGLL PTRVENEDCL TVNVVQPQNV TPGKKLPVVA WIFGGGFEEG ASNEYPGALV VEESIKRGQP VIYVSMNYRL SAYGFLASKE VQAAGVGNLG LQDQRLALRW IQKYISAFGG DPSRVTIWGE SAGAISVALH LVANNGVNEG LFHGAFMQSG SPIPVGSILN GQKYYNALVA NTGCTGATDT LACLRALPFK TLKAGVDLAP GLFSYQSLNV AWLPRVDGKF ITDNPQNLTL AGKVARVPLV SGDCDDEGTL FTLQLSNITT EQQVFNYVSS NYMPQAPAAA ISKLLAYYPQ DPTQGSPYGT GTKNQELGPQ FKRLASLQGD LVFQAPRRFF LQTVSSSQPA WSYLSTRLKS LPIVGSMHGT DLLNSYGILN LNADLLGYLI NFVNKLNPND GSLPQWPQYT RSSPIMLTFQ DDPLKRVTIT ADAYRQDGMV LLTQLSLAYP L S_{EQ ID NO:5 is a lipase derived from Geotrichum candidum.} QAPTAVLNGN EVISGVLEGK VDTFKGIPFA DPPVGDLRFK HPQPFTGSYQ GLKANDFSSA CMQLDPGNAI SLLDKVVGLG KIIPDNLRGP LYDMAQGSVS MNEDCLYLNV FRPAGTKPDA KLPVMVWIYG GAFVFGSSAS YPGNGYVKES VEMGQPVVFV SINYRTGPYG FLGGDAITAE GNTNAGLHDQ RKGLEWVSDN IANFGGDPDK VMIFGESAGA MSVAHQLVAY GGDNTYNGKQ LFHSAILQSG GPLPYFDSTS VGPESAYSRF AQYAGCDASA GDNETLACLR SKSSDVLHSA QNSYDLKDLF GLLPQFLGFG PRPDGNIIPD AAYELYRSGR YAKVPYITGN QEDEGTILAP VAINATTTPH VKKWLKYICS EASDASLDRV LSLYPGSWSE GAPFRTGILN ALTPQFKRIA AIFTDLLFQS PRRVMLNATK DVNRWTYLAT QLHNLVPFLG TFHGSDLLFQ YYVDLGPSSA YRRYFISFAN HHDPNVGTNL KQWDMYTDAG REMLQIHMIG NSMRTDDFRI EGISNFESDV TLFG DEFINITIONS In accordance with this detailed description, the following definitions apply. Note that the singular forms "a," "an," and "the" include plural references unless the context clearly dictates otherwise. Unless defined otherwise or clearly indicated by context, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. AlphaFold structure prediction: AlphaFold is a computational method for predicting the three-dimensional structure of a polypeptide from its amino acid sequence (Jumper et al., Highly accurate protein structure prediction with AlphaFold. Nature, 2021). Predicted structures for millions of polypeptides deposited in the UniProt database have been deposited in the AlphaFold _{Protein Structure Database, using the AlphaFold Monomer v2.0 model (Varadi et al. AlphaFold} Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Research, 2021). In the AlphaFold Protein Structure Database, the three-dimensional structure of a polypeptide can be obtained by searching for the UniProt accession number of the polypeptide. In addition to the many three-dimensional structures that are already publicly available, code is available for reproducing and predicting structures of new polypeptides at source code repositories such as Github.com under deepmind/alphafold/, using notebooks/AlphaFold.ipynb, which uses AlphaFold v2.3.1 or newer. Additionally, it can be found in Github.com under sokrypton/ColabFold using v1.5.2 or newer, using AlphaFold2.ipynb. For technical details, please see Jumper et al. (vide supra). AlphaFold produces a per-residue estimate of its confidence on a scale from 0 to 100. This confidence measure is called pLDDT and corresponds to the model’s predicted score on the lDDT-Cα metric. It is stored in the B-factor fields of the mmCIF and PDB files available for download (although unlike a B-factor, higher pLDDT is better). Regions with pLDDT score of more than 90 are expected to be modelled to high accuracy. These should be suitable for any application that benefits from high accuracy (e.g., characterization of binding sites). Regions with a pLDDT score between 70 and 90 are expected to be modelled well, corresponding to a generally good backbone prediction. c_{DNA: The term "cDNA" means a DNA molecule that can be prepared by reverse} transcription from a mature, spliced, mRNA molecule obtained from a eukaryotic or prokaryotic cell. cDNA lacks intron sequences that may be present in the corresponding genomic DNA. The initial, primary RNA transcript is a precursor to mRNA that is processed through a series of steps, including splicing, before appearing as mature spliced mRNA. C_{oding sequence: The term “coding sequence” means a polynucleotide, which directly} specifies the amino acid sequence of a variant. The boundaries of the coding sequence are generally determined by an open reading frame, which begins with a start codon such as ATG, GTG or TTG and ends with a stop codon such as TAA, TAG, or TGA. The coding sequence may be a genomic DNA, cDNA, synthetic DNA, or a combination thereof. _{Control sequences: The term “control sequences” means nucleic acid sequences} involved in regulation of expression of a polynucleotide in a specific organism or in vitro. Each control sequence may be native (i.e., from the same gene) or heterologous (i.e., from a different gene) to the polynucleotide encoding the variant, and native or heterologous to each other. Such control sequences include, but are not limited to leader, polyadenylation, prepropeptide, propeptide, signal peptide, promoter, terminator, enhancer, and transcription or translation initiator and terminator sequences. At a minimum, the control sequences include a promoter, and transcriptional and translational stop signals. The control sequences may be provided with linkers for the purpose of introducing specific restriction sites facilitating ligation of the control sequences with the coding region of the polynucleotide encoding a variant. E_{xpression: The term “expression” includes any step involved in the production of a} _{lipase or a variant thereof including, but not limited to, transcription, post-transcriptional} modification, translation, post-translational modification, and secretion. E_{xpression vector: An "expression vector" refers to a linear or circular DNA construct} comprising a DNA sequence encoding a variant, which coding sequence is operably linked to a suitable control sequence capable of effecting expression of the DNA in a suitable host. Such control sequences may include a promoter to effect transcription, an optional operator sequence to control transcription, a sequence encoding suitable ribosome binding sites on the mRNA, enhancers and sequences which control termination of transcription and translation. E_{xtension: The term “extension” means an addition of one or more amino acids to the} _{amino and/or carboxyl terminus of a variant, wherein the “extended” variant has lipase activity.} _{Fragment: The term “fragment” means a variant having one or more amino acids absent} _{from the amino and/or carboxyl terminus of the variant; wherein the fragment has lipase activity.} _{Fusion polypeptide: The term “fusion polypeptide” is a polypeptide in which one} polypeptide is fused at the N-terminus and/or the C-terminus of a lipase or lipase variant of the present invention. A fusion polypeptide is produced by fusing a polynucleotide encoding another polypeptide to a polynucleotide of the present invention, or by fusing two or more polynucleotides of the present invention together. Techniques for producing fusion polypeptides are known in the _{art and include ligating the coding sequences encoding the polypeptides so that they are in frame} and that expression of the fusion polypeptide is under control of the same promoter(s) and terminator. Fusion polypeptides may also be constructed using intein technology in which fusion _{polypeptides are created post-translationally (Cooper et al., 1993, EMBO J. 12: 2575-2583;} _{Dawson et al., 1994, Science 266: 776-779). A fusion polypeptide can further comprise a} cleavage site between the two polypeptides. Upon secretion of the fusion protein, the site is cleaved releasing the two polypeptides. Examples of cleavage sites include, but are not limited _{to, the sites disclosed in Martin et al., 2003, J. Ind. Microbiol. Biotechnol. 3: 568-576; Svetina et} _{al., 2000, J. Biotechnol. 76: 245-251; Rasmussen-Wilson et al., 1997, Appl. Environ. Microbiol.} _{63: 3488-3493; Ward et al., 1995, Biotechnology 13: 498-503; and Contreras et al., 1991,} _{Biotechnology 9: 378-381; Eaton et al., 1986, Biochemistry 25: 505-512; Collins-Racie et al., 1995,} _{Biotechnology 13: 982-987; Carter et al., 1989, Proteins: Structure, Function, and Genetics 6:} _{240-248; and Stevens, 2003, Drug Discovery World 4: 35-48.} _{Half-life: “half-life” is a measure of a lipase’s or lipase variant’s stability and is determined} as the time it takes for the lipase to lose half of its enzymatic activity under a given set of conditions. It is denoted as T½ or T½ and is measured at a suitable time scale. Half-life can be calculated at _{a given detergent concentration and storage temperature (e.g.,at room temperature, 30ºC or} 37ºC) for a wild-type control and/or variants, as the degradation follows an exponential decay and the incubation time (hours) is known. H_{alf-life improvement factor: The term "half-life improvement factor" or "HIF" is the} improvement of half-life of a lipase variant compared to the reference lipase, such as a parent or wild-type lipase. A half-life improvement factor (HIF) under a given set of storage conditions (detergent concentration and temperature) can be calculated as: _{where the reference (e.g., the wild-type (wt)) is incubated under the same conditions as the vari-} _{ant. In the cases where the reference (e.g., wild-type or parent) lipase is not stable in the give} detergent concentration a more stable variant of the parent lipase may be used as reference. H_{eterologous: The term "heterologous" means, with respect to a host cell, that a poly-} peptide or nucleic acid does not naturally occur in the host cell. The term "heterologous" means, with respect to a polypeptide or nucleic acid, that a control sequence, e.g., promoter, of a poly- peptide or nucleic acid is not naturally associated with the polypeptide or nucleic acid, i.e., the control sequence is from a gene other than the gene encoding the mature polypeptide. H_{ost Strain or Host Cell: A "host strain" or "host cell" is an organism into which an} expression vector, phage, virus, or other DNA construct, including a polynucleotide encoding a variant has been introduced. Exemplary host strains are microorganism cells (e.g., bacteria, filamentous fungi, and yeast) capable of expressing the polypeptide of interest and/or fermenting saccharides. The term "host cell" includes protoplasts created from cells. I_{mproved property: The term “improved property” means a characteristic associated with} _{a variant that is improved compared to the parent (e.g., wilt-type). Such improved properties} _{include, but are not limited to, catalytic efficiency, catalytic rate, chemical stability, mildness,} oxidation stability, pH activity, pH stability, specific activity, stability under storage conditions, substrate binding, substrate cleavage, substrate specificity, substrate stability, surface properties, thermal activity, thermostability, reduced malodor generation, wash performance, and improved benefit risk factor (BRF). _{Introduced: The term "introduced" in the context of inserting a nucleic acid sequence into} _{a cell means "transfection", "transformation" or "transduction," as known in the art.} _{Isolated: The term “isolated” means a variant, nucleic acid, cell, or other specified material} or component that is separated from at least one other material or component, including but not limited to, other proteins, nucleic acids, cells, etc. An isolated polypeptide, nucleic acid, cell or _{other material is thus in a form that does not occur in nature. An isolated polypeptide includes,} but is not limited to, a culture broth containing the secreted variant expressed in a host cell. L_{ipase: The terms “lipase”, “lipase enzyme”, “lipolytic enzyme”, “lipid esterase”, “lipolytic} polypeptide”, and “lipolytic protein” refer to an enzyme in class EC3.1.1 as defined by Enzyme Nomenclature. It may have lipase activity (triacylglycerol lipase, EC3.1.1.3), cutinase activity (EC3.1.1.74), sterol esterase activity (EC3.1.1.13) and/or wax-ester hydrolase activity (EC3.1.1.50). In this context a “lipase substrate” is any substrate which can be hydrolyzed by the _{lipase of the invention. For purposes of the present invention lipase activity (i.e. the hydrolytic} activity of the lipase) may be determined with a pNP assay using substrates with various chain length as described in Example A. L_{ipase variant: The terms “lipase variant” refers to a lipase where one or more mutations} _{have been introduced when the lipase variant is aligned with the parent lipase.} _{Malodor: The term ”malodor” means an odor which is not desired on clean items. Malodor} can be quantified by SPME-GC as released butyric acid or assessed by sensory panel scoring. Unless otherwise specified the term malodour may be used interchangeably with the term odor. M_{ature polypeptide: The term “mature polypeptide” means a polypeptide in its mature} form following N-terminal processing and/or C-terminal processing (e.g., removal of signal peptide). M_{ature polypeptide coding sequence: The term “mature polypeptide coding sequence”} _{means a polynucleotide that encodes a mature polypeptide having protease activity.} _{Mutant: The term “mutant” means a polynucleotide encoding a variant.} _{Native: The term "native" means a nucleic acid or polypeptide naturally occurring in a host} cell. N_{ucleic acid: The term "nucleic acid" encompasses DNA, RNA, heteroduplexes, and} synthetic molecules capable of encoding a variant. Nucleic acids may be single stranded or _{double stranded and may be chemically modified. The terms "nucleic acid" and "polynucleotide"} are used interchangeably. Because the genetic code is degenerate, more than one codon may be used to encode a particular amino acid, and the present compositions and methods encompass nucleotide sequences that encode a particular amino acid sequence. Unless otherwise indicated, nucleic acid sequences are presented in 5'-to-3' orientation. N_{ucleic acid construct: The term "nucleic acid construct" means a nucleic acid molecule,} _{either single- or double-stranded, which is isolated from a naturally occurring gene or is modified} to contain segments of nucleic acids in a manner that would not otherwise exist in nature or which is synthetic, and which comprises one or more control sequences operably linked to the nucleic acid sequence. O_{perably linked: The term "operably linked" means that specified components are in a} relationship (including but not limited to juxtaposition) permitting them to function in an intended manner. For example, a regulatory sequence is operably linked to a coding sequence such that expression of the coding sequence is under control of the regulatory sequence. P_{arent or parent lipase: The term “parent” or “parent lipase” means a lipase to which an} _{alteration is made to produce lipase variants of the present invention. The parent may preferably} be one of the wild-type lipases of the invention shown in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 4. P_{urified: The term “purified” means a nucleic acid, lipase or lipase variant of the invention} or cell that is substantially free from other components as determined by analytical techniques well known in the art (e.g., a purified variant or nucleic acid may form a discrete band in an electrophoretic gel, chromatographic eluate, and/or a media subjected to density gradient centrifugation). A purified nucleic acid or variant is at least about 50% pure, usually at least about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about _{92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, about} 99.5%, about 99.6%, about 99.7%, about 99.8% or more pure (e.g., percent by weight or on a molar basis). In a related sense, a composition is enriched for a molecule when there is a substantial increase in the concentration of the molecule after application of a purification or _{enrichment technique. The term "enriched" refers to a compound, lipase or variant thereof, cell,} nucleic acid, amino acid, or other specified material or component that is present in a composition at a relative or absolute concentration that is higher than a starting composition. ln one aspect, the term "purified" as used herein refers to the lipase or lipase variant or cell being essentially free from components (especially insoluble components) from the production organism. In other aspects, the term "purified" refers to the lipase or variant thereof of the invention being essentially free of insoluble components (especially insoluble components) from the native organism from which it is obtained. In one aspect, the lipase or variant thereof of the invention is separated from some of the soluble components of the organism and culture _{medium from which it is recovered. The lipase or variant thereof may be purified (i.e., separated)} by one or more of the unit operations filtration, precipitation, or chromatography. Accordingly, the lipase or variant of the invention may be purified such that only minor amounts of other proteins, in particular, other polypeptides, are present. The term "purified" as used herein may refer to removal of other components, particularly other proteins and most particularly other enzymes present in the cell of origin of the polypeptide. The lipase or variant may be "substantially pure", i.e., free from other components from the organism in which it is produced, e.g., a host organism for recombinantly produced variant. In one aspect, the polypeptide is at least 40% pure by weight of the total polypeptide material present in the preparation. In one aspect, the polypeptide is at least 50%, 60%, 70%, 80% or 90% pure by weight of the total polypeptide material present in the preparation. As used herein, a "substantially pure polypeptide" may denote a polypeptide preparation that contains at most 10%, preferably at most 8%, more preferably at most 6%, more preferably at most 5%, more preferably at most 4%, more preferably at most 3%, even more preferably at most 2%, most preferably at most 1%, and even most preferably at most 0.5% by weight of other polypeptide material with which the polypeptide is natively or recombinantly associated. It is, therefore, preferred that the substantially pure lipase or variant thereof is at least 92% pure, preferably at least 94% pure, more preferably at least 95% pure, more preferably at least 96% pure, more preferably at least 97% pure, more preferably at least 98% pure, even more preferably at least 99% pure, most preferably at least 99.5% pure by weight of the total polypeptide material present in the preparation. The lipase or variant thereof of the present invention is preferably in a substantially pure form (i.e., the preparation is essentially free of other polypeptide material with which it is natively or recombinantly associated). This can be accomplished, for example by preparing the lipase or variant thereof by well-known recombinant methods or by classical purification methods. R_{ecombinant: The term "recombinant" is used in its conventional meaning to refer to the} manipulation, e.g., cutting and rejoining, of nucleic acid sequences to form constellations different from those found in nature. The term recombinant refers to a cell, nucleic acid, lipase or variant thereof, or vector that has been modified from its native state. Thus, for example, recombinant cells express genes that are not found within the native (non-recombinant) form of the cell, or express native genes at different levels or under different conditions than found in nature. The term “recombinant” is synonymous with “genetically modified” and “transgenic”. R_{ecover: The terms "recover" or “recovery” means the removal of a polypeptide from at} least one fermentation broth component selected from the list of a cell, a nucleic acid, or other specified material, e.g., recovery of the polypeptide from the whole fermentation broth, or from _{the cell-free fermentation broth, by polypeptide crystal harvest, by filtration, e.g., depth filtration} (by use of filter aids or packed filter medias, cloth filtration in chamber filters, rotary-drum filtration, drum filtration, rotary vacuum-drum filters, candle filters, horizontal leaf filters or similar, using _{sheet or pad filtration in framed or modular setups) or membrane filtration (using sheet filtration,} module filtration, candle filtration, microfiltration, ultrafiltration in either cross flow, dynamic cross flow or dead end operation), or by centrifugation (using decanter centrifuges, disc stack _{centrifuges, hydro cyclones or similar), or by precipitating the polypeptide and using relevant solid-} liquid separation methods to harvest the polypeptide from the broth media by use of classification separation by particle sizes. Recovery encompasses isolation and/or purification of the polypeptide. Solvent Accessible Surface Area (SASA): The SASA of an amino acid on surface of a lipase is determined using computational algorithms. First the protein structure is determined us- ing AlphaFold. A spherical probe, typically the size of a water molecule (~1.4 Å radius), is chosen to roll over the surface of the protein in question. Algorithms are applied to calculate the SASA. Many algorithms exist for this purpose, such as Lee-Richards' algorithm, Shrake-Rupley's algo- rithm, etc. These algorithms usually involve geometrical calculations. The path traced by the cen- ter of the probe forms the SASA. It is calculated in square angstroms (Å²). Software tools such as PyMOL, VMD, NACCESS or DSSP can be used to calculate the SASA of a protein. In context of the present invention, the relative SASA was determined using the program DSSP (mkdssp version 3.0.0) (Touw WG, Baakman C, Black J, te Beek TA, Krieger E, Joosten RP & Vriend G. A series of PDB-related databanks for everyday needs. Nucleic Acids Res. (2015) _{43, D364-D368, W. Kabsch and C. Sander, Biopolymers 22 (1983) 2577- 2637), and given in} values of Sander and Rost algorithm (Rost, B. and Sander, C. (1994), Conservation and predic- tion of solvent accessibility in protein families. Proteins, 20: 216-22) The relative SASA was set to 0.09 meaning that 9% of the surface of the amino acid is exposed. Additional amino acids were included if any atoms in their backbone or side chain were within the distance criterion (i.e., 2Å, _{3Å, 4Å or 5Å) of any atom in the backbone or side chain of said positions, and if the additional} _{amino acid had a relative SASA above the 0.09 threshold. A typical side chain length of Glu (E)} and Arg (R) are > 4 Å and > 7 Å, respectively. In context of the present invention, a distance threshold of 5 Å is therefore a reasonable distance criterion for additional amino acid positions, since they are within a likely interaction range. S_{equence Identity: The relatedness between two amino acid sequences or between two} nucleotide sequences is described by the parameter “sequence identity”. For purposes of the present invention, the sequence identity between two amino acid sequences is determined as the output of “longest identity” using the Needleman-Wunsch _{algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the} Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open _{Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 6.6.0 or later.} The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. In order for the Needle program to report the longest identity, the -nobrief option must be specified in the command line. The output of Needle labeled “longest identity” is calculated as follows: (_{Identical Residues x 100)/(Length of Alignment – Total Number of Gaps in Alignment)} For purposes of the present invention, the sequence identity between two polynucleotide sequences is determined as the output of “longest identity” using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), preferably version 6.6.0 or later. The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. In order for the Needle program to report the longest identity, the nobrief option must be specified in the command line. The output of Needle labeled “longest identity” is calculated as follows: _{(Identical Deoxyribonucleotides x 100)/(Length of Alignment – Total Number of Gaps in Alignment)} Sequence Difference: The term "sequence difference" means the percent of amino acid differences between a polypeptide and the polypeptide of SEQ ID NOs: 1, 2, 3 or 4, respectively, and is calculated as follows: (_{Different Residues x 100)/(Length of SEQ ID NOs: 1, 2, 3, and 4, respectively)} wherein the different residues comprise any substitution, deletion, or insertion (e.g., an extension at the N-terminus and/or C-terminus) in the sequence. S_{ignal Peptide: A "signal peptide" is a sequence of amino acids attached to the N-} terminal portion of a protein, which facilitates the secretion of the protein outside the cell. The mature form of an extracellular protein lacks the signal peptide, which is cleaved off during the secretion process. Structural Similarity: The relatedness between two amino acid sequences has conventionally been described by the parameter “sequence identity”. However, since the biological function of a polypeptide is defined by its three-dimensional structure rather than its amino acid sequence, a better way of assessing a functional relationship between polypeptides is by comparing their three-dimensional structures. Thus, for the purposes of the present invention, the relatedness between the three-dimensional structure of two polypeptides is described by the parameter “structural similarity”. A three-dimensional structure of any polypeptide may be obtained experimentally via, e.g., X-ray crystallography or using in silico methods such as AlphaFold (vide supra). The structural similarity between three-dimensional structures may then be determined by the TM-score, which is calculated using the following general formula (Zhang & Skolnick, Proteins 57:702–710, 2004): where LN is the length of the native structure, LT is the length of the aligned residues to the template structure, di is the distance between the ith pair of aligned residues and d0 is a scale to normalize the match difference. ‘Max’ denotes the maximum value after optimal spatial superposition. For the purposes of the present invention, LN is always the length of the reference protein, _{indicating the use of a fixed reference length L to prevent artificially large TM-scores from} alignment of substructures: T_M-score A_{structural alignment of the three-dimensional structures of two polypeptides is} necessary before the TM-score can be calculated. This is achieved via algorithms that optimize the structural overlap, and several methods are available, such as CEalign (Shindyalov and Bourne, Protein Eng., 11, 739-747, 1998), DALI (Holm and Sander, Trends Biochem. Sci., 20, 478-480, 1995), or TM-align (Nucleic Acids Res.33:2302-2309, 2005). For the purposes of the present invention, TM-align is applied. For convenience, TM-score is integrated in the TM-align software, which is available from the author’s website. The version of TM-align is preferably updated 2019-08-22 or later, and the TM-score between a reference and _{a query protein is determined by running this command:} TMalign <query.pdb> <reference.pdb> -L <length of reference> Where <query.pdb> is the name of the PDB file containing coordinates of the query polypeptide, <reference.pdb> is the name of the PDB file containing coordinates of the reference polypeptide. The TM-score is calculated and reported in the output, along with several other parameters from the alignment. T_{he maximal TM-score is 1, e.g., 1.0, corresponding to identical three-dimensional} structures. S_{ubsequence: The term “subsequence” means a polynucleotide having one or more} nucleotides absent from the 5' and/or 3' end of a mature polypeptide coding sequence; wherein _{the subsequence encodes a fragment having lipase activity.} _{Variant: The term “variant” means a polypeptide having lipase activity comprising a} substitution, an insertion (including extension), and/or a deletion (e.g., truncation), at one or more positions. A substitution means replacement of the amino acid occupying a position with a different amino acid; a deletion means removal of the amino acid occupying a position; and an insertion means adding 1-5 amino acids (e.g., 1-3 amino acids, in particular, 1 amino acid) adjacent to and immediately following the amino acid occupying a position. W_{ild-type: The term "wild-type" in reference to an amino acid sequence or nucleic acid} sequence means that the amino acid sequence or nucleic acid sequence is a native or naturally- occurring sequence. As used herein, the term "naturally-occurring" refers to anything (e.g., proteins, amino acids, or nucleic acid sequences) that is found in nature. Conversely, the term "non-naturally occurring" refers to anything that is not found in nature (e.g., recombinant nucleic acids and protein sequences produced in the laboratory or modification of the wild-type sequence). Wash cycle: The term “wash cycle” is defined as a washing operation wherein laundry, fabrics and/or textiles are immersed in wash liquor, mechanical action of some kind is applied in order to release stains and to facilitate flow of wash liquor in and out of the textile and finally the superfluous wash liquor is removed. After one or more wash cycles, the laundry, fabrics and/or textile is generally rinsed and dried. Wash liquor: The term “wash liquor” refers to an aqueous solution containing a detergent composition in dilute form, such as the wash liquor in a laundry process. Wash performance: The term “wash performance” is used as detergent composition’s, enzyme’s or polymer’s capability to remove stains present on the object to be cleaned or maintain color and whiteness of textile during wash. The improvement in the wash performance may be _{quantified by fat removal or odor generation.} Weight percentage: Weight percentage is abbreviated w/w%, wt% or w%. The abbrevi- ations are used interchangeably. Conventions for Designation of Variants F_{or purposes of the present invention, the polypeptide disclosed in SEQ ID NOs: 1, 2, 3} _{and 4, respectively, may be used to determine the corresponding amino acid positions in another} _{lipases. The amino acid sequence of another lipase is aligned with the polypeptide disclosed in} SEQ ID NOs:1, 2, 3 and 4, respectively, and based on the alignment, the amino acid position number corresponding to any amino acid residue in the polypeptide disclosed in SEQ ID NOs:1, 2, 3, and 4, respectively, is determined using the Needleman-Wunsch algorithm (Needleman and _{Wunsch, 1970, J. Mol. Biol.48: 443-453) as implemented in the Needle program of the EMBOSS} package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, _{Trends Genet. 16: 276-277), preferably version 6.6.0.0 or later. The parameters used are gap} open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of _{BLOSUM62) substitution matrix. A multiple alignment of the lipases in SEQ ID NOs: 1, 2, 3 and} _{4, respectively, using MUSCLE (MUSCLE v3.7 by Robert C. Edgar) is provided in Figure 1.} In describing the variants of the present invention, the nomenclature described below is adapted for ease of reference. The accepted IUPAC single letter or three letter amino acid abbreviation is employed. S_{ubstitutions: For an amino acid substitution, the following nomenclature is used: Original} _{amino acid, position, substituted amino acid. Accordingly, the substitution of Thr at position 226} _{with Ala is designated as “T226A”. Multiple mutations are separated by addition marks (“+”) or by} commas, e.g., “G205R+S411F” or “G205R,S411F”, representing substitutions at positions 205 _{and 411 of Gly (G) with Arg (R) and Ser (S) with Phe (F), respectively. Because the amino acid} residue at a given position varies from parent to parent, the amino acid to be substituted may be indicated with X, e.g., “X226A”. _{Deletions: For an amino acid deletion, the following nomenclature is used: Original amino} acid, position, *. Accordingly, the deletion of the amino acid Gly at position 195 is designated as “Gly195*”. Multiple deletions are separated by addition marks (“+”) or by commas, e.g., _{“G195*+S411*” or “G195*,S411*”. Because the amino acid residue at a given position varies from} parent to parent, the amino acid to be deleted may be indicated with X, e.g., “X195*”. I_{nsertions: For an amino acid insertion, the following nomenclature is used: Original amino} _{acid, position, original amino acid, inserted amino acid. Accordingly, the insertion of Lys after the} amino acid Gly at position 195 is designated “G195GK”. Because the amino acid residue at a given position varies from parent to parent, the insertion of lysine after the amino acid at position 195 may be indicated with “X195*”. An insertion of multiple amino acids is designated [original amino acid, position, original amino acid, inserted amino acid #1, inserted amino acid #2; etc.]. For example, the insertion of _{Lys and Ala after the amino acid Gly at position 195 is indicated as “G195GKA”. In such cases,} the inserted amino acid residue(s) are numbered by the addition of lower case letters to the position number of the amino acid residue preceding the inserted amino acid residue(s). In the above example, the sequence would thus be: P_{arent: Variant:} _{195 195195a 195b} _{G G - K - A} Alternatively, an insertion of an amino acid residue such as lysine after the amino acid at position 195 may be indicated by “195aK”, and the insertion of two or more additional amino acid _{residues such as Lys and Ala after the amino acid at position 195 may be indicated by} “195aK,195bA”. M_{ultiple alterations: Variants comprising multiple alterations are separated by addition} _{marks (“+”), e.g., “R170Y+G195E” representing a substitution of Arg and Gly at positions 170 and} _{195 with Tyr and Glu, respectively.} _{Different alterations: Where different alterations can be introduced at a position, the} different alterations are separated by a comma, e.g., “R170Y,E” represents a substitution of Arg _{at position 170 with Tyr or Glu. Thus, “Y167G,A+R170G,A” designates the following variants:} “Y167G+R170G”, Y167G+R170A”, “Y167A+R170G”, and “Y167A+R170A”. DETAILED DESCRIPTION OF THE INVENTION The present invention relates to novel lipases with a common three-dimensional structure _{(TM-score > 0.8), and variants thereof with an improved half-life improvement factor (HIF).} The inventors have surprisingly found that several wild-type lipases, despite having a low sequence identity to each other, structurally are very similar (i.e., Alphafold TM-score above 0.8) _{and further have improved HIF compared to the Geotrichum candidum lipase I (GCL I) shown in} _{SEQ ID NO: 5. The inventors also surprisingly found that by modifying amino acids in selected} _{regions of said wildtype lipases to either Arg (R) or Glu (E), the activity and/or stability is improved.} Arg (R) and Glu (E) were selected due to their electrostatic properties as either positively or negatively charged amino acids, respectively. _{Novel Lipases of the invention} _{The invention relates to novel wild-type lipases (see the Table below) The wild-type} lipases are the preferred parents of the lipase variants of the invention. The novel lipases have a common three-dimensional structure (i.e., have a TM-score > 0.8). W_{ild-type Lipase Donor} _{SEQ ID NO: 1 Eleutherascus tuberculatus} _{SEQ ID NO: 2 Rhizoctonia solani} _{SEQ ID NO: 3 Westerdykella sp.} _{SEQ ID NO: 4 Phlebiodontia subochracea} Thus, in the first aspect, the invention relates to novel (parent) lipases having: i) a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, especially 1.00, compared to the three-dimensional structure of the lipase shown in any one of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4, respectively, wherein the three-dimensional structure is calculated using Al- phaFold; and/or ii) a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, in particular 100% identity to the amino acid sequence of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4, respectively; and iii) lipase activity. _{In a first embodiment, the lipase has a TM-score of at least 0.80, e.g., at least 0.81, at} least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 1, but has a TM-score less than 1.00, such as less than 0.99, such as less than 0.98, such as less than 0.97 such as less than 0.96, such as less than 0.95 compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 5, wherein the three-dimensional structure is calculated using AlphaFold; and wherein the lipase has lipase activity. In a second embodiment, the lipase has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 2, but has a TM-score less than 1.00, such as less than 0.99, such as less than 0.98, such as less than 0.97 such as less than 0.96, such as less than 0.95 compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 5, wherein the three-dimensional structure is calculated using AlphaFold; and wherein the lipase has lipase activity. In a third embodiment, the lipase has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 3, but has a TM-score less than 1.00, such as less than 0.99, such as less than 0.98, such as less than 0.97 such as less than 0.96, such as less than 0.95 compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 5, wherein the three-dimensional structure is calculated using AlphaFold; and wherein the lipase has lipase activity. In an fourth embodiment, the lipase has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 4, but has a TM-score less than 1.00, such as less than 0.99, such as less than 0.98, such as less than 0.97 such as less than 0.96, such as less than 0.95 compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 5, wherein the three-dimensional structure is calculated using AlphaFold; and wherein the lipase has lipase activity. The lipases of the invention shown in SEQ ID NOs: 1, 2, 3, and 4, respectively, have improved _{HIF compared to the Geotrichum candidum lipase I (GCL I) which is shown in SEQ ID NO: 5.} Lipase Variants of the invention The invention also relates to variants of the novel (wild-type) parent lipases of the invention. Therefore, in the second aspect, the invention relates to lipase variants with improved half- life improvement factor (HIF) compared to the corresponding parent lipases, i.e., SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, and SEQ ID NO: 4, respectively. In an embodiment, the invention relates to variants of a parent lipase of the invention, wherein the variant comprises: a) one or more mutations at positions corresponding to positions: V15, S17, P18, I71, G72, P116, Q117, N122, H125, V351, S352, P353, T354, T354, P390, T391, A395, G441, I442, P443, V446, S467, P468, L472, W526 of SEQ ID NO: 1, wherein posi- tion numbering is based on the numbering of SEQ ID NO: 1; b_{) one or more mutations, in particular to E or R, on the surface of the lipase in SEQ ID} NO: 1 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to SEQ ID NO: 1, com- pared to the three-dimensional structure of the parent lipase, wherein the three-dimensional struc- ture is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 1; and iii) the variant has lipase activity. In a preferred embodiment, the mutation or mutations (is)are (a) substitution(s). In a pre- _{ferred embodiment, the target position(s) is(are) replaced with/substituted to either an Arg (R) or} a Glu (E). In an embodiment, the variant of the invention comprises substitutions corresponding to one or more of: V15E,R, S17E,R, P18E,R, I71E,R, G72E,R, P116E,R, Q117E,R, N122E,R, H125E,R, V351E,R, S352E,R, P353E,R, T354E,R, P390E,R, T391E,R, A395E,R, G441E,R, I442E,R, P443E,R, V446E,R, S467E,R, P468E,R, L472E,R, W526E,R, using SEQ ID NO: 1 for numbering. In a preferred embodiment, said variant of the invention comprises one or more mutations _{corresponding to: V15E, S17E, S17R, P18E, P18R, I71R, G72E, P116R, Q117E, N122R, H125E,} V351E, S352E, P353R, T353E. T353R, P390R, T391R, T391E, A395R, A395E, G441E, I442R, P443E, P443R, V446E, S467E, P468R, P468E, L472E, W526R, D462A+L472E, W526R, T391R, T391E, P116D+P468K, P116R+A395D, G72E+A395K+G512D, G72E+A395K, P443R+S467D, A395K+L472E, T391E+A395D+P468K, Q117E+T391E+P443K, I71K+Q117E+T391E+A395K, wherein the position numbering is based on SEQ ID NO: 1. In an embodiment, one or more of the following positions on the surface of the lipase in SEQ ID NO: 1 within 5Å of the positions corresponding to the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 1) are mutated to Glu (E) or Arg (R): 3, 13, 16, 19, 20, 21,} 24, 57, 67, 68, 73, 74, 114, 115, 119, 128, 129, 328, 333, 334, 388, 389, 392, 393, 394, 396, 434, _{438, 440, 444, 445, 451, 452, 464, 465, 466, 469, 473, 474, 519, 522, 524, 527, 528, in particular} P3E,R, E13R, H16E,R, I19E,R, F20E,R, N21E,R, F24E,R, K57E,R, G67E,R, S68E,R, D69E,R, F73E,R, T74E,R, A114E,R, R115E, N119E,R, Q128E,R, S129E,R, T328E,R, W333E,R, G334E,R, T388E,R, L389E,R, P392E,R, A393E,R, G394E,R, L396E,R, R434E, V438E,R, A440E,R, D444E,R, Y445E,R, F451E,R, Q452E,R, W464E,R, G465E,R, Y466E,R, S469E,R, _{G473E,R, K474E,R, E519R, R522E, R524E, V527E,R, E528R in SEQ ID NO: 1.} In an embodiment, one or more of the following positions on the surface of the lipase in _{SEQ ID NO: 1 within 4Å of the positions corresponding to the positions mentioned under item a)} _{above (i.e., mutations in SEQ ID NO: 1) are mutated to Glu (E) or Arg (R): 3, 16, 19, 20, 21, 24,} 57, 68, 69, 73, 114, 115, 119, 128, 129, 328, 333, 334, 389, 392, 393, 394, 396, 438, 440, 444, _{445, 464, 465, 466, 469, 473, 474, 519, 522, 524, 527, 528, in particular P3, H16, I19, F20, N21,} F24, K57, S68, D69, F73, A114, R115, N119, Q128, S129, T328, W333, G334, L389, P392, A393, G394, L396, V438, A440, D444, Y445, W464,G465, Y466, S469, G473, K474, E519, R522, R524, V527, E528 in SEQ ID NO: 1. In an embodiment, one or more of the following positions on the surface of the lipase in SEQ ID NO: 1 within 3Å of the positions corresponding in the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 1) are mutated to Glu (E) or Arg (R): 16, 19, 21, 24, 73,} _{115, 328, 389, 392, 393, 394, 396, 440, 444, 445, 466, 469, 473, 527, in particular H16E,R,} _{I19E,R, N21E,R, F24E,R, F73E,R, R115E, T328E,R, L389E,R, P392E,R, A393E,R, G394E,R,} _{L396E,R, A440E,R, D444E,R, Y445E,R, Y466E,R, S469E,R, G473E,R, V527E,R in SEQ ID NO:} 1. In an embodiment, one or more of the following positions on the surface of the lipase in SEQ ID NO: 1 within 2Å of the positions corresponding in the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 1) are mutated to Glu (E) or Arg (R): 16, 19, 73, 115, 389,} 392, 394, 396, 440, 444, 445, 466, 469, 473, 527, in particular H16E,R, I19E,R, F73E,R, R115E, L389E,R, P392E,R, G394E,R, L396E,R, A440E,R, D444E,R, Y445E,R, Y466E,R, S469E,R, _{G473E,R, V527E,R in SEQ ID NO: 1.} In an embodiment, the invention relates to variants of a parent lipase of the invention, wherein the variant comprises: a) one or more mutations at positions corresponding to positions: Y494 or S500 of SEQ ID NO: 2, wherein position numbering is based on the numbering of SEQ ID NO: 2; and/or _{b) one or more mutations, in particular to E or R, on the surface of the lipase in SEQ ID NO: 2} within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at l_{east 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to} SEQ ID NO: 2, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 2; and iii) the variant has lipase activity. Said variants comprises one or more mutations corresponding to: Y494E or S500E of SEQ ID NO: 2, wherein the position numbering is based on the numbering of SEQ ID NO: 2. In a preferred embodiment, the mutation or mutations (is)are (a) substitution(s). In a pre- _{ferred embodiment, the target position(s) is(are) replaced with/substituted to either an Arg (R) or} a Glu (E). In an embodiment, one or more of the following positions on the surface of the lipase in SEQ ID NO: 2 within 5Å of the positions corresponding to the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 2) are mutated to Glu (E) or Arg (R): 484, 487, 492, 493,} 496, 499, 501, 502, 513, in particular N484E,R, R487E, R492E, P493E,R, P496E,R, G499E,R, _{N501E,R, A502E,R, L513E,R in SEQ ID NO: 2.} _{In an embodiment, one or more of the following positions on the surface of the lipase in} SEQ ID NO: 2 within 4Å of the positions corresponding to the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 2) are mutated to Glu (E) or Arg (R): 484, 492, 493, 496,} _{499, 501, 502, 513, in particular N484E,R, R492E, P493E,R, P496E,R, G499E,R, N501E,R,} _{A502E,R, L513E,R in SEQ ID NO: 2.} _{In an embodiment, one or more of the following positions on the surface of the lipase in} SEQ ID NO: 2 within 3Å of the positions corresponding in the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 2) are mutated to Glu (E) or Arg (R): 493, 496, 499, 501,} _{in particular P493E,R, P496E,R, G499E,R, N501E,R in SEQ ID NO: 2.} In an embodiment one or more of the following positions on the surface of the lipase in SEQ ID NO: 2 within 2Å of the positions corresponding in the positions mentioned under item a) _{above (for mutations in SEQ ID NO: 1) are mutated to Glu (E) or Arg (R): 493, 499, 501, in par-} _{ticular P493E,R, G499E,R, N501E,R in SEQ ID NO: 2.} In an embodiment, the invention relates to variants of a parent lipase of the invention, wherein the variant comprises: a) one or more mutations at positions corresponding to positions: _{L38, A41, Y76, Q171, Y176, K212, K308, S325, A371, F374, V514, P515, F517, Y527, K530 of} SEQ ID NO: 3, wherein position numbering is based on the numbering of SEQ ID NO: 3; _{b) one or more mutations, in particular to E or R, on the surface of the lipase in SEQ ID NO: 3} within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at l_{east 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to} SEQ ID NO: 3, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 3; and iii) the variant has lipase activity. S_{aid variants comprise one or more mutations corresponding to: L38E,R, A41E,R,} _{Y76E,R, Q171E,R, Q171E,R, Y176E,R, K212E,R, S325E,R, A371E,R, F374E,R, K308E,R,} _{V514E,R, P515E,R, F517E,R, Y527E,R, K530E,R, in particular L38R, A41R, Y76R, Q171R,} Q171E, Y176E, K212E, S325E, A371E, F374E, K308E, V514R, P515E, F517R, Y527E, K530R, A55V+V514R, S489L+P515E of SEQ ID NO: 3, wherein the position numbering is based on the numbering of SEQ ID NO: 3. In a preferred embodiment, the mutation or mutations (is)are (a) substitution(s). In a pre- _{ferred embodiment, the target position(s) is(are) replaced with/substituted to either an Arg (R) or} a Glu (E). In an embodiment, one or more of the following positions on the surface of the lipase in SEQ ID NO: 3 within 5Å of the positions corresponding to the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 3) are mutated to Glu (E) or (Arg) R: 32, 33, 35, 36, 37, 42,} _{43, 44, 157, 158, 168, 174, 175, 178, 179, 208, 211, 213, 260, 306, 307, 309, 310, 368, 369,} 370, 372, 373, 375, 376, 382, 389, 429, 446, 447, 512, 513, 516, 518, 519, 525, 526, 528, 529, _{531, 532, in particular A32E,R, A33E,R, L35E,R, G36E,R, N37E,R, A42E,R, P43E,R, K44E,R,} G157E,R, A158E,R, F168E,R, Q174E,R, R175E, Q178E,R, K179E,R, G208E,R, D211E,R, V213E,R, R260E, A306E,R, V307E,R, G309E,R, K310E,R, D368E,R, L369E,R, S370E,R, P372E,R, L373E,R, D375E,R, T376E,R, P382E,R, V389E,R, Q429E,R, T446E,R, T447E,R, G512E,R, G513E,R, V516E,R, N518E,R, E519R, K525E,R, Y526E,R, T528E,R, Y529E,R, _{D531E,R, P532E,R in SEQ ID NO: 3.} _{In an embodiment, one or more of the following positions on the surface of the lipase in} SEQ ID NO: 3 within 4Å of the positions corresponding to the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 3) are mutated to Glu (E) or Arg (R): 32, 33, 35, 36, 37, 42,} _{43, 44, 158, 168, 174, 175, 178, 179, 211, 213, 307, 309, 368, 370, 372, 373, 375, 376, 389,} _{429, 447, 513, 516, 518, 519, 525, 528, 529, 531, 532, in particular A32E,R, A33E,R, L35E,R,} G36E,R, N37E,R, A42E,R, P43E,R, K44E,R, A158E,R, F168E,R, Q174E,R, R175E, Q178E,R, K179E,R, D211E,R, V213E,R, V307E,R, G309E,R, D368E,R, L369E,R, S37E,R0, P372E,R, L373E,R, D375E,R, T376E,R, V389E,R, Q429E,R, T447E,R, G513E,R, V516E,R, N518E,R, _{E519R, K525E,R, Y526E,R, T528E,R, Y529E,R, D531E,R, P532E,R in SEQ ID NO: 3.} In an embodiment, one or more of the following positions on the surface of the lipase in _{SEQ ID NO: 3 within 3Å of the positions corresponding to the positions mentioned under item a)} _{above (i.e., mutations in SEQ ID NO: 3) are mutated to Glu (E) or Arg (R): 35, 37, 42, 175, 178,} _{179, 211, 213, 307, 309, 370, 372, 373, 375, 513, 516, 518, 526, 528, 529, 531, in particular} L35E,R, N37E,R, A42E,R, R175E, Q178E,R, K179E,R, D211E,R, V213E,R, V307E,R, G309E,R, S370E,R, P372E,R, L373E,R, D375E,R, G513E,R, V516E,R, N518E,R, Y526E,R, T528E,R, _{Y529E,R, D531E,R in SEQ ID NO: 3.} In an embodiment, one or more of the following positions on the surface of the lipase in _{SEQ ID NO: 3 within 2Å of the positions corresponding to the positions mentioned under item a)} _{above (i.e., mutations in SEQ ID NO: 3) are mutated to Glu (E) or Arg (R): 37, 42, 175, 211, 213,} _{307, 309, 370, 372, 373, 375, 513, 516, 518, 528, 529, 531, in particular N37E,R, A42E,R, R175E,} D211E,R, V213E,R, V307E,R, G309E,R, S370E,R, P372E,R, L373E,R, D375E,R, G513E,R, _{V516E,R, N518E,R, Y526E, T528E,R, Y529E,R, D531E,R in SEQ ID NO: 3.} In an embodiment, the invention relates to variants of a parent lipase of the invention, wherein the variant comprises: a) one or more mutations at positions corresponding to positions: P45, S70, L71, P72, L75, I79, K81, V83, N84, L90, K193, L397, I443, Y529 of SEQ ID NO: 4 wherein position numbering is based on the numbering of SEQ ID NO: 4; b) one or more mutations, in particular to E or R, on the surface of the lipase in SEQ ID NO: 4 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to SEQ ID NO: 4, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 4; and iii) the variant has lipase activity. Said variants comprise one or more mutations corresponding to: P45R, S70E, S70R, L71R, P72E, L75R, L75E, I79R, K81E, K81R, V83R, N84E, L90R, K193E, I443E, Y529E, S70R+P72E+A73V+I79R+K81E+N84E, I79R+K81E+N84E, S70R+A73V+L75E+I79R+K81R+N84E, P72E+A73V+K81E+N84E, K81E+N84E, P72E+A73V+K81R+N84E, P72E+A73V+K81R+N84E+S359G, R437L+I443E of SEQ ID NO: 4, wherein the position numbe- ring is based on the numbering of SEQ ID NO: 4. In a preferred embodiment, the mutation or mutations (is)are (a) substitution(s). In a pre- _{ferred embodiment, the target position(s) is(are) replaced with/substituted to either an Arg (R) or} a Glu (E). In an embodiment, one or more of the following positions on the surface of the lipase in SEQ ID NO: 4 within 5Å of the positions corresponding to the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 4) are mutated to Glu (E) or Arg (R): 8, 32, 43, 44, 46, 47,} 67, 68, 69, 73, 74, 76, 77, 78, 80, 82, 85, 86, 87, 88, 89, 91, 92, 93, 135, 186, 189, 192, 194, 196, _{293, 344, 346, 365, 366, 367, 395, 396, 398, 402, 441, 442, 527, 528, 530, 531, in particular} _{A18E,R, Q32E,R, P43E,R, A44E,R, N46E,R, S47E,R, N67E,R, G68E,R, P69E,R, A73E,R,} _{N74E,R, P76E,R, P77E,R, S78E,R, V80E,R, I82E,R, E85R, T86E,R, F87E,R, G88E,R, L89E,R,} P91E,R, T92E;R, R93E, Y135E,R, L186E,R, R189E, Q192E,R, Y194E,R, S196E,R, F293E,R, _{Q344E,R, S346E,R, Q365E,R, A366E,R, P367E,R, Q395E,R, E396R, G398E,R, K402E,R,} _{L441E,R, P442E,R, L527E,R, A528E,R, P530E,R, L531E,R in SEQ ID NO: 4.} _{In an embodiment, one or more of the following positions on the surface of the lipase in} _{SEQ ID NO: 4 within 4Å of the positions corresponding to the positions mentioned under item a)} _{above (i.e., mutations in SEQ ID NO: 4) are mutated to E or R: 32, 44, 46, 47, 68, 69, 73, 74, 76,} 77, 78, 80, 82, 85, 86, 87, 88, 89, 91, 92, 93, 186, 189, 192, 194, 344, 346, 365, 366, 367, 395, 396, 398, 402, 441, 442, 527, 528, 530, 531, in particular Q32E,R, A44E,R, N46E,R, S47E,R, G68E,R, P69E,R, A73E,R, N74E,R, P76E,R, P77E,R, S78E,R, V80E,R, I82E,R, E85R, T86E,R, F87E,R, G88E,R, L89E,R, P91E,R, T92E,R, R93E, L186E,R, R189E, Q192E,R, Y194E,R, Q344E,R, S346E,R, Q365E,R, A366E,R, P367E,R, Q395E,R, E396R, G398E,R, K402E,R, _{L441E,R, P442E,R, L527E,R, A528E,R, P530E,R, L531E,R in SEQ ID NO: 4.} _{In an embodiment, one or more of the following positions on the surface of the lipase in} SEQ ID NO: 4 within 3Å of the positions corresponding in the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 4) are mutated to Glu (E) or Arg (R): 44, 46, 69, 73, 74, 76,} 78, 80, 82, 85, 87, 88, 89, 91, 189, 192, 194, 344, 396, 398, 442, 528, 530, in particular A44E,R, N46E,R, P69E,R, A73E,R, N74E,R, P76E,R, S78E,R, V80E,R, I82E,R, E85R, F87E,R, G88E,R, L89E,R, P91E,R, R189E,R, Q192E,R, Y194E,R, Q344E,R, E396R, G398E,R, P442E,R, _{A528E,R, P530E,R in SEQ ID NO: 4.} In an embodiment, one or more of the following positions on the surface of the lipase in SEQ ID NO: 4 within 2Å of the positions corresponding in the positions mentioned under item a) _{above (i.e., mutations in SEQ ID NO: 4) are mutated to Glu (E) or Arg (R): 44, 46, 69, 73, 74, 76,} _{78, 80, 82, 85, 89, 91, 192, 194, 396, 398, 442, 528, 530, in particular A44E,R, N46E,R, P69E,R,} A73E,R, N74E,R, P76E,R, S78E,R, V80E,R, I82E,R, E85R, L89E,R, P91E,R, T92E,R, Y194E,R, _{E396R, G398E,R, P442E,R, A528E,R, P530E,R in SEQ ID NO: 4.} In an embodiment, a lipase of the invention or a lipase variant of the invention has at most 10%, preferably at most 5%, at most 4% at most 3%, at most 2%, at most 1% sequence _{differences relative to SEQ ID NOs: 1, 2, 3, and 4, respectively.} _{The lipase variants of the invention have an improved half-life improvement factor (HIF)} compared to the corresponding parent lipase. This is illustrated in the Examples. I_{n an embodiment, a variant of the invention has a TM-score of at least 0.90, e.g., at least} 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least _{0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0, compared to the three-} _{dimensional structure of the parent lipase (i.e., SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 and} _{SEQ ID NO: 4, respectively), wherein the three-dimensional structure is calculated using} AlphaFold. I_{n an embodiment, a variant of the invention has a TM-score of at least 0.95, e.g., at least} 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0, compared to the three-dimensional structure of the parent lipase, (i.e., SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: _{3 and SEQ ID NO: 4, respectively), wherein the three-dimensional structure is calculated using} AlphaFold. I_{n an embodiment, a variant of the invention has a TM-score of at least 0.980, e.g., at least} _{0.985, at least 0.990, at least 0.995, at least 0.999, but less than 1.0, compared to the three-} dimensional structure of the parent lipase (i.e., SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, and _{SEQ ID NO: 4, respectively), wherein the three-dimensional structure is calculated using} AlphaFold. I_{n an embodiment, a variant of the invention has a TM-score of at least 0.990, e.g., at least} 0.991, at least 0.992, at least 0.993, at least 0.994, at least 0.995, at least 0.996, at least 0.997, at least 0.998, at least 0.999, but less than 1.0, compared to the three-dimensional structure of the parent lipase (i.e., SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, and SEQ ID NOL 4, respectively), wherein the three-dimensional structure is calculated using AlphaFold. In an embodiment, the parent lipase is selected from the group consisting of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, or SEQ ID NO:4, respectively. I_{n another embodiment, the parent is SEQ ID NO:1 and the variant has at least 60%, e.g.,} at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%, sequence identity to the polypeptide of SEQ ID NO:1. I_{n another embodiment, the parent is SEQ ID NO:2 and the variant has at least 60%, e.g.,} at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%, sequence identity to the polypeptide of SEQ ID NO:2. I_{n another embodiment, the parent is SEQ ID NO:3 and the variant has at least 60%, e.g.,} at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%, sequence identity to the polypeptide of SEQ ID NO:3. I_{n another embodiment, the parent is SEQ ID NO:4 and the variant has at least 60%, e.g.,} at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%, sequence identity to the polypeptide of SEQ ID NO:4. I_{n one aspect, the number of mutations, especially substitutions, in the variants of the} _{present invention is 1-30, e.g., 1-25, 1-20, 1-15 and 1-10, such as 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11,} _{12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, or 30, substitutions. In a} preferred embodiment, the number of substitutions in the variants of the present invention is 1- _{11, such as 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, or 11 substitutions.} The variants of the invention may further comprise an extension of one or more amino acids at the N-terminal and/or C-terminal ends. Alternatively, the variants of the invention may further comprise a truncation of one or more amino acids at the N-terminal and/or C-terminal ends. F_{urther amino acid changes introduced into parent lipases to provide variants according} to the present invention may be of a minor nature, that is conservative amino acid substitutions or insertions that do not significantly affect the folding and/or activity of the protein; small deletions, _{typically of 1-30 amino acids; small amino- or carboxyl-terminal extensions, such as an amino-} terminal methionine residue; a small linker peptide of up to 20-25 residues; or a small extension that facilitates purification by changing net charge or another function, such as a poly-histidine tract, an antigenic epitope or a binding domain. Examples of conservative substitutions are within the groups of basic amino acids (arginine, lysine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine), and small amino acids (glycine, alanine, serine, threonine and methionine). Amino acid substitutions that do not generally alter specific activity are known in the art and are described, for example, by H. Neurath and R.L. Hill, 1979, In, The Proteins, Academic Press, New York. Common substitutions are Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile, Leu/Val, Ala/Glu, and Asp/Gly. Alternatively, the amino acid changes are of such a nature that the physico-chemical properties of the polypeptides are altered. For example, amino acid changes may improve the thermal stability or storage stability of the lipase. Essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham and _{Wells, 1989, Science 244: 1081-1085). In the latter technique, single alanine mutations are} introduced at every residue in the molecule, and the resultant molecules are tested for lipase activity to identify amino acid residues that are critical to the activity of the molecule. See also, _{Hilton et al., 1996, J. Biol. Chem.271: 4699-4708. The active site of the enzyme or other biological} interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, in conjunction with mutation of putative contact site amino acids. See, for example, de _{Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224: 899-904; Wlodaver} _{et al., 1992, FEBS Lett. 309: 59-64. The identity of essential amino acids can also be inferred} from an alignment with a related polypeptide, and/or be inferred from sequence homology and conserved catalytic machinery with a related polypeptide or within a polypeptide or protein family with polypeptides/proteins descending from a common ancestor, typically having similar three- _{dimensional structures, functions, and significant sequence similarity. Additionally, or alternatively,} protein structure prediction tools can be used for protein structure modelling to identify essential amino acids and/or active sites of polypeptides. See, for example, Jumper et al., 2021, “Highly _{accurate protein structure prediction with AlphaFold”, Nature 596: 583-589.} _{In an embodiment, the lipase variants of the invention have HIF compared to a reference} _{lipase (e.g., SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4) above 1.0. In preferred} _{embodiments, the HIF is improved by at least 5%, e.g., at least 10%, at least 20%, at least 30%,} at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 125%, at least 150%, at least 175%, at least 200%, at least 250%, at least 300%, at least 400%, at least 500%, at least 600%, at least 700%, at least 800%, at least 900%, at least 1000%, or more, compared to the parent. In preferred embodiments, the HIF is above 1.00, above 1.10, in particular above 1.50, above 2.00, above 2.50, above 3.00, above 3.50, above 4.00, above 5.00, above 6.00, above 7.00, above 8.00, above 9.00, above 10.00, above 11.00, above 12.00, above 13.00, above 14.00, above 15.00, above 16.00, above 17.00, above 18.00, above 19,00, above 20.00, above 21.00, above 22.00, above 23.00, above 24.00, above 25.00, above 26.00, above 27.00, above 28.00, above 29.00, above 30.00 such as between 1.00 and 30.00, such as between 2.00 and 25.00, such as between 3.00 and 20.00, such as between 4.00 and 15,00, such as between 5.00 and 10.00. In one embodiment, one or more additional enzymes may be combined with a lipase or lipase variant of the invention. The additional enzyme is selected from the group consisting of amylase (e.g., alpha-amylase), arabinase, carbohydrase, cellulase (e.g., endoglucanase), cutinase, DNase, galactanase, haloperoxygenase, another lipase, mannanase, oxidase (e.g., laccase or peroxidase), pectinase, pectin lyase, protease, xylanase, xanthanase or xyloglucanase. In a preferred embodiment, the companion enzyme is an alpha-amylase. I_{n one embodiment, the lipase variant provides improved HIF at pH 8-14, preferably pH} 9-13, most preferably pH 10-12. Preparation of Lipase Variants The lipase variants of the invention can be prepared using any mutagenesis procedure known in the art, such as site-directed mutagenesis, synthetic gene construction, semi-synthetic gene construction, random mutagenesis, shuffling, etc. S_{ite-directed mutagenesis is a technique in which one or more mutations are introduced} at one or more defined sites in a polynucleotide encoding the parent. S_{ite-directed mutagenesis can be accomplished in vitro by PCR involving the use of} oligonucleotide primers containing the desired mutation. Site-directed mutagenesis can also be _{performed in vitro by cassette mutagenesis involving the cleavage by a restriction enzyme at a} site in the plasmid comprising a polynucleotide encoding the parent and subsequent ligation of _{an oligonucleotide containing the mutation in the polynucleotide. Usually, the restriction enzyme} that digests the plasmid and the oligonucleotide is the same, permitting sticky ends of the plasmid and the insert to ligate to one another. See, e.g., Scherer and Davis, 1979, Proc. Natl. Acad. Sci. _{USA 76: 4949-4955; and Barton et al., 1990, Nucleic Acids Res. 18: 7349-4966.} _{Site-directed mutagenesis can also be accomplished in vivo by methods known in the art.} _{See, e.g., US 2004/0171154; Storici et al., 2001, Nature Biotechnol. 19: 773-776; Kren et al.,} _{1998, Nat. Med. 4: 285-290; and Calissano and Macino, 1996, Fungal Genet. Newslett. 43: 15-} 16. Any site-directed mutagenesis procedure can be used in the present invention. There are many commercial kits available that can be used to prepare variants. S_{ynthetic gene construction entails in vitro synthesis of a designed polynucleotide} molecule to encode a polypeptide of interest. Gene synthesis can be performed utilizing several techniques, such as the multiplex microchip-based technology described by Tian et al., 2004, _{Nature 432: 1050-1054, and similar technologies wherein oligonucleotides are synthesized and} assembled upon photo-programmable microfluidic chips. Single or multiple amino acid substitutions, deletions, and/or insertions can be made and tested using known methods of mutagenesis, recombination, and/or shuffling, followed by a relevant screening procedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988, _{Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156;} _{WO 95/17413; or WO 95/22625. Other methods that can be used include error-prone PCR,} _{phage display (e.g., Lowman et al., 1991, Biochemistry 30: 10832-10837; US 5,223,409;} _{WO 92/06204) and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Ner et} _{al., 1988, DNA 7: 127).} Mutagenesis/shuffling methods can be combined with high-throughput, automated screening methods to detect activity of cloned, mutagenized polypeptides expressed by host cells _{(Ness et al., 1999, Nature Biotechnology 17: 893-896). Mutagenized DNA molecules that encode} active polypeptides can be recovered from the host cells and rapidly sequenced using standard methods in the art. These methods allow the rapid determination of the importance of individual amino acid residues in a polypeptide. Semi-synthetic gene construction is accomplished by combining aspects of synthetic gene construction, and/or site-directed mutagenesis, and/or random mutagenesis, and/or shuffling. Semi-synthetic construction is typified by a process utilizing polynucleotide fragments that are synthesized, in combination with PCR techniques. Defined regions of genes may thus be synthesized de novo, while other regions may be amplified using site-specific mutagenic primers, while yet other regions may be subjected to error-prone PCR or non-error prone PCR amplification. Polynucleotide subsequences may then be shuffled. Polynucleotides The present invention also relates to polynucleotides encoding a lipase or lipase variant _{of the present invention. The polynucleotide may be a genomic DNA, a cDNA, a synthetic DNA,} _{a synthetic RNA, a mRNA, or a combination thereof. In an aspect, the polynucleotide is isolated.} In another aspect, the polynucleotide is purified. Nucleic Acid Constructs The present invention also relates to nucleic acid constructs comprising a polynucleotide encoding a lipase or variant thereof of the present invention. In a preferred embodiment, the invention relates to nucleic acid constructs comprising a polynucleotide encoding a lipase or _{variant thereof operably linked to one or more control sequences that direct the expression of the} coding sequence in a suitable host cell under conditions compatible with the control sequences. The polynucleotide may be manipulated in a variety of ways to provide for expression of _{a lipase or variant thereof. Manipulation of the polynucleotide prior to its insertion into a vector} may be desirable or necessary depending on the expression vector. The techniques for modifying polynucleotides utilizing recombinant DNA methods are well known in the art. Promoters The control sequence may be a promoter, a polynucleotide recognized by a host cell for _{expression of a polynucleotide encoding a lipase or lipase variant of the present invention. The} _{promoter contains transcriptional control sequences that mediate the expression of the lipase or} _{a variant thereof. The promoter may be any polynucleotide that shows transcriptional activity in} the host cell including mutant, truncated, and hybrid promoters, and may be obtained from genes encoding extracellular or intracellular polypeptides either homologous or heterologous to the host cell. Examples of suitable promoters for directing transcription of the polynucleotide of the present invention in a bacterial host cell are described in Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Lab., NY, Davis et al., 2012, Basic Methods in _{Molecular Biology, Elsevier, and Song et al., 2016, PLOS One 11(7): e0158447.} Examples of suitable promoters for directing transcription of the polynucleotide of the present invention in a filamentous fungal host cell are promoters obtained from Aspergillus, _{Fusarium, Rhizomucor and Trichoderma cells, such as the promoters described in Mukherjee et} al., 2013, “Trichoderma: Biology and Applications”, and by Schmoll and Dattenböck, 2016, “Gene Expression Systems in Fungi: Advancements and Applications”, Fungal Biology. For expression in a yeast host, examples of useful promoters are described by Smolke et al., 2018, “Synthetic Biology: Parts, Devices and Applications” (Chapter 6: Constitutive and Regulated Promoters in Yeast: How to Design and Make Use of Promoters in S. cerevisiae), and by Schmoll and Dattenböck, 2016, “Gene Expression Systems in Fungi: Advancements and Applications”, Fungal Biology. Terminators The control sequence may also be a transcription terminator, which is recognized by a host cell to terminate transcription. The terminator is operably linked to the 3’-terminus of the polynucleotide encoding the lipase or lipase variant. Any terminator that is functional in the host cell may be used in the present invention. Preferred terminators for bacterial host cells may be obtained from the genes for Bacillus _{clausii alkaline protease (aprH), Bacillus licheniformis alpha-amylase (amyL), and Escherichia} _{coli ribosomal RNA (rrnB).} Preferred terminators for filamentous fungal host cells may be obtained from Aspergillus _{or Trichoderma species, such as obtained from the genes for Aspergillus niger glucoamylase,} _{Trichoderma reesei beta-glucosidase, Trichoderma reesei cellobiohydrolase I, and Trichoderma} _{reesei endoglucanase I, such as the terminators described in Mukherjee et al., 2013,} “Trichoderma: Biology and Applications”, and by Schmoll and Dattenböck, 2016, “Gene Expression Systems in Fungi: Advancements and Applications”, Fungal Biology. Preferred terminators for yeast host cells may be obtained from the genes for _{Saccharomyces cerevisiae enolase, Saccharomyces cerevisiae cytochrome C (CYC1), and} _{Saccharomyces cerevisiae glyceraldehyde-3-phosphate dehydrogenase. Other useful} _{terminators for yeast host cells are described by Romanos et al., 1992, Yeast 8: 423-488.} mRNA Stabilizers The control sequence may also be an mRNA stabilizer region downstream of a promoter _{and upstream of the coding sequence of a gene which increases expression of the gene.} Examples of suitable mRNA stabilizer regions are obtained from a Bacillus thuringiensis _{cryIIIA gene (WO 94/25612) and a Bacillus subtilis SP82 gene (Hue et al., 1995, J. Bacteriol.177:} 3465-3471). Examples of mRNA stabilizer regions for fungal cells are described in Geisberg et al., _{2014, Cell 156(4): 812-824, and in Morozov et al., 2006, Eukaryotic Cell 5(11): 1838-1846.} Leader Sequences The control sequence may also be a leader, a nontranslated region of an mRNA that is important for translation by the host cell. The leader is operably linked to the 5’-terminus of the _{polynucleotide encoding the lipase or lipase variant of the invention. Any leader that is functional} in the host cell may be used. Suitable leaders for bacterial host cells are described by Hambraeus et al., 2000, _{Microbiology 146(12): 3051-3059, and by Kaberdin and Bläsi, 2006, FEMS Microbiol. Rev.30(6):} 967-979. Preferred leaders for filamentous fungal host cells may be obtained from the genes for _{Aspergillus oryzae TAKA amylase and Aspergillus nidulans triose phosphate isomerase.} Suitable leaders for yeast host cells may be obtained from the genes for Saccharomyces _{cerevisiae enolase (ENO-1), Saccharomyces cerevisiae 3-phosphoglycerate kinase,} _{Saccharomyces cerevisiae alpha-factor, and Saccharomyces cerevisiae alcohol} dehydrogenase/glyceraldehyde-3-phosphate dehydrogenase (ADH2/GAP). Polyadenylation Sequences The control sequence may also be a polyadenylation sequence, a sequence operably linked to the 3’-terminus of the polynucleotide and, when transcribed, is recognized by the host cell as a signal to add polyadenosine residues to transcribed mRNA. Any polyadenylation sequence that is functional in the host cell may be used. Preferred polyadenylation sequences for filamentous fungal host cells are obtained from _{the genes for Aspergillus nidulans anthranilate synthase, Aspergillus niger glucoamylase,} _{Aspergillus niger alpha-glucosidase, Aspergillus oryzae TAKA amylase, and Fusarium} _{oxysporum trypsin-like protease.} Useful polyadenylation sequences for yeast host cells are described by Guo and Sherman, _{1995, Mol. Cellular Biol.15: 5983-5990.} Signal Peptides The control sequence may also be a signal peptide coding region that encodes a signal peptide linked to the N-terminus of a lipase or lipase variant and directs the lipase or variant thereof into the cell’s secretory pathway. The 5’-end of the coding sequence of the polynucleotide may inherently contain a signal peptide coding sequence naturally linked in translation reading _{frame with the segment of the coding sequence that encodes the lipase or lipase variant of the} invention. Alternatively, the 5’-end of the coding sequence may contain a signal peptide coding sequence that is foreign to the coding sequence. A foreign signal peptide coding sequence may be required where the coding sequence does not naturally contain a signal peptide coding sequence. Alternatively, a foreign signal peptide coding sequence may simply replace the natural _{signal peptide coding sequence in order to enhance secretion of the lipase or variant of the} invention. However, any signal peptide coding sequence that directs the expressed lipase or variant thereof into the secretory pathway of a host cell may be used. Effective signal peptide coding sequences for filamentous fungal host cells are the signal _{peptide coding sequences obtained from the genes for Aspergillus niger neutral amylase,} _{Aspergillus niger glucoamylase, Aspergillus oryzae TAKA amylase, Humicola insolens cellulase,} _{Humicola insolens endoglucanase V, Humicola lanuginosa lipase, and Rhizomucor miehei} _{aspartic proteinase, such as the signal peptide described by Xu et al., 2018, Biotechnology Letters} 40: 949-955 Useful signal peptides for yeast host cells are obtained from the genes for Saccharomyces _{cerevisiae alpha-factor and Saccharomyces cerevisiae invertase. Other useful signal peptide} coding sequences are described by Romanos et al., 1992, supra. Propeptides The control sequence may also be a propeptide coding sequence that encodes a _{propeptide positioned at the N-terminus of a lipase or lipase variant of the invention. The resultant} polypeptide is known as a proenzyme or propolypeptide (or a zymogen in some cases). A propolypeptide is generally inactive and can be converted to an active lipase or lipase variant of the invention by catalytic or autocatalytic cleavage of the propeptide from the propolypeptide. The _{propeptide coding sequence may be obtained from the genes for Bacillus subtilis alkaline} _{protease (aprE), Bacillus subtilis neutral protease (nprT), Myceliophthora thermophila laccase} _{(WO 95/33836), Rhizomucor miehei aspartic proteinase, and Saccharomyces cerevisiae alpha-} factor. Where both signal peptide and propeptide sequences are present, the propeptide sequence is positioned next to the N-terminus of said lipase or variant thereof and the signal peptide sequence is positioned next to the N-terminus of the propeptide sequence. Regulatory Sequences I_{t may also be desirable to add regulatory sequences that regulate expression of the lipase} or lipase variant of the invention relative to the growth of the host cell. Examples of regulatory sequences are those that cause expression of the gene to be turned on or off in response to a chemical or physical stimulus, including the presence of a regulatory compound. Regulatory _{sequences in prokaryotic systems include the lac, tac, and trp operator systems. In yeast, the} ADH2 system or GAL1 system may be used. In filamentous fungi, the Aspergillus niger _{glucoamylase promoter, Aspergillus oryzae TAKA alpha-amylase promoter, and Aspergillus} _{oryzae glucoamylase promoter, Trichoderma reesei cellobiohydrolase I promoter, and} _{Trichoderma reesei cellobiohydrolase II promoter may be used. Other examples of regulatory} sequences are those that allow for gene amplification. In eukaryotic systems, these regulatory sequences include the dihydrofolate reductase gene that is amplified in the presence of methotrexate, and the metallothionein genes that are amplified with heavy metals. Transcription Factors The control sequence may also be a transcription factor, a polynucleotide encoding a polynucleotide-specific DNA-binding polypeptide that controls the rate of the transcription of _{genetic information from DNA to mRNA by binding to a specific polynucleotide sequence. The} transcription factor may function alone and/or together with one or more other polypeptides or transcription factors in a complex by promoting or blocking the recruitment of RNA polymerase. _{Transcription factors are characterized by comprising at least one DNA-binding domain which} often attaches to a specific DNA sequence adjacent to the genetic elements which are regulated by the transcription factor. The transcription factor may regulate the expression of a protein of interest either directly, i.e., by activating the transcription of the gene encoding the protein of interest by binding to its promoter, or indirectly, i.e., by activating the transcription of a further transcription factor which regulates the transcription of the gene encoding the protein of interest, such as by binding to the promoter of the further transcription factor. Suitable transcription factors for fungal host cells are described in WO 2017/144177. Suitable transcription factors for _{prokaryotic host cells are described in Seshasayee et al., 2011, Subcellular Biochemistry 52: 7-} _{23, as well in Balleza et al., 2009, FEMS Microbiol. Rev.33(1): 133-151.} Expression Vectors The present invention also relates to recombinant expression vectors comprising a polynucleotide encoding a lipase or lipase variant of the present invention. In a preferred embodiment, the invention relates to recombinant expression vectors comprising a polynucleotide encoding a lipase or lipase variant of the present invention, a promoter, and transcriptional and translational stop signals. The various nucleotide and control sequences may be joined together to produce a recombinant expression vector that may include one or more convenient restriction sites to allow for insertion or substitution of the polynucleotide encoding the lipase or lipase variant of the invention at such sites. Alternatively, the polynucleotide may be expressed by inserting the polynucleotide or a nucleic acid construct comprising the polynucleotide into an appropriate vector _{for expression. In creating the expression vector, the coding sequence is located in the vector so} that the coding sequence is operably linked with the appropriate control sequences for expression. The recombinant expression vector may be any vector (e.g., a plasmid or virus) that can be conveniently subjected to recombinant DNA procedures and can bring about expression of the polynucleotide. The choice of the vector will typically depend on the compatibility of the vector with the host cell into which the vector is to be introduced. The vector may be a linear or closed circular plasmid. The vector may be an autonomously replicating vector, i.e., a vector that exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g., a plasmid, an extrachromosomal element, a minichromosome, or an artificial chromosome. The vector may contain any means for assuring self-replication. Alternatively, the vector may be one that, when introduced into the host cell, is integrated into the genome and replicated together with the chromosome(s) into which it has been integrated. Furthermore, a single vector or plasmid or two or more vectors or plasmids that together contain the total DNA to be introduced into the genome of the host cell, or a transposon, may be used. The vector preferably contains one or more selectable markers that permit easy selection of transformed, transfected, transduced, or the like cells. A selectable marker is a gene the product of which provides for biocide or viral resistance, resistance to heavy metals, prototrophy to auxotrophs, and the like. The vector preferably contains at least one element that permits integration of the vector into the host cell's genome or autonomous replication of the vector in the cell independent of the genome. For integration into the host cell genome, the vector may rely on the polynucleotide’s sequence encoding the polypeptide or any other element of the vector for integration into the genome by homologous recombination, such as homology-directed repair (HDR), or non- homologous recombination, such as non-homologous end-joining (NHEJ). For autonomous replication, the vector may further comprise an origin of replication enabling the vector to replicate autonomously in the host cell in question. The origin of replication may be any plasmid replicator mediating autonomous replication that functions in a cell. The term “origin of replication” or “plasmid replicator” means a polynucleotide that enables a plasmid or vector to replicate in vivo. More than one copy of a polynucleotide of the present invention may be inserted into a host cell to increase production of a polypeptide. For example, 2 or 3 or 4 or 5 or more copies are inserted into a host cell. An increase in the copy number of the polynucleotide can be obtained by integrating at least one additional copy of the sequence into the host cell genome or by including an amplifiable selectable marker gene with the polynucleotide where cells containing amplified copies of the selectable marker gene, and thereby additional copies of the polynucleotide, can be selected for by cultivating the cells in the presence of the appropriate selectable agent. Host Cells The present invention also relates to recombinant host cells comprising a polynucleotide of the present invention. In a preferred embodiment, the invention relates to recombinant host _{cells comprising a polynucleotide of the present invention operably linked to one or more control} sequences that direct the production of a lipase or variant thereof of the present invention. A construct or vector comprising a polynucleotide is introduced into a host cell so that the construct or vector is maintained as a chromosomal integrant or as a self-replicating extra- _{chromosomal vector as described earlier. The choice of a host cell will to a large extent depend} _{upon the gene encoding the lipase or variant thereof and its source. The recombinant host cell} may comprise a single copy, or at least two copies, e.g., three, four, five, or more copies of the polynucleotide of the present invention. The host cell may be any cell useful in the recombinant production of a lipase or lipase variant of the invention, e.g., a prokaryotic cell or a fungal cell. The host cell may be any microbial cell useful in the recombinant production of a polypeptide of the present invention, e.g., a prokaryotic cell or a fungal cell. The prokaryotic host cell may be any Gram-positive or Gram-negative bacterium. Gram- positive bacteria include, but are not limited to, Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, and Streptomyces. Gram-negative bacteria include, but are not limited to, Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma. T_{he bacterial host cell may be any Bacillus cell including, but not limited to, Bacillus} alkalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus stearothermophilus, Bacillus subtilis, and Bacillus _{thuringiensis cells. In an embodiment, the Bacillus cell is a Bacillus amyloliquefaciens, Bacillus} _{licheniformis and Bacillus subtilis cell.} _{For purposes of this invention, Bacillus classes/genera/species shall be defined as} _{described in Patel and Gupta, 2020, Int. J. Syst. Evol. Microbiol.70: 406-438.} _{The bacterial host cell may also be any Streptococcus cell including, but not limited to,} Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis, and Streptococcus _{equi subsp. Zooepidemicus cells.} _{The bacterial host cell may also be any Streptomyces cell including, but not limited to,} _{Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces} _{griseus, and Streptomyces lividans cells.} Methods for introducing DNA into prokaryotic host cells are well-known in the art, and any suitable method can be used including but not limited to protoplast transformation, competent cell transformation, electroporation, conjugation, transduction, with DNA introduced as linearized or as circular polynucleotide. Persons skilled in the art will be readily able to identify a suitable method for introducing DNA into a given prokaryotic cell depending, e.g., on the genus. Methods _{for introducing DNA into prokaryotic host cells are for example described in Heinze et al., 2018,} _{BMC Microbiology 18:56, Burke et al., 2001, Proc. Natl. Acad. Sci. USA 98: 6289-6294, Choi et} _{al., 2006, J. Microbiol. Methods 64: 391-397, and Donald et al., 2013, J. Bacteriol.195(11): 2612-} 2620. The host cell may be a fungal cell. “Fungi” as used herein includes the phyla Ascomycota, Basidiomycota, Chytridiomycota, and Zygomycota as well as the Oomycota and all mitosporic fungi (as defined by Hawksworth et al., In, Ainsworth and Bisby’s Dictionary of The Fungi, 8th edition, 1995, CAB International, University Press, Cambridge, UK). Fungal cells may be transformed by a process involving protoplast-mediated transformation, Agrobacterium-mediated transformation, electroporation, biolistic method and _{shock-wave-mediated transformation as reviewed by Li et al., 2017, Microbial Cell Factories 16:} _{168 and procedures described in EP 238023, Yelton et al., 1984, Proc. Natl. Acad. Sci. USA 81:} 1470-1474, Christensen et al., 1988, Bio/Technology 6: 1419-1422, and Lubertozzi and Keasling, _{2009, Biotechn. Advances 27: 53-75. However, any method known in the art for introducing DNA} into a fungal host cell can be used, and the DNA can be introduced as linearized or as circular polynucleotide. The fungal host cell may be a yeast cell. “Yeast” as used herein includes ascosporogenous yeast (Endomycetales), basidiosporogenous yeast, and yeast belonging to the Fungi Imperfecti (Blastomycetes). Since the classification of yeast may change in the future, for the purposes of this invention, yeast shall be defined as described in Biology and Activities of _{Yeast (Skinner, Passmore, and Davenport, editors, Soc. App. Bacteriol. Symposium Series No.} 9, 1980). The yeast host cell may be a Candida, Hansenula, Kluyveromyces, Pichia, _{Saccharomyces, Schizosaccharomyces, or Yarrowia cell, such as a Kluyveromyces lactis,} Saccharomyces carlsbergensis, Saccharomyces cerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii, Saccharomyces kluyveri, Saccharomyces norbensis, Saccharomyces _{oviformis, or Yarrowia lipolytica cell. In a preferred embodiment, the yeast host cell is a Pichia or} _{Komagataella cell, e.g., a Pichia pastoris cell (Komagataella phaffii).} The fungal host cell may be a filamentous fungal cell. “Filamentous fungi” include all filamentous forms of the subdivision Eumycota and Oomycota (as defined by Hawksworth et al., 1995, supra). The filamentous fungi are generally characterized by a mycelial wall composed of chitin, cellulose, glucan, chitosan, mannan, and other complex polysaccharides. Vegetative growth is by hyphal elongation and carbon catabolism is obligately aerobic. In contrast, vegetative _{growth by yeasts such as Saccharomyces cerevisiae is by budding of a unicellular thallus and} carbon catabolism may be fermentative. The filamentous fungal host cell may be an Acremonium, Aspergillus, Aureobasidium, Bjerkandera, Ceriporiopsis, Chrysosporium, Coprinus, Coriolus, Cryptococcus, Filibasidium, Fusarium, Humicola, Magnaporthe, Mucor, Myceliophthora, Neocallimastix, Neurospora, Paecilomyces, Penicillium, Phanerochaete, Phlebia, Piromyces, Pleurotus, Schizophyllum, _{Talaromyces, Thermoascus, Thielavia, Tolypocladium, Trametes, or Trichoderma cell. In a} _{preferred embodiment, the filamentous fungal host cell is an Aspergillus, Trichoderma or} _{Fusarium cell. In a further preferred embodiment, the filamentous fungal host cell is an Aspergillus} _{niger, Aspergillus oryzae, Trichoderma reesei, or Fusarium venenatum cell.} For example, the filamentous fungal host cell may be an Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae, Bjerkandera adusta, Ceriporiopsis aneirina, Ceriporiopsis caregiea, _{Ceriporiopsis gilvescens, Ceriporiopsis pannocinta, Ceriporiopsis rivulosa, Ceriporiopsis subrufa,} Ceriporiopsis subvermispora, Chrysosporium inops, Chrysosporium keratinophilum, Chrysosporium lucknowense, Chrysosporium merdarium, Chrysosporium pannicola, Chrysosporium queenslandicum, Chrysosporium tropicum, Chrysosporium zonatum, Coprinus cinereus, Coriolus hirsutus, Fusarium bactridioides, Fusarium cerealis, Fusarium crookwellense, Fusarium culmorum, Fusarium graminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negundi, Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusarium sambucinum, Fusarium sarcochroum, Fusarium sporotrichioides, Fusarium sulphureum, Fusarium torulosum, Fusarium trichothecioides, Fusarium venenatum, Humicola insolens, Humicola lanuginosa, Mucor miehei, Myceliophthora thermophila, Neurospora crassa, Penicillium purpurogenum, Phanerochaete chrysosporium, Phlebia radiata, Pleurotus eryngii, Talaromyces emersonii, Thielavia terrestris, Trametes villosa, Trametes versicolor, Trichoderma harzianum, Trichoderma koningii, Trichoderma longibrachiatum, Trichoderma reesei, or Trichoderma viride cell. I_{n an aspect, the host cell is isolated. In another aspect, the host cell is purified.} Methods of Production I_{n an aspect, the present invention relates to methods of producing or obtaining lipases or} _{lipase variants of the invention.} _{In an embodiment, the invention relates to methods for obtaining a lipase variant according} to the invention, comprising: (_{a) introducing into a parent lipase according to the invention, one or more mutations at} _{positions defined in the appended claims and optionally further introducing mutations at at least} one, two, three, e.g., at least four, at least five, at least six, at least seven, at least eight, or nine positions; and (b) recovering the lipase variant. In an embodiment, the present invention relates to methods of producing a lipase or variant thereof of the present invention, comprising: (a) cultivating a recombinant host cell of the present invention under conditions conducive _{for production of the lipase or lipase variant of the invention; and optionally} _{(b) recovering the lipase or variant thereof.} The host cell is cultivated in a nutrient medium suitable for production of the lipase and lipase variant using methods known in the art. For example, the cells may be cultivated by shake flask cultivation, or small-scale or large-scale fermentation (including continuous, batch, fed-batch, or solid state fermentations) in laboratory or industrial fermentors in a suitable medium and under _{conditions allowing the lipase or variant thereof to be expressed and/or isolated. Suitable media} are available from commercial suppliers or may be prepared according to published compositions (e.g., in catalogues of the American Type Culture Collection). If the lipase or variant of the invention is secreted into the nutrient medium, the lipase or variant can be recovered directly from the medium. If the lipase or variant is not secreted, it can be recovered from cell lysates. The lipase or variant thereof of the invention may be detected using methods known in the art that are specific, including, but not limited to, the use of specific antibodies, formation of an enzyme product, disappearance of an enzyme substrate, or an enzyme assay determining the _{relative or specific activity of the lipase or variant thereof.} The lipase or variant thereof may be recovered from the medium using methods known in the art, including, but not limited to, collection, centrifugation, filtration, extraction, spray-drying, evaporation, or precipitation. In one aspect, the whole fermentation broth is recovered. In another aspect, a cell-free fermentation broth comprising the polypeptide is recovered. The lipase or variant thereof may be purified by a variety of procedures known in the art to obtain substantially pure lipase or variants and/or fragments (see, e.g., Wingfield, 2015, Current Protocols in Protein Science; 80(1): 6.1.1-6.1.35; Labrou, 2014, Protein Downstream Processing, 1129: 3-10). In an alternative aspect, the lipase or variant thereof is not recovered. Granules The present invention also relates to enzyme granules/particles comprising a lipase or lipase variant of the invention. In an embodiment, the granule comprises a core, and optionally one or more coatings (outer layers) surrounding the core. The core may have a diameter, measured as equivalent spherical diameter (volume based average particle size), of 20-2000 µm, particularly 50-1500 µm, 100-1500 µm or 250-1200 µm. The core diameter, measured as equivalent spherical diameter, can be determined using laser diffraction, such as using a Malvern Mastersizer and/or the method described under ISO13320 (2020). In an embodiment, the core comprises a lipase or variant thereof of the present invention. The core may include additional materials such as fillers, fiber materials (cellulose or synthetic fibers), stabilizing agents, solubilizing agents, suspension agents, viscosity regulating agents, light spheres, plasticizers, salts, lubricants and fragrances. The core may include a binder, such as synthetic polymer, wax, fat, or carbohydrate. The core may include a salt of a multivalent cation, a reducing agent, an antioxidant, a peroxide decomposing catalyst and/or an acidic buffer component, typically as a homogenous blend. The core may include an inert particle with the lipase or variant thereof absorbed into it, or applied onto the surface, e.g., by fluid bed coating. The core may have a diameter of 20-2000 µm, particularly 50-1500 µm, 100-1500 µm or 250-1200 µm. The core may be surrounded by at least one coating, e.g., to improve the storage stability, to reduce dust formation during handling, or for coloring the granule. The optional coating(s) may include a salt coating, or other suitable coating materials, such as polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA). The coating may be applied in an amount of at least 0.1% by weight of the core, e.g., at least 0.5%, at least 1%, at least 5%, at least 10%, or at least 15%. The amount may be at most 100%, 70%, 50%, 40% or 30%. The coating is preferably at least 0.1 µm thick, particularly at least 0.5 µm, at least 1 µm or at least 5 µm. In some embodiments, the thickness of the coating is below 100 µm, such as below 60 µm, or below 40 µm. The coating should encapsulate the core unit by forming a substantially continuous layer. A substantially continuous layer is to be understood as a coating having few or no holes, so that _{the core unit has few or no uncoated areas. The layer or coating should, in particular, be} homogeneous in thickness. The coating can further contain other materials as known in the art, e.g., fillers, antisticking agents, pigments, dyes, plasticizers and/or binders, such as titanium dioxide, kaolin, calcium carbonate or talc. A salt coating may comprise at least 60% by weight of a salt, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% by weight. To provide acceptable protection, the salt coating is preferably at least 0.1 µm thick, e.g., at least 0.5 µm, at least 1 µm, at least 2 µm, at least 4 µm, at least 5 µm, or at least 8 µm. In a particular embodiment, the thickness of the salt coating is below 100 µm, such as below 60 µm, or below 40 µm. The salt may be added from a salt solution where the salt is completely dissolved or from a salt suspension wherein the fine particles are less than 50 µm, such as less than 10 µm or less than 5 μm. The salt coating may comprise a single salt or a mixture of two or more salts. The salt may be water soluble, in particular, having a solubility at least 0.1 g in 100 g of water at 20°C, preferably at least 0.5 g per 100 g water, e.g., at least 1 g per 100 g water, e.g., at least 5 g per 100 g water. The salt may be an inorganic salt, e.g., salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids (less than 10 carbon atoms, e.g., 6 or less carbon atoms) such as citrate, malonate or acetate. Examples of cations in these salts are alkali or earth alkali metal ions, the ammonium ion or metal ions of the first transition series, such as sodium, potassium, magnesium, calcium, zinc or aluminum. Examples of anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, monobasic phosphate, dibasic phosphate, hypophosphite, dihydrogen pyrophosphate, tetraborate, borate, carbonate, bicarbonate, metasilicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, _{butyrate, propionate, benzoate, tartrate, ascorbate or gluconate. In particular, alkali- or earth alkali} metal salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids such as citrate, malonate or acetate may be used. The salt in the coating may have a constant humidity at 20°C above 60%, particularly above 70%, above 80% or above 85%, or it may be another hydrate form of such a salt (e.g., anhydrate). The salt coating may be as described in WO 00/01793 or WO 2006/034710. Specific examples of suitable salts are NaCl (CH_20°C=76%), Na₂CO₃ (CH_20°C=92%), NaNO3 (CH20°C=73%), Na2HPO4 (CH20°C=95%), Na3PO4 (CH25°C=92%), NH4Cl (CH20°C = 79.5%), (NH4)2HPO4 (CH20°C = 93,0%), NH4H2PO4 (CH20°C = 93.1%), (NH4)2SO4 (CH20°C=81.1%), KCl (CH20°C=85%), K2HPO4 (CH20°C=92%), KH2PO4 (CH20°C=96.5%), KNO3 (CH20°C=93.5%), Na2SO4 (CH20°C=93%), K2SO4 (CH20°C=98%), KHSO4 (CH20°C=86%), MgSO4 (CH20°C=90%), ZnSO4 (CH20°C=90%) and sodium citrate (CH25°C=86%). Other examples include NaH2PO4, (NH4)H2PO4, CuSO4, Mg(NO3)2 and magnesium acetate. The salt may be in anhydrous form, or it may be a hydrated salt, i.e., a crystalline salt hydrate with bound water(s) of crystallization, such as described in WO 99/32595. Specific examples include anhydrous sodium sulfate (Na2SO4), anhydrous magnesium sulfate (MgSO4), magnesium sulfate heptahydrate (MgSO4^.7H2O), zinc sulfate heptahydrate (ZnSO4^.7H2O), sodium phosphate dibasic heptahydrate (Na2HPO4^.7H2O), magnesium nitrate hexahydrate (Mg(NO3)2(6H2O)), sodium citrate dihydrate and magnesium acetate tetrahydrate. Preferably the salt is applied as a solution of the salt, e.g., using a fluid bed. The coating materials can be waxy coating materials and film-forming coating materials. Examples of waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- _{and di- and triglycerides of fatty acids. Examples of film-forming coating materials suitable for} application by fluid bed techniques are given in GB 1483591. T_{he granules may optionally have one or more additional coatings. Examples of suitable} coating materials are polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and _{polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are described in} WO 93/07263 and WO 97/23606. The core can be prepared by granulating a blend of the ingredients, e.g., by a method comprising granulation techniques such as crystallization, precipitation, pan-coating, fluid bed coating, fluid bed agglomeration, rotary atomization, extrusion, prilling, spheronization, size reduction methods, drum granulation, and/or high shear granulation. Methods for preparing the core can be found in the Handbook of Powder Technology; _{Particle size enlargement by C. E. Capes; Vol. 1; 1980; Elsevier. Preparation methods include} known feed and granule formulation technologies, e.g., (a) Spray dried products, wherein a liquid enzyme-containing solution is atomized in a spray drying tower to form small droplets which during their way down the drying tower dry to form _{an enzyme-containing particulate material. Very small particles can be produced this way} (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; Vol. 71; _{pages 140-142; Marcel Dekker).} (b) Layered products, wherein the enzyme is coated as a layer around a pre-formed inert core particle, wherein an enzyme-containing solution is atomized, typically in a fluid bed apparatus wherein the pre-formed core particles are fluidized, and the enzyme-containing solution adheres to the core particles and dries up to leave a layer of dry enzyme on the surface of the core particle. Particles of a desired size can be obtained this way if a useful core particle of the desired size can be found. This type of product is described in, e.g., WO 97/23606. (c) Absorbed core particles, wherein rather than coating the lipase or lipase variant as a layer around the core, the enzyme is absorbed onto and/or into the surface of the core. Such a process is described in WO 97/39116. (d) Extrusion or pelletized products, wherein a lipase or lipase variant-containing paste is pressed to pellets or under pressure is extruded through a small opening and cut into particles which are subsequently dried. Such particles usually have a considerable size because of the material in which the extrusion opening is made (usually a plate with bore holes) sets a limit on the allowable pressure drop over the extrusion opening. Also, very high extrusion pressures when using a small opening increase heat generation in the enzyme paste, which is harmful to the enzyme (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; Vol. 71; pages 140-142; Marcel Dekker). (e) Prilled products, wherein a lipase or variant-containing powder is suspended in molten wax and the suspension is sprayed, e.g., through a rotating disk atomizer, into a cooling chamber where the droplets quickly solidify (Michael S. Showell (editor); Powdered detergents; Surfactant _{Science Series; 1998; Vol. 71; pages 140-142; Marcel Dekker). The product obtained is one} wherein the lipase or variant thereof is uniformly distributed throughout an inert material instead of being concentrated on its surface. US 4,016,040 and US 4,713,245 describe this technique. (_{f) Mixer granulation products, wherein a lipase or variant-containing liquid is added to a} dry powder composition of conventional granulating components. The liquid and the powder in a suitable proportion are mixed and as the moisture of the liquid is absorbed in the dry powder, the components of the dry powder will start to adhere and agglomerate and particles will build up, forming granulates comprising the enzyme. Such a process is described in US 4,106,991, EP 170360, EP 304332, EP 304331, WO 90/09440 and WO 90/09428. In a particular aspect of this process, various high-shear mixers can be used as granulators. Granulates consisting of lipase or lipase variant, fillers and binders etc. are mixed with cellulose fibers to reinforce the particles to produce a so-called T-granulate. Reinforced particles are more robust and release less enzymatic dust. (g) Size reduction, wherein the cores are produced by milling or crushing of larger particles, pellets, tablets, briquettes etc. containing the enzyme. The wanted core particle fraction is obtained by sieving the milled or crushed product. Over and undersized particles can be recycled. Size reduction is described in Martin Rhodes (editor); Principles of Powder Technology; 1990; Chapter 10; John Wiley & Sons. (h) Fluid bed granulation. Fluid bed granulation involves suspending particulates in an air stream and spraying a liquid onto the fluidized particles via nozzles. Particles hit by spray droplets _{get wetted and become tacky. The tacky particles collide with other particles and adhere to them} to form a granule. (i) The cores may be subjected to drying, such as in a fluid bed drier. Other known methods for drying granules in the feed or enzyme industry can be used by the skilled person. The drying _{preferably takes place at a product temperature of from 25 to 90°C. For some enzymes, it is} _{important the cores comprising the lipase or variant thereof contain a low amount of water before} coating with the salt. If water sensitive enzymes are coated with a salt before excessive water is removed, the excessive water will be trapped within the core and may affect the activity of the _{enzyme negatively. After drying, the cores preferably contain 0.1-10% w/w water.} Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 and US 4,661,452 and may optionally be coated by methods known in the art. The granulate may further comprise one or more additional enzymes. Each enzyme will then be present in more granules securing a more uniform distribution of the enzymes, and also reduces the physical segregation of different enzymes due to different particle sizes. Methods for producing multi-enzyme co-granulates is disclosed in the ip.com disclosure IPCOM000200739D. Another example of formulation of enzymes by the use of co-granulates is disclosed in WO 2013/188331. The present invention also relates to protected enzymes prepared according to the method disclosed in EP 238216. In an embodiment, the granule further comprises one or more additional enzymes, e.g., hydrolase, isomerase, ligase, lyase, oxidoreductase, and transferase. The one or more additional enzymes are preferably selected from the group consisting of acetylxylan esterase, acylglycerol lipase, amylase, alpha-amylase, beta-amylase, arabinofuranosidase, cellobiohydrolases, cellulase, feruloyl esterase, galactanase, alpha-galactosidase, beta-galactosidase, beta- glucanase, beta-glucosidase, lysophospholipase, lysozyme, alpha-mannosidase, beta- mannosidase (mannanase), phytase, phospholipase A1, phospholipase A2, phospholipase D, protease, pullulanase, pectin esterase, triacylglycerol lipase, xylanase, beta-xylosidase or any combination thereof. Liquid Formulations The present invention also relates to liquid compositions comprising a lipase or lipase variant of the invention. The composition may comprise an enzyme stabilizer (examples of which include polyols such as propylene glycol or glycerol, sugar or sugar alcohol, lactic acid, reversible _{protease inhibitor, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl} boronic acid derivative such as 4-formylphenyl boronic acid). In some embodiments, filler(s) or carrier material(s) are included to increase the volume of such compositions. Suitable filler or carrier materials include, but are not limited to, various _{salts of sulfate, carbonate and silicate as well as talc, clay and the like. Suitable filler or carrier} materials for liquid compositions include, but are not limited to, water or low molecular weight primary and secondary alcohols including polyols and diols. Examples of such alcohols include, but are not limited to, methanol, ethanol, propanol and isopropanol. In some embodiments, the compositions contain from about 5% to about 90% of such materials. In an aspect, the liquid formulation comprises 20-80% w/w of polyol. In one embodiment, the liquid formulation comprises 0.001-2% w/w preservative. In another embodiment, the invention relates to liquid formulations comprising: (_{A) 0.001-25% w/w of a lipase or lipase variant of the present invention;} _{(B) 20-80% w/w of polyol;} _{(C) optionally 0.001-2% w/w preservative; and} _{(D) water.} In another embodiment, the invention relates to liquid formulations comprising: (_{A) 0.001-25% w/w of a lipase or lipase variant of the present invention;} _{(B) 0.001-2% w/w preservative;} _{(C) optionally 20-80% w/w of polyol; and} _{(D) water.} In another embodiment, the liquid formulation comprises one or more formulating agents, such as a formulating agent selected from the group consisting of polyol, sodium chloride, sodium benzoate, potassium sorbate, sodium sulphate, potassium sulphate, magnesium sulphate, sodium thiosulfate, calcium carbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol, lactose, starch, PVA, acetate and phosphate, preferably selected from the group consisting of sodium sulphate, dextrin, cellulose, sodium thiosulfate, kaolin and calcium carbonate. In one embodiment, the polyols is selected from the group consisting of glycerol, sorbitol, propylene glycol (MPG), ethylene glycol, diethylene glycol, triethylene glycol, 1,2-propylene glycol or 1,3-propylene glycol, dipropylene glycol, polyethylene glycol (PEG) having an average molecular weight below about 600 and polypropylene glycol (PPG) having an average molecular weight below about 600, more preferably selected from the group consisting of glycerol, sorbitol and propylene glycol (MPG) or any combination thereof. In another embodiment, the liquid formulation comprises 20-80% polyol (i.e., total amount of polyol), e.g., 25-75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% polyol. In one embodiment, the liquid formulation comprises 20-80% polyol, e.g., 25-75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% polyol, wherein the polyol is selected from the group consisting of glycerol, sorbitol, propylene glycol (MPG), ethylene glycol, diethylene glycol, triethylene glycol, 1,2-propylene glycol or 1,3-propylene glycol, dipropylene glycol, polyethylene glycol (PEG) having an average molecular weight below about 600 and polypropylene glycol (PPG) having an average molecular weight below about 600. In one embodiment, the liquid formulation comprises 20-80% polyol (i.e., total amount of polyol), e.g., 25-75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% _{polyol, wherein the polyol is selected from the group consisting of glycerol, sorbitol, and propylene} glycol (MPG). In another embodiment, the preservative is selected from the group consisting of sodium sorbate, potassium sorbate, sodium benzoate and potassium benzoate or any combination thereof. In one embodiment, the liquid formulation comprises 0.02-1.5% w/w preservative, e.g., 0.05-1% w/w preservative or 0.1-0.5% w/w preservative. In one embodiment, the liquid formulation comprises 0.001-2% w/w preservative (i.e., total amount of preservative), e.g., 0.02- 1.5% w/w preservative, 0.05-1% w/w preservative, or 0.1-0.5% w/w preservative, wherein the preservative is selected from the group consisting of sodium sorbate, potassium sorbate, sodium benzoate and potassium benzoate or any combination thereof. In another embodiment, the liquid formulation further comprises one or more additional enzymes, e.g., hydrolase, isomerase, ligase, lyase, oxidoreductase, and transferase. The one or more additional enzymes are preferably selected from the group consisting of acetylxylan esterase, acylglycerol lipase, amylase, alpha-amylase, beta-amylase, arabinofuranosidase, cellobiohydrolases, cellulase, feruloyl esterase, galactanase, alpha-galactosidase, beta- galactosidase, beta-glucanase, beta-glucosidase, lysophospholipase, lysozyme, alpha- mannosidase, beta-mannosidase (mannanase), phytase, phospholipase A1, phospholipase A2, phospholipase D, protease, pullulanase, pectin esterase, triacylglycerol lipase, xylanase, beta- xylosidase or any combination thereof. Fermentation Broth Formulations or Cell Compositions The present invention also relates to a fermentation broth formulation or a cell composition comprising a lipase or variant thereof of the present invention. The fermentation broth formulation or the cell composition further comprises additional ingredients used in the fermentation process, _{such as, for example, cells (including, the host cells containing the gene encoding the lipase or} variant thereof of the present invention which are used to produce the lipase or lipase variant of interest), cell debris, biomass, fermentation media and/or fermentation products. In some embodiments, the composition is a cell-killed whole broth containing organic acid(s), killed cells and/or cell debris, and culture medium. The term "fermentation broth" as used herein refers to a preparation produced by cellular fermentation that undergoes no or minimal recovery and/or purification. For example, _{fermentation broths are produced when microbial cultures are grown to saturation, incubated} under carbon-limiting conditions to allow protein synthesis (e.g., expression of enzymes by host cells) and secretion into cell culture medium. The fermentation broth can contain unfractionated or fractionated contents of the fermentation materials derived at the end of the fermentation. Typically, the fermentation broth is unfractionated and comprises the spent culture medium and cell debris present after the microbial cells (e.g., filamentous fungal cells) are removed, e.g., by centrifugation. In some embodiments, the fermentation broth contains spent cell culture medium, extracellular enzymes, and viable and/or nonviable microbial cells. In some embodiments, the fermentation broth formulation or the cell composition comprises a first organic acid component comprising at least one 1-5 carbon organic acid and/or a salt thereof and a second organic acid component comprising at least one 6 or more carbon organic acid and/or a salt thereof. In some embodiments, the first organic acid component is acetic acid, formic acid, propionic acid, a salt thereof, or a mixture of two or more of the foregoing and the second organic acid component is benzoic acid, cyclohexanecarboxylic acid, 4-methylvaleric acid, phenylacetic acid, a salt thereof, or a mixture of two or more of the foregoing. In one aspect, the composition contains an organic acid(s), and optionally further contains killed cells and/or cell debris. In some embodiments, the killed cells and/or cell debris are removed from a cell-killed whole broth to provide a composition that is free of these components. The fermentation broth formulation or cell composition may further comprise a preservative and/or anti-microbial (e.g., bacteriostatic) agent, including, but not limited to, sorbitol, sodium chloride, potassium sorbate, and others known in the art. The cell-killed whole broth or cell composition may contain the unfractionated contents of the fermentation materials derived at the end of the fermentation. Typically, the cell-killed whole broth or cell composition contains the spent culture medium and cell debris present after the microbial cells (e.g., filamentous fungal cells) are grown to saturation, incubated under carbon- limiting conditions to allow protein synthesis. In some embodiments, the cell-killed whole broth or cell composition contains the spent cell culture medium, extracellular enzymes, and killed filamentous fungal cells. In some embodiments, the microbial cells present in the cell-killed whole broth or cell composition can be permeabilized and/or lysed using methods known in the art. A whole broth or cell composition as described herein is typically a liquid, but may contain insoluble components, such as killed cells, cell debris, culture media components, and/or insoluble enzyme(s). In some embodiments, insoluble components may be removed to provide a clarified liquid composition. _{The whole broth formulations and cell compositions of the present invention may be} _{produced by a method described in WO 90/15861 or WO 2010/096673.} _{Compositions of the invention} _{The invention also relates to a composition comprising a lipase or lipase variant of the} _{invention, e.g., a detergent or cleaning composition. The composition may also be used for other} uses such as in a biodiesel process. In a preferred embodiment, the invention relates to a composition comprising a lipase or lipase variant of the invention and further comprising: one or more detergent components; and/or one or more additional enzymes. In a preferred embodiment, the composition is a detergent composition comprising one or more detergent components, in particular one or more non- naturally occurring detergent components. The present invention also relates to a composition comprising a lipase or lipase variant of the present invention and further comprising one or more additional enzymes selected from the _{group consisting of amylases (e.g., alpha-amylases), catalases, cellulases (e.g.,} endoglucanases), cutinases, DNases, haloperoxygenases, lipases, mannanases, pectinases, pectin lyases, peroxidases, proteases, xanthanases, lichenases and xyloglucanases, or any mixture thereof. A_{detergent composition may, e.g., be in the form of a bar, a homogeneous tablet, a tablet} having two or more layers, a pouch having one or more compartments, a regular or compact _{powder, a granule, a paste, a gel, or a regular, compact, or concentrated liquid.} In one preferred embodiment, the detergent composition is a liquid composition. In one preferred embodiment, the detergent composition is a powder composition. In one preferred embodiment, the detergent composition is a laundry soap bar. The invention also relates to use of a composition of the present in a cleaning process, such as laundry or hard surface cleaning such as dishwashing. The choice of additional components for a detergent composition is within the skill of the artisan and includes conventional ingredients, including the exemplary non-limiting components set forth below. The choice of components may include, for fabric care, the consideration of the type of fabric to be cleaned, the type and/or degree of soiling, the temperature at which cleaning is to take place, and the formulation of the detergent product. I_{n a particular embodiment, a detergent composition comprises a lipase or lipase variant} of the invention and one or more non-naturally occurring detergent components, such as surfactants, hydrotropes, builders, co-builders, chelators or chelating agents, bleaching system or bleach components, polymers, fabric hueing agents, fabric conditioners, foam boosters, suds suppressors, dispersants, dye transfer inhibitors, fluorescent whitening agents, perfume, optical brighteners, bactericides, fungicides, soil suspending agents, soil release polymers, anti- redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants, and solubilizers. In one embodiment, the lipase or variant of the invention may be added to a detergent composition in an amount corresponding to 0.01-200 mg of enzyme protein per liter of wash liquor, preferably 0.05-50 mg of enzyme protein per liter of wash liquor, in particular 0.1-10 mg of enzyme protein per liter of wash liquor. An automatic dish wash (ADW) composition may for example include 0.001%-30%, such as 0.01%-20%, such as 0.1-15%, such as 0.5-10% of enzyme protein by weight of the composition. A granulated composition for laundry may for example include 0.001%-20%, such as 0.01%-10%, such as 0.05%-5% of enzyme protein by weight of the composition. A liquid composition for laundry may for example include 0.0001%-10%, such as 0.001- 7%, such as 0.1%-5% of enzyme protein by weight of the composition. T_{he enzymes such as the lipase or lipase variant of the invention may be stabilized using} conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in, for example, WO 92/19709 and WO 92/19708 or the lipases or variants according to the invention may be stabilized using peptide aldehydes or ketones such as described in WO 2005/105826 and WO 2009/118375. The lipases or lipase variants of the invention may be formulated in liquid laundry compositions such as a liquid laundry compositions composition comprising: a_{) at least 0.01 mg of active lipase or lipase variant per liter detergent,} _{b) 2 wt% to 60 wt% of at least one surfactant} _{c) 5 wt% to 50 wt% of at least one builder} The detergent composition may be formulated into a granular detergent for laundry. Such detergent may comprise: a_{) at least 0.01 mg of active lipase or lipase variant per gram of composition} _{b) anionic surfactant, preferably 5 wt % to 50 wt %} _{c) nonionic surfactant, preferably 1 wt % to 8 wt %} _{d) builder, preferably 5 wt % to 40 wt %, such as carbonates, zeolites, phosphate builder,} calcium sequestering builders or complexing agents. Although components mentioned below are categorized by general header according to a particular functionality, this is not to be construed as a limitation, as a component may comprise additional functionalities as will be appreciated by the person skilled in the art. Surfactants The detergent or cleaning composition of the invention may comprise one or more surfac- tants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic, or a mixture thereof. In a particular embodiment, the detergent composition includes a surfactant system (comprising more than one surfactant) e.g. a mixture of one or more nonionic surfactants and one or more anionic surfactants. In one embodiment the detergent comprises at least one ani- onic surfactant and at least one non-ionic surfactant, the weight ratio of anionic to nonionic surfactant may be from 20:1 to 1:20. In one embodiment the amount of anionic surfactant is higher than the amount of non-ionic surfactant e.g. the weight ratio of anionic to non-ionic surfactant may be from 10:1 to 1.1:1 or from 5:1 to 1.5:1. The amount of anionic to non-ionic surfactant may also be equal and the weight ratios 1:1. In one embodiment the amount of non-ionic surfactant is higher than the amount of anionic surfactant and the weight ratio may be 1:10 to 1:1.1. Preferably the weight ratio of anionic to non-ionic surfactant is from 10:1 to 1:10, such as from 5:1 to 1:5, or from 5:1 to 1:1.2. Preferably, the weight fraction of non-ionic surfactant to anionic surfactant is from 0 to 0.5 or 0 to 0.2 thus non-ionic surfactant can be present or absent if the weight fraction is 0, but if non-ionic surfactant is present, then the weight fraction of the nonionic surfactant is preferably at most 50% or at most 20% of the total weight of anionic surfactant and non-ionic surfactant. Light duty detergent usually comprises more nonionic than anionic surfactant and there the fraction of non-ionic surfactant to anionic surfactant is preferably from 0.5 to 0.9. The total weight of surfactant(s) is typically present at a level of from about 0.1% to about 60% by weight, such as about 1% to about 40%, or about 3% to about 20%, or about 3% to about 10%. The surfactant(s) is chosen based on the desired cleaning application, and may include any conventional surfactant(s) known in the art. When included therein the detergent will usually contain from about 1% to about 40% by weight of an anionic surfactant, such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant. Non-limiting examples of anionic surfactants include sulfates and sulfonates, typically available as sodium or potassium salts or salts of monoethanolamine (MEA, 2-aminoethan-1-ol) or triethanolamine (TEA, 2,2',2''-nitrilotri- ethan-1-ol); in particular, linear alkylbenzenesulfonates (LAS), isomers of LAS such as branched alkylbenzenesulfonates (BABS) and phenylalkanesulfonates; olefin sulfonates, in particular alpha- olefinsulfonates (AOS); alkyl sulfates (AS), in particular fatty alcohol sulfates (FAS), i.e., primary al- cohol sulfates (PAS) such as dodecyl sulfate (SLS); alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates); paraffin sulfonates (PS) includ- ing alkane-1-sulfonates and secondary alkanesulfonates (SAS); ester sulfonates, including sul- fonated fatty acid glycerol esters and alpha-sulfo fatty acid methyl esters (alpha-SFMe or SES or _{MES); alkyl- or alkenylsuccinic acids such as dodecenyl/tetradecenyl succinic acid (DTSA); diesters} and monoesters of sulfosuccinic acid; fatty acid derivatives of amino acids. Anionic surfactants may be added as acids, as salts or as ethanolamine derivatives. W_{hen included therein, the detergent will usually contain from about 0,1% to about 40% by} weight of a cationic surfactant, for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%. Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyl- distearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary am- monium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and com- binations thereof. W_{hen included therein, the detergent will usually contain from about 0.2% to about 40% by} weight of a nonionic surfactant, for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%. Non-limiting examples of nonionic surfactants in- clude alcohol ethoxylates (AE or AEO) e.g. the AEO-series such as AEO-7, alcohol propoxylates, in particular propoxylated fatty alcohols (PFA), ethoxylated and propoxylated alcohols, alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters (in particular methyl ester ethoxylates, MEE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanola- mides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof. W_{hen included therein, the detergent will usually contain from about 0.01 to about 10 % by} weight of a semipolar surfactant. Non-limiting examples of semipolar surfactants include amine ox- ides (AO) such as alkyldimethylamine oxides, in particular N-(coco alkyl)-N,N-dimethylamine oxide and N-(tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, and combinations thereof. W_{hen included therein, the detergent will usually contain from about 0.01 % to about 10 %} by weight of a zwitterionic surfactant. Non-limiting examples of zwitterionic surfactants include beta- ines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof. Additional bio-based surfactants may be used e.g. wherein the surfactant is a sugar-based non-ionic surfactant which may be a hexyl-β-D-maltopyranoside, thiomaltopyranoside or a cyclic- maltopyranoside, such as described in EP2516606 B1. Other biosurfactants may include rhamno- lipids and sophorolipids. Hydrotropes A hydrotrope is a compound that solubilises hydrophobic compounds in aqueous solutions (or oppositely, polar substances in a non-polar environment). Typically, hydrotropes have both hydrophilic and a hydrophobic character (so-called amphiphilic properties as known from surfac- tants); however, the molecular structure of hydrotropes generally do not favor spontaneous self- aggregation, see e.g. review by Hodgdon and Kaler (2007), Current Opinion in Colloid & Interface Science 12: 121-128. Hydrotropes do not display a critical concentration above which self-aggre- gation occurs as found for surfactants and lipids forming miceller, lamellar or other well defined meso-phases. Instead, many hydrotropes show a continuous-type aggregation process where the sizes of aggregates grow as concentration increases. However, many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing substances of polar and non-polar character, including mixtures of water, oil, surfactants, and polymers. Hydrotropes are classically used across industries from pharma, personal care, food, to technical applications. Use of hydrotropes in detergent compositions allow for example more concentrated formulations of surfactants (as in the process of compacting liquid detergents by removing water) without in- ducing undesired phenomena such as phase separation or high viscosity. T_{he detergent or cleaning composition of the invention may contain 0-10% by weight, for} example 0-5% by weight, such as about 0.5 to about 5%, or about 3% to about 5%, of a hy- drotrope. Any hydrotrope known in the art for use in detergents may be utilized. Non-limiting exam- ples of hydrotropes include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium _{xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides,} alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof. Builders and Co-Builders The detergent or cleaning composition of the invention may contain about 0-65% by weight, such as about 5% to about 50% of a detergent builder or co-builder, or a mixture thereof. The builder and/or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and/or co-builder known in the art for use in cleaning detergents may be utilized. Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Clariant), ethanolamines such as 2- aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2'-iminodiethan-1-ol), triethanola- mine (TEA, also known as 2,2',2''-nitrilotriethan-1-ol), and (carboxymethyl)inulin (CMI), and combi- nations thereof. The detergent or cleaning composition of the invention may also contain from about 0-50% by weight, such as about 5% to about 30%, of a detergent co-builder. The detergent composition may include a co-builder alone, or in combination with a builder, for example a zeolite builder. Non- limiting examples of co-builders include or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA). According to the present invention, these components can be included in lower levels than in currently available detergent compositions. Further non-limit- ing examples include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and _{phosphonates, and alkyl- or alkenylsuccinic acid. Additional specific examples include 2,2’,2”-nitrilot-} riacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N’-disuccinic acid (EDDS), methylglycinedi- acetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diylbis(phos- phonic acid (HEDP),ethylenediaminetetramethylenetetrakis(phosphonic acid) (EDTMPA),diethy- lenetriaminepentamethylenepentakis(phosphonic acid) (DTMPA or DTPMPA), N-(2-hydroxy- ethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfome- thyl)aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SEAS), N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfoethyl)glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), α-alanine-N,N- diacetic acid (α-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phe- nylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N- diacetic acid (SLDA) , taurine-N,N-diacetic acid (TUDA) and sulfomethyl-N,N-diacetic acid (SMDA), N-(2-hydroxyethyl)ethylenediamine-N,N’,N’’-triacetic acid (HEDTA), diethanolglycine (DEG), ami- notrimethylenetris(phosphonic acid) (ATMP), and combinations and salts thereof. Further exemplary builders and/or co-builders are described in, e.g., WO 09/102854 and US 5977053. Polymers and Dispersants Generally, detergent or cleaning compositions of the invention may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1% of a polymer. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as mentioned above, or may provide anti-redeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties. Some polymers may have more than one of the above- mentioned properties and/or more than one of the below-mentioned motifs. Exemplary polymers include poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or poly(eth- ylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and silicones, co- polymers of terephthalic acid and oligomeric glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N- oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (PVPVI). Further exemplary poly- mers include polyethylene oxide and polypropylene oxide (PEO-PPO), diquaternium ethoxy sulfate, _{styrene/acrylic copolymer and perfume capsules Other exemplary polymers are disclosed in, e.g.,} WO 2006/130575. Salts of the above-mentioned polymers are also contemplated. The detergent compositions of the present invention can also contain dispersants. In particular powdered detergents may comprise dispersants. Suitable water-soluble organic materials include _{the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least} two carboxyl radicals separated from each other by not more than two carbon atoms. Suitable dispersants are for example described in Powdered Detergents, Surfactant science series volume 71, Marcel Dekker, Inc. Fabric Hueing Agents T_{he detergent or cleaning compositions of the present invention may also include fabric} hueing agents such as dyes or pigments, which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liquor comprising said detergent compositions and thus altering the tint of said fabric through absorption/reflection of visible light. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum. Suitable fabric hueing agents include dyes and dye-clay conjugates and may also include pigments. Suit- able dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.I.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in WO2005/03274, WO2005/03275, WO2005/03276 and EP1876226 (hereby incorporated by ref- erence). The detergent composition preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.0001 wt% to about 0.04 wt% fabric hueing agent. The composition may comprise from 0.0001 wt% to 0.2 wt% fabric hue- ing agent, this may be especially preferred when the composition is in the form of a unit dose pouch. Suitable hueing agents are also disclosed in, e.g. WO 2007/087257 and WO2007/087243. Dye Transfer Inhibiting Agents The detergent or cleaning compositions of the present invention may also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N- _{vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures} thereof. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about 0.0001 % to about 10%, from about 0.01% to about 5% or even from about 0.1% to about 3% by weight of the composition. Fluorescent Whitening Agent T_{he detergent or cleaning compositions of the present invention will preferably also con-} tain additional components that may tint articles being cleaned, such as fluorescent whitening agent or optical brighteners. Where present the brightener is preferably at a level of about 0.01% to about 0.5%. Any fluorescent whitening agent suitable for use in a laundry detergent composi- tion may be used in the composition of the present invention. The most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives. Examples of the dia- minostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4'-bis-(2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis- (2,4-dianilino-s-triazin-6-ylamino) stilbene-2.2'-disulfonate, 4,4'-bis-(2-anilino-4-(N-methyl-N-2- hydroxy-ethylamino)-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1,2,3-tria- zol-2-yl)stilbene-2,2'-disulfonate and sodium 5-(2H-naphtho[1,2-d][1,2,3]triazol-2-yl)-2-[(E)-2- phenylvinyl]benzenesulfonate. Preferred fluorescent whitening agents are Tinopal DMS and Tino- pal CBS available from Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of 4,4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate. Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl)-disulfonate. Also preferred are fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chem- icals, Mumbai, India. Tinopal CBS-X is a 4.4'-bis-(sulfostyryl)-biphenyl disodium salt also known as Disodium Distyrylbiphenyl Disulfonate.Other fluorescers suitable for use in the invention in- clude the 1-3-diaryl pyrazolines and the 7-alkylaminocoumarins. Suitable fluorescent brightener levels include lower levels of from about 0.01, from 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt%. Soil Release Polymers The detergent or cleaning compositions of the present invention may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and poly- ester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics. The soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series volume 71, Marcel Dekker, Inc. Another type of soil release polymers are amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure. The core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523 (hereby incorporated by reference). Further- more, random graft co-polymers are suitable soil release polymers. Suitable graft co-polymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/113314 (hereby incorporated by reference). Anti-redeposition Agents The detergent or cleaning compositions of the present invention may also include one or more anti-redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyoxyethylene and/or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid. The cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents. Rheology Modifiers The detergent or cleaning compositions of the present invention may also include one or more rheology modifiers, structurants or thickeners, as distinct from viscosity reducing agents. The rheology modifiers are selected from the group consisting of non-polymeric crystalline, hy- droxy-functional materials, polymeric rheology modifiers which impart shear thinning characteris- tics to the aqueous liquid matrix of a liquid detergent composition. The rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example as shown in EP 2169040. O_{ther suitable adjunct materials include, but are not limited to, anti-shrink agents, anti-} wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and/or structure elasticizing agents. Additional Enzymes A_{detergent additive or detergent composition comprising the lipase or variant of the} _{invention may comprise one or more enzymes such as a protease, amylase (e.g., alpha-amylase),} _{arabinase, carbohydrase, cellulase (e.g., endoglucanase), cutinase, DNase, galactanase,} haloperoxygenase, another lipase, mannanase, oxidase, e.g., laccase and/or peroxidase, pectinase, pectin lyase, xylanase, xanthanase or xyloglucanase. The properties of the selected enzyme(s) should be compatible with the selected _{detergent (e.g., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients,} etc.). Cellulases The term “cellulase” means one or more (e.g., several) enzymes that hydrolyze a cellulosic material. The terms “cellulase” and the expression “polypeptide having cellulase activity” are used interchangeably. Cellulases may be selected from the group consisting of cellulases belonging to GH5, GH44, GH45, EC 3.2.1.4, EC 3.2.1.21, EC 3.2.1.91 and EC 3.2.1.172. Such enzymes in- _{clude endoglucanase(s) (e.g., EC 3.2.1.4), cellobiohydrolase(s), beta-glucosidase(s), or combi-} nations thereof. Suitable cellulases include mono-component and mixtures of enzymes of bacterial or fun- gal origin. Chemically modified or protein engineered mutants are also contemplated. The cellu- lase may for example be a mono-component or a mixture of mono-component endo-1,4-beta- glucanase also referred to as endoglucanase. _{Suitable cellulases include those from the genera Bacillus, Pseudomonas, Humicola, My-} _{celiophthora, Fusarium, Thielavia, Trichoderma, and Acremonium. Exemplary cellulases include} _{a fungal cellulase from Humicola insolens (US 4,435,307) or from Trichoderma, e.g., T. reesei or} _{T. viride. Other suitable cellulases are from Thielavia, e.g., Thielavia terrestris as described inWO} _{96/29397, or the fungal cellulases produced from Myceliophthora thermophila and Fusarium ox-} _{ysporum disclosed in US 5,648,263, US 5,691,178, US 5,776,757, WO 89/09259 and WO} _{91/17244. Also relevant are cellulases from Bacillus as described in WO 02/099091 and JP} _{2000210081. Suitable cellulases are alkaline or neutral cellulases having care benefits. Exam-} ples of cellulases are described in EP 0495257, EP 0531372, WO 96/11262, WO 96/29397, WO 98/08940. Other examples are cellulase variants such as those described in WO 94/07998, EP 0531315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471, WO 98/12307. Other cellulases are endo-beta-1,4-glucanase enzyme having a sequence of at least 97% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO:2 of WO 2002/099091 or a family 44 xyloglucanase, which a xyloglucanase enzyme having a sequence of at least 60% identity to positions 40-559 of SEQ ID NO: 2 of WO 2001/062903. Yet another group of suitable cellulases comprise a stabilized linker between the core and the CBM. Particularly useful are such cellulase having at least 80% identity to SEQ ID NO: 397, SEQ ID NO: 398 or SEQ ID NO: 399 of WO 2023/061928. Commercially available cellulases include Carezyme®, Carezyme® Premium, Cel- _{luzyme®, Carezyme Elite®, Celluclean®, Celluclast®, Endolase®, Renozyme®, Whitezyme®} _{Celluclean® Classic, and Cellusoft® (Novozymes A/S); Puradax®, Puradax HA, Puradax EG,} _{Revitalenz 1000, Revitalenz 200, and Revitalenz 2000 (Dupont Industrial Biosciences); KAC-} _{500(B)™ (Kao Corporation); and Biotouch DCL and Biotouch FLX1 (AB Enzymes).} The two basic approaches for measuring cellulolytic enzyme activity include: (1) measur- ing the total cellulolytic enzyme activity, and (2) measuring the individual cellulolytic enzyme ac- tivities (endoglucanases, cellobiohydrolases, and beta-glucosidases) as reviewed in Zhang et al., _{2006, Biotechnology Advances 24: 452-481. Total cellulolytic enzyme activity can be measured} using insoluble substrates, including Whatman №1 filter paper, microcrystalline cellulose, bacte- rial cellulose, algal cellulose, cotton, pretreated lignocellulose, etc. The most common total cellu- lolytic activity assay is the filter paper assay using Whatman №1 filter paper as the substrate. The assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, _{1987, Pure Appl. Chem.59: 257-68).} Proteases T_{he composition may comprise one or more proteases including those of bacterial, fungal,} plant, viral or animal origin, e.g., vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may for example be of the S1 _{family, such as trypsin, or the S8 family such as subtilisin. A metalloprotease may for example be} a thermolysin from, e.g., family M4 or other metalloprotease such as those from M5, M7 or M8 families. The term "subtilases" refers to a sub-group of serine protease according to Siezen et al., Protein Engng. 4 (1991) 719-737 and Siezen et al. Protein Science 6 (1997) 501-523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate. The subtilases may be divided into 6 sub-divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family. E_{xamples of subtilases are those derived from Bacillus such as Bacillus lentus, B.} _{alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in;} US7262042 and WO09/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN’, subtilisin 309, subtilisin 147 and subtilisin 168 described in WO89/06279 and protease PD138 described in (WO93/18140). Other useful proteases may be those described in WO92/175177, WO01/016285, WO02/026024 and WO02/016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO89/06270, WO94/25583 and WO05/040372, and the chymotrypsin proteases derived from Cellumonas described in WO05/052161 and WO05/052146. A_{further preferred protease is the alkaline protease from Bacillus lentus DSM 5483, as} described for example in WO95/23221, and variants thereof which are described in WO92/21760, WO95/23221, EP1921147 and EP1921148. Examples of metalloproteases are the neutral metalloprotease as described in WO 07/044993 (Genencor Int.) such as those derived from Bacillus amyloliquefaciens. Examples of useful proteases are the variants described in: WO92/19729, WO96/034946, WO98/20115, WO98/20116, WO99/011768, WO01/44452, WO03/006602, WO04/03186, WO04/041979, WO07/006305, WO11/036263, WO11/036264, especially the variants with substitutions in one or more of the following positions: 3, 4, 9, 15, 27, 36, 57, 68, 76, 87, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 106, 118, 120, 123, 128, 129, 130, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and 274 using the BPN’ numbering. More preferred the subtilase variants may comprise the mutations: S3T, V4I, S9R, A15T, K27R, *36D, V68A, N76D, N87S,R, *97E, A98S, S99G,D,A, S99AD, S101G,M,R S103A, V104I,Y,N, S106A, G118V,R, H120D,N, N123S, S128L, P129Q, S130A, G160D, Y167A, R170S, _{A194P, G195E, V199M, V205I, L217D, N218D, M222S, A232V, K235L, Q236H, Q245R, N252K,} T274A (using BPN’ numbering).Examples of metalloproteases are the neutral metalloproteases as described in WO 2007/044993 (Genencor Int.) such as those derived from Bacillus amyloliquefaciens. Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, Blaze®; Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, _{Ovozyme®, Coronase®, Coronase® Ultra, Neutrase®, Everlase®, Esperase®, Progress® Excel,} Progress® Key, and Progress® Uno (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect Prime®, Purafect MA®, Purafect Ox®, Purafect OxP®, Puramax®, Properase®, FN2®, FN3®, FN4®, Excellase®, Eraser®, Opticlean®, _{Optimase®, Preferenz® P200, Preferenz® P300, and Preferenz® P400 (DuPont/IFF), Axapem™} (Gist-Brocades N.V.), BLAP (sequence shown in Figure 29 of US5352604) and variants hereof _{(Henkel AG) and KAP (Bacillus alkalophilus subtilisin) from Kao.} Other Lipases and Cutinases Additional suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include _{lipase from Thermomyces, e.g., from T. lanuginosus (previously named Humicola lanuginosa) as} described in EP 258068 and EP 305216, cutinase from Humicola, e.g., H. insolens (WO _{96/13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia),} _{e.g., P. alcaligenes or P. pseudoalcaligenes (EP 218272), P. cepacia (EP 331376), P. sp. strain} _{SD705 (WO 95/06720 & WO 96/27002), P. wisconsinensis (WO 96/12012), GDSL-type} _{Streptomyces lipases (WO 2010/065455), cutinase from Magnaporthe grisea (WO 2010/107560),} _{cutinase from Pseudomonas mendocina (US 5,389,536), lipase from Thermobifida fusca (WO} _{2011/084412), Geobacillus stearothermophilus lipase (WO 2011/084417), lipase from Bacillus} _{subtilis (WO 2011/084599), and lipase from Streptomyces griseus (WO 2011/150157) and S.} _{pristinaespiralis (WO 2012/137147).} Other examples are lipase variants such as those described in EP 407225, WO 92/05249, WO 94/01541, WO 94/25578, WO 95/14783, WO 95/30744, WO 95/35381, WO 95/22615, WO 96/00292, WO 97/04079, WO 97/07202, WO 00/34450, WO 00/60063, WO 01/92502, WO 2007/87508 and WO 2009/109500. Preferred commercial lipase products include Lipolase™, Lipex™; Lipex Evity 100L, Lipex _{Evity 200L, Lipolex™ and Lipoclean™ (Novozymes A/S), Lumafast (originally from Dniasco US))} and Lipomax (originally from Danisco US). Still other examples are lipases sometimes referred to as acyltransferases or _{perhydrolases, e.g., acyltransferases with homology to Candida antarctica lipase A (WO} _{2010/111143), acyltransferase from Mycobacterium smegmatis (WO 2005/056782),} perhydrolases from the CE 7 family (WO 2009/067279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO 2010/100028). Amylases Suitable amylases which can be used together with the lipase and lipase variants of the invention may be an alpha-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1,296,839. S_{uitable amylases include amylases having SEQ ID NO:2 in WO 95/10603 or variants} _{having 90% sequence identity to SEQ ID NO:3 thereof. Preferred variants are described in WO} _{94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO:4 of WO 99/19467, such as variants} with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444. D_{ifferent suitable amylases include amylases having SEQ ID NO:6 in WO 02/10355 or} variants thereof having 90% sequence identity to SEQ ID NO:6. Preferred variants of SEQ ID _{NO:6 are those having a deletion in positions 181 and 182 and a substitution in position 193.} Other amylases which are suitable are hybrid alpha-amylases comprising residues 1-33 _{of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO:6 of WO} _{2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO:4} of WO 2006/066594 or variants having 90% sequence identity thereof. Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181, N190, M197, I201, A209 and Q264. Most preferred variants of the hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase _{derived from B. amyloliquefaciens shown in SEQ ID NO:6 of WO 2006/066594 and residues 36-} _{483 of SEQ ID NO:4 are those having the substitutions:} M197T; H156Y+A181T+N190F+A209V+Q264S; or G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S. O_{ther suitable amylases are amylases having the sequence of SEQ ID NO:6 in WO} 99/19467 or variants thereof having 90% sequence identity to SEQ ID NO:6. Preferred variants _{of SEQ ID NO:6 are those having a substitution, a deletion or an insertion in one or more of the} following positions: R181, G182, H183, G184, N195, I206, E212, E216 and K269. Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184. Additional amylases which can be used are those having SEQ ID NO:1, SEQ ID NO:3, _{SEQ ID NO:2 or SEQ ID NO:7 of WO 96/23873 or variants thereof having 90% sequence identity} _{to SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3 or SEQ ID NO:7. Preferred variants of SEQ ID} _{NO:1, SEQ ID NO:2, SEQ ID NO:3 or SEQ ID NO:7 are those having a substitution, a deletion or} an insertion in one or more of the following positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96/23873 for numbering. More preferred variants _{are those having a deletion in two positions selected from 181, 182, 183 and 184, such as 181} and 182, 182 and 183, or positions 183 and 184. Most preferred amylase variants of SEQ ID _{NO:1, SEQ ID NO:2 or SEQ ID NO:7 are those having a deletion in positions 183 and 184 and a} substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476. O_{ther amylases which can be used are amylases having SEQ ID NO:2 of WO} 2008/153815, SEQ ID NO:10 in WO 01/66712 or variants thereof having 90% sequence identity _{to SEQ ID NO:2 of WO 2008/153815 or 90% sequence identity to SEQ ID NO:10 in WO 01/66712.} Preferred variants of SEQ ID NO:10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211 and 264. F_{urther suitable amylases are amylases having SEQ ID NO:2 of WO 2009/061380 or} _{variants having 90% sequence identity to SEQ ID NO:2 thereof. Preferred variants of SEQ ID} _{NO:2 are those having a truncation of the C-terminus and/or a substitution, a deletion or an} insertion in one of more of the following positions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, _{Q359, K444 and G475. More preferred variants of SEQ ID NO:2 are those having the substitution} in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131I, T165I, K178L, T182G, M201L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/or deletion in position R180 and/or S181 or of T182 and/or G183. Most _{preferred amylase variants of SEQ ID NO:2 are those having the substitutions:} N128C+K178L+T182G+Y305R+G475K; N128C+K178L+T182G+F202Y+Y305R+D319T+G475K; S125A+N128C+K178L+T182G+Y305R+G475K; or S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K, wherein the variants are C-terminally truncated and optionally further comprise a substitution at position 243 and/or a deletion at position 180 and/or position 181. F_{urther suitable amylases are amylases having SEQ ID NO:1 of WO 2013/184577 or} _{variants having 90% sequence identity to SEQ ID NO:1 thereof. Preferred variants of SEQ ID} _{NO:1 are those having a substitution, a deletion or an insertion in one of more of the following} positions: K176, R178, G179, T180, G181, E187, N192, M199, I203, S241, R458, T459, D460, _{G476 and G477. More preferred variants of SEQ ID NO:1 are those having the substitution in one} of more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241QADN, R458N, T459S, D460T, G476K and G477K and/or a deletion in position R178 and/or S179 or of _{T180 and/or G181. Most preferred amylase variants of SEQ ID NO:1 comprise the substitutions:} E187P+I203Y+G476K E187P+I203Y+R458N+T459S+D460T+G476K and optionally further comprise a substitution at position 241 and/or a deletion at position 178 and/or position 179. F_{urther suitable amylases are amylases having SEQ ID NO:1 of WO 2010/104675 or} _{variants having 90% sequence identity to SEQ ID NO:1 thereof. Preferred variants of SEQ ID} _{NO:1 are those having a substitution, a deletion or an insertion in one of more of the following} positions: N21, D97, V128 K177, R179, S180, I181, G182, M200, L204, E242, G477 and G478. M_{ore preferred variants of SEQ ID NO:1 are those having the substitution in one of more} of the following positions: N21D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K and G478K and/or a deletion in position R179 and/or S180 or of I181 and/or G182. Most preferred _{amylase variants of SEQ ID NO:1 comprise the substitutions N21D+D97N+V128I, and optionally} further comprise a substitution at position 200 and/or a deletion at position 180 and/or position 181. Other suitable amylases are the alpha-amylase having SEQ ID NO:12 in WO 01/66712 or a variant having at least 90% sequence identity to SEQ ID NO:12. Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO:12 in WO 01/66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particularly preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R118K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions. Other examples are amylase variants such as those described in WO 2011/098531, WO 2013/001078 and WO 2013/00108™7. Commercially available amylases are Amplify™, Amplify _{Prime™, Achieve Advance™, Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme} _{Plus™, Natalase™, Liquozyme X and BAN™ (from Novozymes A/S), and Rapidase™,} Purastar™/Effectenz™, Powerase, Preferenz S100, Preferenz S110, Preferenz S210, Preferenz _{S1000, Excellenz S2000, Excellenz S2001, and Excellenz S3300 (from Danisco US).} Peroxidases/Oxidases Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257. C_{ommercially available peroxidases include Guardzyme™ (Novozymes A/S).} Adjunct materials Any detergent components known in the art for use in laundry detergents may also be utilized. Other optional detergent components include anti-corrosion agents, anti-shrink agents, anti-soil redeposition agents, anti-wrinkling agents, bactericides, binders, corrosion inhibitors, disintegrants/disintegration agents, dyes, enzyme stabilizers (including boric acid, borates, CMC, and/or polyols such as propylene glycol), fabric conditioners including clays, fillers/processing aids, fluorescent whitening agents/optical brighteners, foam boosters, foam (suds) regulators, perfumes, soil-suspending agents, softeners, suds suppressors, tarnish inhibitors, and wicking agents, either alone or in combination. Any ingredient known in the art for use in laundry detergents may be utilized. The choice of such ingredients is well within the skill of the artisan. D_{ispersants: The detergent compositions of the present invention can also contain} dispersants. In particular powdered detergents may comprise dispersants. Suitable water-soluble _{organic materials include the homo- or co-polymeric acids or their salts, in which the} polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms. Suitable dispersants are for example described in Powdered Detergents, Surfactant Science Series, volume 71, Marcel Dekker, Inc., 1997. D_{ye Transfer Inhibiting Agents: The detergent compositions of the present invention may} also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about 0.0001% to about 10%, from about 0.01% to about 5% or even from about 0.1% to about 3% by weight of the composition. F_{luorescent whitening agent: The detergent compositions of the present invention will} preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent or optical brighteners. Where present the brightener is preferably at a level of about 0.01% to about 05%. Any fluorescent whitening agent suitable for use in a laundry _{detergent composition may be used in the composition of the present invention. The most} commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulphonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives. Examples of the diaminostilbene-sulphonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4'-bis-(2-diethanolamino-4-anilino-s-triazin-6- ylamino) stilbene-2,2'-disulphonate; 4,4'-bis-(2,4-dianilino-s-triazin-6-ylamino) stilbene-2.2'- disulphonate; 4,4'-bis-(2-anilino-4(N-methyl-N-2-hydroxy-ethylamino)-s-triazin-6-ylamino) stilbene-2,2'-disulphonate, 4,4'-bis-(4-phenyl-2,1,3-triazol-2-yl)stilbene-2,2'-disulphonate; 4,4'- bis-(2-anilino-4(1-methyl-2-hydroxy-ethylamino)-s-triazin-6-ylamino) stilbene-2,2'-disulphonate and 2-(stilbyl-4"-naptho-1.,2':4,5)-1,2,3-trizole-2"-sulphonate. Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of 4,4'-bis-(2-morpholino-4 anilino-s-triazin-6-ylamino) stilbene disulphonate. Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl) disulphonate. Also preferred are fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India. Other fluorescers suitable for use in the invention include the 1-3-diaryl pyrazolines and the 7-alkylaminocoumarins. Suitable fluorescent brightener levels include lower levels of from about 0.01, from 0.05, from about 0.1 or even from about 0.2 wt. % to upper levels of 0.5 or even 0.75 wt. %. S_{oil release polymers: The detergent compositions of the present invention may also} include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics. The soil release polymers may for example be nonionic or anionic terephthalate based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series volume _{71, Marcel Dekker, Inc. Another type of soil release polymers is amphiphilic alkoxylated grease} cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure. The core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523 (hereby incorporated by reference). Furthermore, random graft co-polymers are suitable soil release polymers Suitable graft co-polymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/113314 (hereby incorporated by reference). Other soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose derivatives such as those described in EP 1867808 or WO 03/040279 (both are hereby incorporated by reference). Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cationically modified cellulose, zwitterionically modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methyl cellulose, carboxy methyl cellulose, ethyl cellulose, hydroxyl ethyl cellulose, hydroxyl propyl methyl cellulose, ester carboxy methyl cellulose, and mixtures thereof. A_{nti-redeposition agents: The detergent compositions of the present invention may also} include one or more anti-redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and/or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimines. The cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents. O_{ther suitable adjunct materials include, but are not limited to, anti-shrink agents, anti-} wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and/or structure elasticizing agents. Formulation of Detergent Products T_{he detergent enzyme(s), i.e., a lipase or lipase variant of the invention and optionally one} or more additional enzymes, may be included in a detergent composition by adding separate additives containing one or more enzymes, or by adding a combined additive comprising all of these enzymes. A detergent additive comprising one or more enzymes can be formulated, for example, as a granulate, liquid, slurry, etc. Preferred detergent additive formulations include granulates, in particular non-dusting granulates, liquids, in particular stabilized liquids, or slurries. The detergent composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid. There are a number of detergent formulation forms such as layers (same or different phases), pouches, as well as forms for machine dosing unit. Pouches can be configured as single or multiple compartments. It can be of any form, _{shape and material which is suitable for holding the composition, e.g., without allowing the release} of the composition from the pouch prior to water contact. The pouch is made from water soluble film which encloses an inner volume. The inner volume can be divided into compartments of the _{pouch. Preferred films are polymeric materials, preferably polymers which are formed into a film} or sheet. Preferred polymers, copolymers or derivates thereof are selected from polyacrylates, and water-soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, maltodextrin, polymethacrylates, most preferably polyvinyl alcohol copolymers and hydroxypropyl methyl cellulose (HPMC). Preferably the level of polymer in the film for example PVA is at least about 60%. The preferred average molecular weight will typically be about 20,000 to about 150,000. Films can also be of blend compositions comprising hydrolytically degradable and water-soluble polymer blends such as polylactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by Chris Craft In. Prod. of Gary, Indiana, US) plus plasticizers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof. The pouches can comprise a solid laundry detergent composition or part components and/or a liquid cleaning composition or part components separated by the water-soluble film. The compartment for liquid components can be different in composition than compartments containing solids. See, e.g., US 2009/0011970. Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction _{between components can be avoided. Different dissolution profiles of each of the compartments} can also give rise to delayed dissolution of selected components in the wash solution. A liquid or gel detergent which is not unit dosed may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water. Other types of liquids, including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel. An aqueous liquid or gel detergent may contain from 0-30% organic solvent. A liquid or gel detergent may be non-aqueous. Laundry Soap Bars A lipase or lipase variant of the invention may be added to laundry soap bars and used for hand washing laundry, fabrics and/or textiles. The term laundry soap bar includes laundry bars, soap bars, combo bars, syndet bars and detergent bars. The types of bar usually differ in the type of surfactant they contain, and the term laundry soap bar includes those containing soaps from fatty acids and/or synthetic soaps. The laundry soap bar has a physical form which is solid and thus not a liquid, gel or powder at room temperature. The laundry soap bar may contain one or more additional enzymes, protease inhibitors such as peptide aldehydes (or hydrosulfite adduct or hemiacetal adduct), boric acid, borate, borax and/or phenylboronic acid derivatives such as 4-formylphenylboronic acid, one or more soaps or synthetic surfactants, polyols such as glycerin, pH controlling compounds such as fatty acids, citric acid, acetic acid and/or formic acid, and/or a salt of a monovalent cation and an organic anion wherein the monovalent cation may be for example Na⁺, K⁺, or NH4⁺ and the organic anion _{may be for example formate, acetate, citrate, or lactate such that the salt of a monovalent cation} and an organic anion may be, for example, sodium formate. The laundry soap bar may also contain complexing agents such as EDTA and HEDP, perfumes and/or different type of fillers, surfactants, e.g., anionic synthetic surfactants, builders, polymeric soil release agents, detergent chelators, stabilizing agents, fillers, dyes, colorants, dye transfer inhibitors, alkoxylated polycarbonates, suds suppressers, structurants, binders, leaching agents, bleaching activators, clay soil removal agents, anti-redeposition agents, polymeric dispersing agents, brighteners, fabric softeners, perfumes and/or other compounds known in the art. The laundry soap bar may be processed in conventional laundry soap bar making _{equipment such as, but not limited to, mixers, plodders, e.g., a two-stage vacuum plodder,} extruders, cutters, logo-stampers, cooling tunnels and wrappers. A premix containing a soap, the enzyme of the invention, optionally one or more additional enzymes, a protease inhibitor, and a salt of a monovalent cation and an organic anion may be prepared and the mixture is then plodded. The enzyme and optional additional enzymes may be added at the same time as the protease inhibitor for example in liquid form. Besides the mixing step and the plodding step, the process may further comprise the steps of milling, extruding, cutting, stamping, cooling and/or wrapping. Granular detergent formulations E_{nzymes such as lipase and lipase variants of the present invention in the form of granules,} comprising an enzyme-containing core and optionally one or more coatings, are commonly used in granular (powder) detergents. Various methods for preparing the core are well-known in the art and include, for example, a) spray drying of a liquid enzyme-containing solution, b) production of layered products with an enzyme coated as a layer around a pre-formed inert core particle, e.g. using a fluid bed apparatus, c) absorbing an enzyme onto and/or into the surface of a pre-formed core, d) extrusion of an enzyme-containing paste, e) suspending an enzyme-containing powder in molten wax and atomization to result in prilled products, f) mixer granulation by adding an enzyme-containing liquid to a dry powder composition of granulation components, g) size reduction of enzyme-containing cores by milling or crushing of larger particles, pellets, etc., and _{h) fluid bed granulation. The enzyme-containing cores may be dried, e.g., using a fluid bed drier} or other known methods for drying granules in the feed or enzyme industry, to result in a water content of typically 0.1 -10% w/w water. The enzyme-containing cores are optionally provided with a coating to improve storage stability and/or to reduce dust formation. One type of coating that is often used for enzyme _{granulates for detergents is a salt coating, typically an inorganic salt coating, which may, e.g., be} applied as a solution of the salt using a fluid bed. Other coating materials that may be used are, for example, polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA). The granules may contain more than one coating, for example a salt coating followed by an additional coating of a material such as PEG, MHPC or PVA. The present invention thus also relates to enzyme granules/particles comprising the _{variant of the invention. In an embodiment, the granule comprises a core, and optionally one or} more coatings (outer layers) surrounding the core. The core may have a diameter, measured as equivalent spherical diameter (volume based average particle size), of 20-2000 µm, particularly 50-1500 µm, 100-1500 µm or 250-1200 µm. In an embodiment, the core comprises one or more polypeptides of the present invention having lipase activity. The core may include additional materials such as fillers, fiber materials (cellulose or synthetic fibers), stabilizing agents, solubilizing agents, suspension agents, viscosity regulating agents, light spheres, plasticizers, salts, lubricants and fragrances. The core may include a binder, such as synthetic polymer, wax, fat, or carbohydrate. The core may include a salt of a multivalent cation, a reducing agent, an antioxidant, a peroxide decomposing catalyst and/or an acidic buffer component, typically as a homogenous blend. The core may include an inert particle with the enzyme absorbed into it, or applied onto the surface, e.g., by fluid bed coating. The core may have a diameter of 20-2000 µm, particularly 50-1500 µm, 100-1500 µm or 250-1200 µm. The core may be surrounded by at least one coating, e.g., to improve the storage stability, to reduce dust formation during handling, or for coloring the granule. The optional coating(s) may include a salt coating, or other suitable coating materials, such as polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA). The coating may be applied in an amount of at least 0.1% by weight of the core, e.g., at least 0.5%, at least 1%, at least 5%, at least 10%, or at least 15%. The amount may be at most 100%, 70%, 50%, 40% or 30%. The coating is preferably at least 0.1 µm thick, particularly at least 0.5 µm, at least 1 µm or at least 5 µm. In some embodiments, the thickness of the coating is below 100 µm, such as below 60 µm, or below 40 µm. The coating should encapsulate the core unit by forming a substantially continuous layer. A substantially continuous layer is to be understood as a coating having few or no holes, so that _{the core unit it is encapsulating/enclosing has few or none uncoated areas. The layer or coating} should, in particular, be homogeneous in thickness. The coating can further contain other materials as known in the art, e.g., fillers, antisticking agents, pigments, dyes, plasticizers and/or binders, such as titanium dioxide, kaolin, calcium carbonate or talc. A salt coating may comprise at least 60% by weight of a salt, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% by weight. To provide acceptable protection, the salt coating is preferably at least 0.1 µm thick, e.g., at least 0.5 µm, at least 1 µm, at least 2 µm, at least 4 µm, at least 5 µm, or at least 8 µm. In a particular embodiment, the thickness of the salt coating is below 100 µm, such as below 60 µm, or below 40 µm. The salt may be added from a salt solution where the salt is completely dissolved or from a salt suspension wherein the fine particles are less than 50 µm, such as less than 10 µm or less than 5 μm. The salt coating may comprise a single salt or a mixture of two or more salts. The salt may be water soluble, in particular, having a solubility at least 0.1 g in 100 g of water at 20°C, preferably at least 0.5 g per 100 g water, e.g., at least 1 g per 100 g water, e.g., at least 5 g per 100 g water. The salt may be an inorganic salt, e.g., salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids (less than 10 carbon atoms, e.g., 6 or less carbon atoms) such as citrate, malonate or acetate. Examples of cations in these salts are alkali or earth alkali metal ions, the ammonium ion or metal ions of the first transition series, such as sodium, potassium, magnesium, calcium, zinc or aluminum. Examples of anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, monobasic phosphate, dibasic phosphate, hypophosphite, dihydrogen pyrophosphate, tetraborate, borate, carbonate, bicarbonate, metasilicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, _{butyrate, propionate, benzoate, tartrate, ascorbate or gluconate. In particular, alkali- or earth alkali} metal salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids such as citrate, malonate or acetate may be used. T_{he salt in the coating may have a constant humidity at 20 °C above 60%, particularly} above 70%, above 80% or above 85%, or it may be another hydrate form of such a salt (e.g., anhydrate). The salt coating may be as described in WO 00/01793 or WO 2006/034710. Specific examples of suitable salts are NaCl (CH20°C=76%), Na2CO3 (CH20°C=92%), NaNO3 (CH20°C=73%), Na2HPO4 (CH20°C=95%), Na3PO4 (CH25°C=92%), NH4Cl (CH20°C = 79.5%), (NH4)2HPO4 (CH20°C = 93,0%), NH4H2PO4 (CH20°C = 93.1%), (NH4)2SO4 (CH20°C=81.1%), KCl (CH20°C=85%), K2HPO4 (CH20°C=92%), KH2PO4 (CH20°C=96.5%), KNO3 (CH20°C=93.5%), Na2SO4 (CH20°C=93%), K2SO4 (CH20°C=98%), KHSO4 (CH20°C=86%), MgSO4 (CH20°C=90%), ZnSO4 (CH20°C=90%) and sodium citrate (CH25°C=86%). Other examples include NaH2PO4, (NH4)H2PO4, CuSO4, Mg(NO3)2 and magnesium acetate. The salt may be in anhydrous form, or it may be a hydrated salt, i.e., a crystalline salt hydrate with bound water(s) of crystallization, such as described in WO 99/32595. Specific exam- ples include anhydrous sodium sulfate (Na2SO4), anhydrous magnesium sulfate (MgSO4), mag- nesium sulfate heptahydrate (MgSO4·7H2O), zinc sulfate heptahydrate (ZnSO4·7H2O), sodium phosphate dibasic heptahydrate (Na2HPO4·7H2O), magnesium nitrate hexahydrate (Mg(NO3)2(6H2O)), sodium citrate dihydrate and magnesium acetate tetrahydrate. Preferably the salt is applied as a solution of the salt, e.g., using a fluid bed. The coating materials can be waxy coating materials and film-forming coating materials. Examples of waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 eth- ylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- _{and di- and triglycerides of fatty acids. Examples of film-forming coating materials suitable for} application by fluid bed techniques are given in GB 1483591. T_{he granules may optionally have one or more additional coatings. Examples of suitable} coating materials are polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and _{polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are described in} WO 93/07263 and WO 97/23606. The core can be prepared by granulating a blend of the ingredients, e.g., by a method comprising granulation techniques such as crystallization, precipitation, pan-coating, fluid bed coating, fluid bed agglomeration, rotary atomization, extrusion, prilling, spheronization, size re- duction methods, drum granulation, and/or high shear granulation. Methods for preparing the core can be found in the Handbook of Powder Technology; Particle size enlargement by C. E. Capes; Volume 1; 1980; Elsevier. Preparation methods include known feed and granule formulation technologies, e.g., (a) Spray dried products, wherein a liquid enzyme-containing solution is atomized in a spray drying tower to form small droplets which during their way down the drying tower dry to form _{an enzyme-containing particulate material. Very small particles can be produced this way} (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; vol. 71; page 140-142; Marcel Dekker). (b) Layered products, wherein the enzyme is coated as a layer around a pre-formed inert core particle, wherein an enzyme-containing solution is atomized, typically in a fluid bed apparatus wherein the pre-formed core particles are fluidized, and the enzyme-containing solution adheres to the core particles and dries up to leave a layer of dry enzyme on the surface of the core particle. Particles of a desired size can be obtained this way if a useful core particle of the desired size can be found. This type of product is described in, e.g., WO 97/23606. (c) Absorbed core particles, wherein rather than coating the enzyme as a layer around the core, the enzyme is absorbed onto and/or into the surface of the core. Such a process is described in WO 97/39116. (d) Extrusion or pelletized products, wherein an enzyme-containing paste is pressed to pellets or under pressure is extruded through a small opening and cut into particles which are subsequently dried. Such particles usually have a considerable size because of the material in which the extrusion opening is made (usually a plate with bore holes) sets a limit on the allowable pressure drop over the extrusion opening. Also, very high extrusion pressures when using a small opening increase heat generation in the enzyme paste, which is harmful to the enzyme (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; vol.71; pages 140- 142; Marcel Dekker). (e) Prilled products, wherein an enzyme-containing powder is suspended in molten wax and the suspension is sprayed, e.g., through a rotating disk atomizer, into a cooling chamber where the droplets quickly solidify (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; vol. 71; page 140-142; Marcel Dekker). The product obtained is one wherein the enzyme is uniformly distributed throughout an inert material instead of being concentrated on its surface. U.S. Patent Nos.4,016,040 and 4,713,245 describe this technique. (f) Mixer granulation products, wherein an enzyme-containing liquid is added to a dry powder composition of conventional granulating components. The liquid and the powder in a suitable proportion are mixed and as the moisture of the liquid is absorbed in the dry powder, the components of the dry powder will start to adhere and agglomerate and particles will build up, forming granulates comprising the enzyme. Such a process is described in U.S. Patent No. 4,106,991 and related documents EP 170360, EP 304332, EP 304331, WO 90/09440 and WO 90/09428. In a particular product of this process, various high-shear mixers can be used as _{granulators. Granulates consisting of enzyme, fillers and binders etc. are mixed with cellulose} fibers to reinforce the particles to produce a so-called T-granulate. Reinforced particles are more robust, and release less enzymatic dust. (g) Size reduction, wherein the cores are produced by milling or crushing of larger particles, pellets, tablets, briquettes etc. containing the enzyme. The wanted core particle fraction is obtained by sieving the milled or crushed product. Over and undersized particles can be recycled. Size reduction is described in Martin Rhodes (editor); Principles of Powder Technology; 1990; Chapter 10; John Wiley & Sons. (h) Fluid bed granulation. Fluid bed granulation involves suspending particulates in an air stream and spraying a liquid onto the fluidized particles via nozzles. Particles hit by spray droplets _{get wetted and become tacky. The tacky particles collide with other particles and adhere to them} to form a granule. (i) The cores may be subjected to drying, such as in a fluid bed drier. Other known methods for drying granules in the feed or enzyme industry can be used by the skilled person. The drying preferably takes place at a product temperature of from 25 to 90°C. For some enzymes, it is important the cores comprising the enzyme contain a low amount of water before coating with the salt. If water sensitive enzymes are coated with a salt before excessive water is removed, it will be trapped within the core and may affect the activity of the enzyme negatively. After drying, the cores preferably contain 0.1-10% w/w water. Non-dusting granulates may be produced, e.g., as disclosed in U.S. Patent Nos. 4,106,991 and 4,661,452 and may optionally be coated by methods known in the art. The granulate may further one or more additional enzymes. Each enzyme will then be present in more granules securing a more uniform distribution of the enzymes, and also reduces the physical segregation of different enzymes due to different particle sizes. Methods for producing multi-enzyme co-granulates is disclosed in the ip.com disclosure IPCOM000200739D. Another example of formulation of enzymes by the use of co-granulates is disclosed in WO 2013/188331. The enzyme may also be a protected enzyme prepared according to the method disclosed in EP 238,216. In an embodiment, the granule further comprises one or more additional enzymes, e.g., hydrolase, isomerase, ligase, lyase, oxidoreductase, and transferase. The one or more additional enzymes are preferably selected from the group consisting of acetylxylan esterase, acylglycerol another lipase, amylase, alpha-amylase, beta-amylase, arabinofuranosidase, cellobiohydrolases, cellulase, feruloyl esterase, galactanase, alpha-galactosidase, beta-galactosidase, beta- glucanase, beta-glucosidase, lysophospholipase, lysozyme, alpha-mannosidase, beta- mannosidase (mannanase), phytase, phospholipase A1, phospholipase A2, phospholipase D, protease, pullulanase, pectin esterase, triacylglycerol lipase, xylanase, beta-xylosidase or any combination thereof. For further information on enzyme granules and production thereof, see WO 2013/007594 _{as well as, e.g., WO 2009/092699, EP 1705241, EP 1382668, WO 2007/001262, US 6,472,364,} _{WO 2004/074419, and WO 2009/102854.} Uses The present invention is also directed to methods for using the lipase or lipase variants of _{the invention or compositions thereof comprising said lipases or lipase variants in laundering of} textile and fabrics, such as household laundry washing and industrial laundry washing. The invention is also directed to methods for using the lipases or lipase variants according to the invention or compositions thereof in cleaning hard surfaces such as floors, tables, walls, roofs etc. as well as surfaces of hard objects such as cars (car wash) and dishes (dishwashing). The lipases and lipase variants of the present invention may be added to and thus become a component of a detergent composition. Thus, one aspect of the invention relates to the use of _{a lipase or lipase variant of the invention in a cleaning process such as laundering and/or hard} surface cleaning. A detergent composition of the present invention may be formulated, for example, as a hand or machine laundry detergent composition including a laundry additive composition suitable _{for pre-treatment of stained fabrics and a rinse added fabric softener composition or be formulated} _{as a detergent composition for use in general household hard surface cleaning operations or be} formulated for hand or machine dishwashing operations. The cleaning process or the textile care process may for example be a laundry process, _{a dishwashing process, or cleaning of hard surfaces such as bathroom tiles, floors, tabletops,} drains, sinks and washbasins. Laundry processes can for example be household laundering but may also be industrial laundering. Furthermore, the invention relates to a process for laundering of fabrics and/or garments, where the process comprises treating fabrics with a washing solution _{containing a detergent composition and at least one lipase or lipase variant of the invention. The} cleaning process or a textile care process can for example be carried out in a machine washing or manually. The washing solution can for example be an aqueous washing solution containing a detergent composition. In one aspect, lipases or lipase variants of the invention are used in a cleaning process, _{e.g., a laundry process, that comprises a short wash cycle, typically a wash cycle of not more} _{than about 30 minutes, such as not more than about 20 minutes, e.g., not more than about 15} minutes or not more than about 10 minutes. In another aspect, the lipase or lipase variants of the invention are used in a cleaning _{process, e.g., a laundry process, where the wash water is used for more than one portion of} laundry. In this case, the wash water containing a detergent with a lipase or lipase variant of the invention may be used in a first wash cycle for a first portion of laundry, and then reused one or more times for additional wash cycles with new portions of laundry. The last few years there has been an increasing interest in replacing components in detergents that are derived from petrochemicals with renewable biological components such as enzymes and polypeptides without compromising the wash performance. When the components of detergent compositions change, new enzyme activities or new enzymes having alternative and/or improved properties compared to the previously used detergent enzymes such as proteases, lipases and amylases may be needed to achieve a similar or improved wash performance when compared to the traditional detergent compositions. The invention further concerns the use of lipases and lipase variants of the invention in a _{fat stain removing process. Fat stains may be stains such as food stains. In an embodiment the} invention relates to the use of a lipase or lipase variant of the invention or a composition of the invention in a cleaning process, preferably laundry or hard surface cleaning such as hand _{dishwashing (HDW) or automatic dishwashing (ADW). Finally, the invention relates to the use of} a lipase or lipase variant of the invention for hydrolyzing a lipase substrate. Washing or Cleaning Method The present invention provides a method of washing or cleaning a fabric, dishware or a hard surface with a detergent composition comprising a lipase or lipase variant of the invention. The method of washing or cleaning comprises contacting an object with a detergent composition comprising a lipase or lipase variant of the invention under conditions suitable for washing or cleaning the object. In a preferred embodiment the detergent composition is used in a laundry or a dish wash process. Another embodiment relates to a method for removing stains from fabric or dishware which comprises contacting the fabric or dishware with a composition comprising a lipase or lipase variant of the invention under conditions suitable for cleaning the object. In the method of cleaning of the invention, the object being cleaned may be any suitable object such as a textile or a hard surface such as dishware or a floor, table, wall, etc. A_{lso contemplated are compositions and methods of treating fabrics using a lipase or} lipase variant of the invention. For example, in one aspect, the feel and appearance of a fabric is _{improved by a method comprising contacting the fabric with a lipase or lipase variant in a solution.} In one aspect, the fabric is treated with the solution under pressure. The detergent compositions of the present invention are suited for use in laundry and hard surface applications, including such as hand dishwashing (HDW) or automatic dishwashing (ADW). Accordingly, the present invention includes a method for laundering a fabric or washing dishware, comprising contacting the fabric/dishware to be cleaned with a solution comprising the detergent composition according to the invention. The fabric may comprise any fabric capable of being laundered in normal consumer use conditions. The dishware may comprise any dishware such as crockery, cutlery, ceramics, plastics such as melamine, metals, china, glass and acrylics. The solution preferably has a pH from about 5.5 to about 11.5. The compositions may be employed at concentrations from about 100 ppm, preferably 500 ppm to about 15,000 ppm in solution. The water temperatures typically range from about 5°C to about 95°C, including about 10°C, about 15°C, about 20°C, about 25°C, about 30°C, about 35°C, about 40°C, about 45°C, _{about 50°C, about 55°C, about 60°C, about 65°C, about 70°C, about 75°C, about 80°C, about} 85°C and about 90°C. The water to fabric ratio is typically from about 1:1 to about 30:1. The enzyme(s) of the detergent composition of the invention may be stabilized using conventional stabilizing agents and inhibitors, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, different salts such as NaCl; KCl; lactic acid, formic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as _{4-formylphenyl boronic acid, or a peptide aldehyde such as di-, tri- or tetrapeptide aldehydes or} aldehyde analogues (either of the form B1-B0-R wherein, R is H, CH3, CX3, CHX2, or CH2X (X=halogen), B0 is a single amino acid residue (preferably with an optionally substituted aliphatic or aromatic side chain); and B1 consists of one or more amino acid residues (preferably one, two or three), optionally comprising an N-terminal protection group, or as described in WO 2009/118375, WO 98/13459) or a protease inhibitor of the protein type such as RASI, BASI, WASI (bifunctional alpha-amylase/subtilisin inhibitors of rice, barley and wheat) or CI2 or SSI. The composition may be formulated as described in, e.g., WO 92/19709, WO 92/19708 and US 6,472,364. In some embodiments, the enzymes employed herein are stabilized by the presence of water-soluble sources of zinc (II), calcium (II) and/or magnesium (II) ions in the finished compositions that provide such ions to the enzymes, as well as other metal ions (e.g., barium (II), scandium (II), iron (II), manganese (II), aluminum (III), Tin (II), cobalt (II), copper (II), Nickel (II), and oxovanadium (IV)). The detergent compositions provided herein are typically formulated such that, during use in aqueous cleaning operations, the wash water has a pH of from about 5.0 to about 12.5, such as from about 5.0 to about 11.5, or from about 6.0 to about 10.5. In some embodiments, granular or liquid laundry products are formulated to have a pH from about 6 to about 8. Techniques for controlling pH at recommended usage levels include the use of buffers, alkalis, acids, etc., and are well known to those skilled in the art. The present invention is further described by the following examples that should not be construed as limiting the scope of the invention. METHODS & MATERIALS W_{ild-type Lipase Donor Country of origin} _{SEQ ID NO: 1 Eleutherascus tuberculatus Netherlands (strain deposit # CBS 144.74)} _{SEQ ID NO: 2 Rhizoctonia solani Brazil} _{SEQ ID NO: 3 Westerdykella sp. China} _{SEQ ID NO: 4 Phlebiodontia subochracea Denmark} Method A: pNP assay for determination of lipase activity Enzymes can be assayed for lipase activity using the pNP assay described below. Principle The substrate pNP-substrate is hydrolyzed by the lipolytic enzyme under standard conditions. pNP-valerate is used as an example of a saturated short chain fatty acid. Valeric acid as the acyl group may be replaced by a long chain fatty acid such as oleic acid. Hydrolysis of the pNP-substrate results in a yellow solution, the absorbance of the solution meas- ured at 405 nm is a function of the activity of the lipolytic enzyme. By varying the pNP substrate the ratio between lipase activity on unsaturated substrates having long fatty acyl chains (e.g., oleic acid) to short acyl chain (e.g., p-nitrophenyl butyrate and/or p- nitrophenyl valerate) can be determined. Variation of substrate may call for adjustment of e.g., buffer system, adjustments that are easily within the purview of the skilled person. Lipase activity Enzymes are diluted in Buffer Substrate: The relevant pNP substrate (e.g. pNp-Valerate Sigma N-4377) 1 mM in Buffer pre- pared from stock-solution 100 mM in Methanol Buffer: 50 mM TRIS, 0,4% Triton X-100, is prepared to pH 7,7 _{Step Preparation} _{1 Substrate-stock is made to 100 mM in Methanol} 112 mg pNp-Valerate in 5 ml Methanol. This solution must be kept in a dark bottle or wrapped in aluminium foil to avoid daylight. The solution is to be kept at -18°C Prepare fresh every 2 weeks 2_{Enzymes are diluted to a concentration corresponding to Vmax < 70 mAbs/min} _{3 Substrate is prepared:} 0,1 ml pNp-Valerate Stock-solution 9,9 ml Buffer S_{tep Assay} _{1 Samples: Diluted enzyme 20 microL} pNP-substrate 150 microL 2_{Reference: Buffer 20 microL} pNP-substrate 150 microL Reference must be included in every assay 3_{The measurement is done as a kinetic measurement at 405 nm.} _{4 Setup:} Wavelength: 405 nm Time: 10:00 min. Interval 10 sec. Reads: 61 Automix: Once Lag time: 0 End time: 10:00 ODmin.: 0 ODmax: 2 5_{Result: Vmax calculated from measurement points} Results are calculated as: [Vmax (enzyme)-Vmax(buffer)] / [slope of standard curve] _{Microtiter plates (Thermo Scientific 26962096F without lid microwell plate) for plate reader spec-} trophotometers (Molecular Devices Spectramax 190) can conveniently be used for determination of lipase activity by standard methods based on use of paranitrophenol-esters. Method B: Active site titration of lipases and lipase variants Concentrations of micro-purified and conventionally purified lipases and lipase variants are determined by burst active site titration.100 µl lipase diluted in 0.01% Triton X-100 to 0.1 mg/mL (or 50 µl lipase diluted in 0.01% Triton X-100 to 0.1 mg/mL + 0.05 mL 0.01% Triton X-100) is mixed with 100 µl ethyl resorufinyl heptylphosphonate inhibitor dissolved in DSMA (3.8 mg/mL) further diluted with buffer (1 M Tris, 4 mM SDS, pH 7.0) to 0.016 mg/mL in the well of a black microtiter plate. Immediately after mixing kinetics of fluorescence from liberated resorufin is meas- ured every 1.5 minute for 5 hours (until bursts are finalized) (excitation at 515 nm, emission at 590 nm, measured on CLARIOstar (from BMG LABTECH). Measured fluorescences are fitted to the equation: F = F0 + Burst * (1-exp(-(t + dt) * ln(2) / T½) + Slope * (t + dt) where F is the measured fluorescence, F0 is the fluorescence background from inhibitor and lipase, t is the time since first fluorescence measurement, dt is the time from mixing of lipase with inhibitor to the first fluorescence measurement. Burst is the fluorescence burst, T½ is the half- time for the exponential burst, and Slope is the slope for the linear change in fluorescence e.g. due to hydrolysis of lipase-ethyl heptylphosphonate complex and/or bleaching of resorufin. From the calculated burst the active lipase concentration is determined using a resorufin standard curve (0-4 µM) included on the microtiter plate. Model detergent used in the experiments. The following model detergent was used in the experiments conducted to test the stability of the lipases and variants thereof: Model detergent C_{ompound Content of compound (% w/w)} _{SLS (sodium lauryl sulfate) 10.0} _{APG (alkylpolyglycoside) 8.0} _{Coco soap 4.0} _{GLDA (glutamic acid-N,N-diacetic acid) 1.5} _{Glycerol 5.0} _{MPG (monopropylene glycol) 2.0} Model detergent C_{ompound Content of compound (% w/w)} _{EtOH 5.0} CaCl2 0.06 N_{a-formate 0.5} _{KOH pH adjusted to about 8 (7.5 to 8.5)} _{H2O, ion exchanged Up to 100%} EXAMPLES Example 1 _{Half-life Improvement Factor (HIF) Determination} _{Each lipase and variants thereof were expressed in A. oryzae, grown in four independent} biological replicates in separate microtiter plates in defined media (MDU-2 w.10 mM NaNO₃), for 4 days at 37 °C in 96-well lidded MTPs without agitation. The expression plates also contained the parent lipases also expressed in A. oryzae. The filamentous material was removed by press- ing a Biopress® plate down into the wells. Expressed lipase variants in supernatants were diluted in dilution media (0.02% v/v Triton X-100 in H₂O), then dispensed into four quadrants per super- natant sample in a 384-well flat black microtiter plate. Model detergent was diluted to 0.2 % in 200 mM Tris-HCl, 15 °dH, pH 8.0. At four different timepoints ranging from 3 to 41 min, this Model detergent solution was dispensed to quadrant wells containing the diluted enzyme sample and shaken briefly. After the incubation period, assay solution (500 µM 4-methylumbelliferyl oleate (4-MU oleate) in 2.4 % v/v ethanol) was added, and the plate were read immediately using a Tecan Infinite M1000 using kinetic fluorescence meas- _{urements settings of λex 372 nm; λem 445 nm for 12 min. The output was saved (Vmax, R2) and} used for calculating half-life (T½), and initial activity, for data that passed quality filters. From linear fit of the logarithm of Vmax as a function of incubation time it was possible to derive the coefficient λ. Half-life were calculated using the equation T_½ = . Half-life improve- ment factors (HIF) were calculated by the ratio of the half-life variant and the half-life of cultivated references. The initial activity (Relative fluorescence units (RFU) min^-1) was calculated from the mean Vmax of the shortest incubation time in the detergent possible for each variant or reference. This was used as a quality threshold to disregard non-active variants. _{Half-life Improvement Factor (HIF) of the lipases and lipase variants were measured as} described above. Example 2 Half-life Improvement Factor (HIF) of variants compared to wildtype lipases shown in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, and SEQ ID NO: 4, respectively. T_{he assay in Example 1 was used for determining HIF. The Model detergent was used at} _{a dilution of 1%. SEQ ID NO: 1, SEQ ID NO. 2, SEQ ID NO: 3 and SEQ ID NO: 4, respectively,} _{were used as reference lipase for the Half-life Improvement Factor (HIF) calculation.} _{An increase in HIF reflects that the variant is more stable in detergent, i.e., have increased} detergent stability, both during wash and storage. The results show that the tested variants have increased stability compared to the respec- tive parent lipases. M_{utations relative to SEQ ID NO: 1 HIF} _{- 1.00} _{S467E 5.35} _{P116R 6.18} _{P468R 6.05} _{P468E 16.30} _{I71R 5.80} _{P443R 3.93} _{I442R 3.89} _{V15E 5.76} _{G72E 2.04} _{A395R 4.62} _{A395E 6.61} _{V446E 5.49} _{P390R 4.40} _{H125E 5.95} _{P18E 4.52} _{P18R 4.75} _{G441E 6.16} _{Q117E 5.43} _{L472E 3.38} _{W526R 5.14} _{T391R 3.93} _{T391E 7.37} _{Mutations relative to SEQ ID NO: 2 HIF} _{- 1.00} _{S500E 21.56} _{Y494E 30.49} _{Mutations relative to SEQ ID NO: 4 HIF} _{- 1.00} _{V83R 1.76} _{L75R 2.87} _{L71R 3.45} _{K193E 1.12} _{P45R+R437L 2.48} _{Y529E 1.05} _{Mutations relative to SEQ ID NO: 3 HIF} _{- 1.00} _{F517R 1.95} _{S489L+P515E 1.99} _{A55V+V514R 1.97} _{K530R 2.04} _{Q171R 2.33} _{Q171E 2.07} _{L38R 2.05} _{A371E 2.09} _{F374E 1.34} _{Y527E 1.31} _{K308E 1.90} _{K212E 2.56} Example 3 Half-life Improvement Factor (HIF) of variants compared to SEQ ID NO: 1, SEQ ID NO: 3 and SEQ ID NO: 4, respectively. T_{he assay in Example 1 was used for determining the HIF. Model detergent was used at} _{a dilution of 2%. SEQ ID NO: 1, SEQ ID NO. 2, SEQ ID NO: 3 and SEQ ID NO: 4, respectively,} were used as reference lipase for the Half-life Improvement Factor (HIF) calculation. _{An increase in HIF reflects that the variant is more stable in detergent, both during wash} and storage. The results show that the tested variants have increased stability compared to the refer- _{ence lipases shown in SEQ ID NO: 1, 3, and 4, respectively.} _{Mutations relative to SEQ ID NO: 1 HIF} _{- 1.00} _{S467E 1.52} _{P116R 5.96} _{P468R 2.81} _{P468E 2.33} _{S17E 8.91} _{I71R 4.66} _{P443R 2.08} _{P443E 2.60} _{I442R 3.03} _{V15E 2.23} _{G72E 1.40} _{A395R 3.86} _{A395E 1.10} _{V446E 2.75} _{P390R 1.02} _{H125E 1.28} _{P18E 1.58} _{G441E 2.94} _{L472E 1.79} _{D462A+L472E 2.43} _{W526R 2.73} _{T391R 1.11} _{P116D+P468K 3.39} _{P116R+A395D 9.98} _{G72E+A395K+G512D 2.67} _{G72E+A395K 2.68} _{P443R+S467D 3.07} _{A395K+L472E 2.56} _{T391E+A395D+P468K 3.85} _{Q117E+T391E+P443K 7.10} _{I71K+Q117E+T391E+A395K 2.94} _{Mutations relative to SEQ ID NO: 4 HIF} _{- 1.00} _{V83R 3.81} _{L75R 3.39} _{S70R+P72E+A73V+I79R+K81E+N84E 3.63} _{I79R+K81E+N84E 8.52} _{L90R 5.58} _{S70R+A73V+L75E+I79R+K81R+N84E 7.07} _{L90R 6.36} _{P72E+A73V+K81E+N84E 5.94} _{K81E+N84E 6.43} _{P72E+A73V+K81R+N84E 3.90} _{P72E+A73V+K81R+N84E+S359G 4.62} _{R437L+I443E 10.58} _{Mutations relative to SEQ ID NO: 3 HIF} _{- 1.00} _{F517R 1.39} _{S489L+P515E 1.54} _{A55V+V514R 1.50} _{Q171R 1.46} _{Q171E 1.82} _{L38R 1.00} _{A41R 1.41} Example 4 Half-life Improvement Factor (HIF) of wild-type lipases shown in SEQ ID NO: 1, SEQ ID NO: 2, _{SEQ ID NO: 3, and SEQ ID NO: 4, respectively, compared to the Geotrichum type} lipase shown in SEQ ID NO: 5. The assay in Example 1 was used for determining HIF. The Model detergent was used at a dilution of 0.2% or 2%. SEQ ID NO: 1, SEQ ID NO. 2, SEQ ID NO: 3 and SEQ ID NO: 4, _{respectively, were compared to reference wild-type lipase from Geotrichum candidum shown in} in SEQ ID NO: 5 for the Half-life Improvement Factor (HIF) calculation. An increase in HIF reflects that the wild-type lipases are more stable in detergent, i.e., have increased detergent stability, both during wash and storage. The results show that the tested _{lipases have increased stability compared to the reference lipase shown in SEQ ID NO: 5.} _{Lipase tested based on their SEQ ID NO HIF} HIF at 0.2% detergent at 2% detergent S_{EQ ID NO: 5 (reference) 1.00 1.00} _{SEQ ID NO: 1 51.87 3.87} _{SEQ ID NO: 2 51.12 N/A} _{SEQ ID NO: 3 5.13 2.10} _{SEQ ID NO: 4 10.25 0.84} Example 5 _{Half-life Improvement Factor (HIF) of variants in Neighboring positions of the target positions} _{compared to SEQ ID NO: 1 and SEQ ID NO: 4.} The assay in Example 1 was used for determining the HIF. The Model detergent was used at a dilution of 2%. SEQ ID NO: 1 and SEQ ID NO: 4, respectively, were used as reference lipase for _{the Half-life Improvement Factor (HIF) calculation (i.e., HIF = 1.00).} An increase in HIF reflects that the variant is more stable in detergent, both during wash and storage. _{The below results show that the tested variants have increased stability compared to the refer-} _{ence lipases shown in SEQ ID NO: 1 and 4, respectively.} _{Mutations relative to SEQ ID NO: 1 HIF} _{- 1.00} _{E13R 1.40} _{I19E 1.35} _{N21R 1.14} _{F24R 1.08} _{D69E 1.14} _{T74R 1.34} _{A114R 1.55} _{R115E 1.17} _{S129E 1.49} _{T328R 1.57} _{W333R 1.13} _{T388R 1.56} _{P392E 1.79} _{G394R 1.23} _{A440E 2.54} _{Y445E 2.32} _{G473E 1.84} _{K474R 3.34} _{R522E 3.00} _{Mutations relative to SEQ ID NO: 4 HIF} _{- 1.00} _{T86R 2.37} Example 6 _{Half-life Improvement Factor (HIF) of variants compared to SEQ ID NO: 1 and SEQ ID NO: 3} The assay in Example 1 was used for determining the HIF. The Model detergent was used at a dilution of 2%. SEQ ID NO: 1 and SEQ ID NO: 4, respectively, were used as reference lipase for _{the Half-life Improvement Factor (HIF) calculation (i.e., HIF = 1.00).} An increase in HIF reflects that the variant is more stable in detergent, both during wash and storage. _{The below results show that the tested variants have increased stability compared to the refer-} _{ence lipases shown in SEQ ID NO: 1 and 4, respectively.} _{Mutations relative to SEQ ID NO: 1 HIF} _{- 1.00} _{N122R 1.67} _{V351E 1.30} _{S352E 1.50} _{P353R 1.41} _{T354E 2.90} _{T354R 2.22} _{Mutations relative to SEQ ID NO: 3 HIF} _{- 1.00} Y76R 1.83 S_{325E 3.27} The invention is further defined by the following numbered paragraphs: 1. A lipase having i) a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, especially 1.00, compared to the three-dimensional structure of the lipase shown in any one of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 4, respectively, wherein the three-dimensional structure is calculated using Al- phaFold; and/or ii) a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, in particular 100% identity to the amino acid sequence of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 4, respectively; and iii) lipase activity. 2. The lipase of paragraph 1, wherein the lipase has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, com- pared to the three-dimensional structure of the lipase shown in SEQ ID NO: 1, but has a TM- score less than 1.00, such as less than 0.99, such as less than 0.98, such as less than 0.97 such as less than 0.96, such as less than 0.95 compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 5, wherein the three-dimensional structure is calculated using Al- phaFold; and wherein the lipase has lipase activity. 3. The lipase of paragraph 1, wherein the lipase has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, com- pared to the three-dimensional structure of the lipase shown in SEQ ID NO: 2, but has a TM- score less than 1.00, such as less than 0.99, such as less than 0.98, such as less than 0.97 such as less than 0.96, such as less than 0.95 compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 5, wherein the three-dimensional structure is calculated using Al- phaFold; and wherein the lipase has lipase activity. 4. The lipase of paragraph 1, wherein the lipase has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least _{0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, com-} pared to the three-dimensional structure of the lipase shown in SEQ ID NO: 3, but has a TM- score less than 1.00, such as less than 0.99, such as less than 0.98, such as less than 0.97 such as less than 0.96, such as less than 0.95 compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 5, wherein the three-dimensional structure is calculated using Al- phaFold; and wherein the lipase has lipase activity. 5. The lipase of paragraph 1, wherein the lipase has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least _{0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, com-} pared to the three-dimensional structure of the lipase shown in SEQ ID NO: 4, but has a TM- score less than 1.00, such as less than 0.99, such as less than 0.98, such as less than 0.97 such as less than 0.96, such as less than 0.95 compared to the three-dimensional structure of the lipase shown in SEQ ID NO: 5, wherein the three-dimensional structure is calculated using Al- phaFold; and wherein the lipase has lipase activity. 6. A variant of a parent lipase of any one of paragraphs 1-5, wherein the variant comprises a) one or more mutations at positions corresponding to positions: V15, S17, P18, I71, G72, P116, Q117, N122, H125, V351, S352, P353, T354, P390, T391, A395, G441, I442, P443, V446, S467, P468, L472, W526 of SEQ ID NO: 1, wherein position numbering is based on the numbering of SEQ ID NO: 1; b) one or more mutations on the surface of the lipase in SEQ ID NO: 1 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to SEQ ID NO: 1, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 1; and iii) the variant has lipase activity. 7. The variant of paragraph 6, wherein the variant comprises one or more mutations correspond- ing to: V15E,R, S17E,R, P18E,R, I71E,R, G72E,R, P116E,R, Q117E,R, N122E,R, H125E,R, V351E,R, S352E,R, P353E,R, T354E,R, P390E,R, T391E,R, A395E,R, G441E,R, I442E,R, P443E,R, V446E,R, S467E,R, P468E,R, L472E,R, W526E,R, in particular V15E, S17E, S17R, P18E, P18R, I71R, G72E, P116R, Q117E, N122R, H125E, V351E, S352E, P353R, T354E, T354R, P390R, T391R, T391E, A395R, A395E, G441E, I442R, P443E, P443R, V446E, S467E, P468R, P468E, L472E, W526R, D462A+L472E, W526R, T391R, T391E, P116D+P468K, P116R+A395D, G72E+A395K+G512D, G72E+A395K, P443R+S467D, A395K+L472E, T391E+A395D+P468K, Q117E+T391E+P443K, I71K+Q117E+T391E+A395K, wherein the position numbering is based on SEQ ID NO: 1. 8. The variant of any one of paragraphs 6 or 7, wherein the variant has an improved half-life Improvement Factor (HIF) compared to the parent lipase shown in SEQ ID NO: 1. _{9. The variant of any one of paragraphs 6-8, wherein one or more of the following positions on} the surface of the lipase in SEQ ID NO: 1 within 5Å of the positions corresponding to the positions _{in paragraph 6a) are mutated to Glu (E) or Arg (R): 3, 13, 16, 19, 20, 21, 24, 57, 67, 68, 69, 73,} 74, 114, 115, 119, 128, 129, 328, 333, 334, 388, 389, 392, 393, 394, 396, 434, 438, 440, 444, 445, 451, 452, 464, 465, 466, 469, 473, 474, 519, 522, 524, 527, 528, in particular P3E,R, E13R, H16E,R, I19E,T, F20E,R, N21E,R, F24E,R, K57E,R, G67E,R, S68E,R, D69E,R, F73E,R, T74E,R, A114E,R, R115E, N119E,R, Q128E,R, S129E,R, T328E,R, W333E,R, G334E,R, T388E,R, L389E,R, P392E,R, A393E,R, G394E,R, L396E,R, R434E, V438E,R, A440E,R, D444E,R, Y445E,R, F451E,R, Q452E,R, W464E,R, G465E,R, Y466E,R, S469E,R, G473E,R, K474E,R, _{E519R, R522E, R524E, V527E,R, E528R in SEQ ID NO: 1.} 10. The variant of any one of paragraphs 6-9, wherein one or more of the following positions on the surface of the lipase in SEQ ID NO: 1 within 4Å of the positions corresponding to the positions _{in paragraph 6a) are mutated to Glu (E) or Arg (R): 3, 16, 19, 20, 21, 24, 57, 68, 69, 73, 114, 115,} 119, 128, 129, 328, 333, 334, 389, 392, 393, 394, 396, 438, 440, 444, 445, 464, 465, 466, 469, 473, 474, 519, 522, 524, 527, 528, in particular P3E,R, H16E,R, I19E,R, F20E,R, N21E,F, F24E,R, K57E,R, S68E,R, D69E,R, F73E,R, A114E,R, R115E, N119E,R, Q128E,R, S129E,R, T328E,R, W333E,R, G334E,R, L389E,R, P392E,R, A393E,R, G394E,R, L396E,R, V438E,R, A440E,R, D444E,R, Y445E,R, W464E,R ,G465E,R, Y466E,R, S469E,R, G473E,R, K474E,R, E519R, _{R522E, R524E, V527E,R, E528R in SEQ ID NO: 1.} _{11. The variant of any one of paragraphs 6-10, wherein one or more of the following positions on} the surface of the lipase in SEQ ID NO: 1 within 3Å of the positions corresponding in the positions _{in paragraph 6a) are mutated to Glu (E) or Arg (R): 16, 19, 21, 24, 73, 115, 328, 389, 392, 393,} 394, 396, 440, 444, 445, 466, 469, 473, 527, in particular H16E,R, I19E,R, N21E,R, F24E,R, F73E,R, R115E, T328E,R, L389E,R, P392E,R, A393E,R, G394E,R, L396E,R, A440E,R, _{D444E,R, Y445E,R, Y466E,R, S469E,R, G473E,R, V527E,R in SEQ ID NO: 1.} 12. The variant of any one of paragraphs 6-10, wherein one or more of the following positions on the surface of the lipase in SEQ ID NO: 1 within 2Å of the positions corresponding in the positions _{in paragraph 6a) are mutated to Glu (E) or Arg (R): 16, 19, 73, 115, 389, 392, 394, 396, 440, 444,} 445, 466, 469, 473, 527, in particular H16E,R, I19E,R, F73E,R, R115E, L389E,R, P392E,R, _{G394E,R, L396E,R, A440E,R, D444E,R, Y445E,R, Y466E,R, S469E,R, G473E,R, V527E,R in} SEQ ID NO: 1. 13. A variant of a parent lipase of any one of paragraphs 1-5, wherein the variant comprises: a) one or more mutations at positions corresponding to positions: Y494 or S500 of SEQ ID NO: 2, wherein position numbering is based on the numbering of SEQ ID NO: 2; and/or b) one or more mutations on the surface of the lipase in SEQ ID NO: 2 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to SEQ ID NO: 2, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 2; and iii) the variant has lipase activity. 14. The variant of paragraph 13, wherein the variant comprises one or more mutations corre- _{sponding to: Y494E,R or S500E,R in particular Y494E or S500E of SEQ ID NO: 2, wherein the} position numbering is based on the numbering of SEQ ID NO: 2. 15. The variant of any one of paragraphs 13 or 14, wherein the variant has an improved half-life Improvement Factor (HIF) compared to the parent lipase shown in SEQ ID NO: 1. _{16. The variant of any one of paragraphs 13-15, wherein one or more of the following positions} on the surface of the lipase in SEQ ID NO: 2 within 5Å of the positions corresponding to the _{positions in paragraph 13a) are mutated to Glu (E) or Arg (R): 484, 487, 492, 493, 496, 499, 501,} 502, 513, in particular N484E,R, R487E, R492E, P493E,R, P496E,R, G499E,R, N501E,R, _{A502E,R, L513E,R in SEQ ID NO: 2.} 17. The variant of any one of paragraphs 13-16, wherein one or more of the following positions on the surface of the lipase in SEQ ID NO: 2 within 4Å of the positions corresponding to the _{positions in paragraph 13a) are mutated to Glu (E) or Arg (R): 484, 492, 493, 496, 499, 501, 502,} 513, in particular N484E,R, R492E, P493E,R, P496E,R, G499E,R, N501E,R, A502E,R, L513E,R in SEQ ID NO: 2. 18. The variant of any one of paragraphs 13-17, wherein one or more of the following positions on the surface of the lipase in SEQ ID NO: 2 within 3Å of the positions corresponding in the _{positions in paragraph 13a) are mutated to Glu (E) or Arg (R): 493, 496, 499, 501, in particular} _{P493E,R, P496E,R, G499E,R, N501E,R in SEQ ID NO: 2.} 19. The variant of any one of paragraphs 13-18, wherein one or more of the following positions on the surface of the lipase in SEQ ID NO: 2 within 2Å of the positions corresponding in the _{positions in paragraph 13a) are mutated to Glu (E) or Arg (R): 493, 499, 501, in particular} _{P493E,R, G499E,R, N501E,R in SEQ ID NO: 2.} 20. A variant of a parent lipase of any one of paragraphs 1-5, wherein the variant comprises: a) one or more mutations at positions corresponding to positions: _{L38, A41, Y76, Q171, Y176, K212, K308, S325, A371, F374, V514, P515, F517, Y527, K530 of} SEQ ID NO: 3, wherein position numbering is based on the numbering of SEQ ID NO: 3; b) one or more mutations on the surface of the lipase in SEQ ID NO: 3 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferred within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to SEQ ID NO: 3, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 3; and iii) the variant has lipase activity. 21. The variant of paragraph 20, wherein the variant comprises one or more mutations corres- _{ponding to: L38E,R, A41E,R, Y76E,R, Q171E,R, Q171E,R, Y176E,R, K212E,R, S325E,R,} _{A371E,R, F374E,R, K308E,R, V514E,R, P515E,R, F517E,R, Y527E,R, K530E,R, in particular} _{L38R, A41R, Y76R, Q171R, Q171E, Y176E, K212E, S325E, A371E, F374E, K308E, V514R,} P515E, F517R, Y527E, K530R, A55V+V514R, S489L+P515E of SEQ ID NO: 3, wherein the po- sition numbering is based on the numbering of SEQ ID NO: 3. 22. The variant of any one of paragraphs 20 or 21, wherein the variant has improved Half-life Improvement Factor (HIF) compared to the parent lipase shown in SEQ ID NO: 3. 23. The variant of any one of paragraphs 20-22, wherein one or more of the following positions on the surface of the lipase in SEQ ID NO: 3 within 5Å of the positions corresponding to the _{positions in paragraph 20a) are mutated to Glu (E) or Arg (R): 32, 33, 35, 36, 37, 42, 43, 44, 157,} 158, 168, 174, 175, 178, 179, 208, 211, 213, 260, 306, 307, 309, 310, 368, 369, 370, 372, 373, 375, 376, 382, 389, 429, 446, 447, 512, 513, 516, 518, 519, 525, 526, 528, 529, 531, 532, in particular A32E,R, A33E,R, L35E,R, G36E,R, N37E,R, A42E,R, P43E,R, K44E,R, G157E,R, A158E,R, F168E,R, Q174E,R, R175E, Q178E,R, K179E,R, G208E,R, D211E,R, V213E,R, R260E, A306E,R, V307E,R, G309E,R, K310E,R, D368E,R, L369E,R, S370E,R, P372E,R, L373E,R, D375E,R, T376E,R, P382E,R, V389E,R, Q429E,R, T446E,R, T447E,R, G512E,R, G513E,R, V516E,R, N518E,R, E519R, K525E,R, Y526E,R, T528E,R, Y529E,R, D531E,R, _{P532E,R in SEQ ID NO: 3.} 24. The variant of any one of paragraphs 20-23, wherein one or more of the following positions on the surface of the lipase in SEQ ID NO: 3 within 4Å of the positions corresponding to the _{positions in paragraph 20a) are mutated to Glu (E) or Arg (R): 32, 33, 35, 36, 37, 42, 43, 44, 158,} 168, 174, 175, 178, 179, 211, 213, 307, 309, 368, 369, 370, 372, 373, 375, 376, 389, 429, 447, 513, 516, 518, 519, 525, 526, 528, 529, 531, 532, in particular A32E,R, A33E,R, L35E,R, G36E,R, N37E,R, A42E,R, P43E,R, K44E,R, A158E,R, F168E,R, Q174E,R, R175E, Q178E,R, K179E,R, D211E,R, V213E,R, V307E,R, G309E,R, D368E,R, L369E,R, S370E,R, P372E,R, L373E,R, D375E,R, T376E,R, V389E,R, Q429E,R, T447E,R, G513E,R, V516E,R, N518E,R, E519R, _{K525E,R, Y526E,R, T528E,R, Y529E,R, D531E,R, P532E,R in SEQ ID NO: 3.} 25. The variant of any one of paragraphs 20-24, wherein one or more of the following positions _{on the surface of the lipase in SEQ ID NO: 3 within 3Å of the positions corresponding in the} _{positions in paragraph 20a) are mutated to Glu (E) or Arg (R): 35, 37, 42, 175, 178, 179, 211, 213,} 307, 309, 370, 372, 373, 375, 513, 516, 518, 526, 528, 529, 531, in particular L35E,R, N37E,R, A42E,R, R175E, Q178E,R, K179E,R, D211E,R, V213E,R, V307E,R, G309E,R, S370E,R, P372E,R, L373E,R, D375E,R, G513E,R, V516E,R, N518E,R, Y526E,R, T528E,R, Y529E,R, _{D531E,R in SEQ ID NO: 3.} 26. The variant of any one of paragraphs 20-25, wherein one or more of the following positions on the surface of the lipase in SEQ ID NO: 3 within 2Å of the positions corresponding in the _{positions in paragraph 20a) are mutated to Glu (E) or Arg (R): 37, 42, 175, 211, 213, 307, 309,} 370, 372, 373, 375, 513, 516, 518, 526, 528, 529, 531, in particular N37E,R, A42E,R, R175E, D211E,R, V213E,R, V307E,R, G309E,R, S370E,R, P372E,R, L373E,R, D375E,R, G513E,R, _{V516E,R, N518E,R, Y526E,D, T528E,R, Y529E,R, D531E,R in SEQ ID NO: 3.} 27. A variant of a parent lipase of any one of paragraphs 1-5, wherein the variant comprises a) one or more mutations at positions corresponding to positions: P45, S70, L71, P72, L75, I79, K81, V83, N84, L90, K193, L397, I443, Y529 of SEQ ID NO: 4 wherein position numbering is based on the numbering of SEQ ID NO: 4; b) one or more mutations on the surface of the lipase in SEQ ID NO: 4 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to SEQ ID NO: 4, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 4; and iii) the variant has lipase activity. 28. The variant of paragraph 27, wherein the variant comprises mutations corresponding to: P45R, S70E, S70R, L71R, P72E, L75R, L75E, I79R, K81E, K81R, V83R, N84E, L90R, K193E, I443E, Y529E, S70R+P72E+A73V+I79R+K81E+N84E, I79R+K81E+N84E, _{S70R+A73V+L75E+I79R+K81R+N84E, P72E+A73V+K81E+N84E, K81E+N84E,} P72E+A73V+K81R+N84E, P72E+A73V+K81R+N84E+S359G, R437L+I443E of SEQ ID NO: 4; wherein the position numbering is based on the numbering of SEQ ID NO: 4. 29. The variant of any one of paragraphs 27 or 28, wherein the variant has improved Half-life Improvement Factor (HIF) compared to the parent lipase shown in SEQ ID NO: 4. _{30. The variant of any one of paragraphs 27-29, wherein one or more of the following positions} on the surface of the lipase in SEQ ID NO: 4 within 5Å of the positions corresponding to the _{positions in paragraph 27a) are mutated to Glu (E) or Arg (R): 8, 32, 43, 44, 46, 47, 67, 68, 69,} 73, 74, 76, 77, 78, 80, 82, 85, 86, 87, 88, 89, 91, 92, 93, 135, 186, 189, 192, 194, 196, 293, 344, _{346, 365, 366, 367, 395, 396, 398, 402, 441, 442, 527, 528, 530, 531 in particular A18E,R,} Q32E,R, P43E,R, A44E,R, N46E,R, S47E,R, N67E,R, G68E,R, P69E,R, A73E,R, N74E,R, P76E,R, P77E,R, S78E,R, V80E,R, I82E,R, E85E,R, T86E,R, F87E,R, G88E,R, L89QE,R, P91E,R, T92E,R, R93E, Y135E,R, L186E,R, R189E, Q192E,R, Y194E,R, S196E,R, F293E,R, _{Q344E,R, S346E,R, Q365E,R, A366E,R, P367E,R, Q395E,R, E396R, G398E,R, K402E,R,} _{L441E,R, P442E,R, L527E,R, A528E,R, P530E,R, L531E,R in SEQ ID NO: 4.} 31. The variant of any one of paragraphs 27-30, wherein one or more of the following positions _{on the surface of the lipase in SEQ ID NO: 4 within 4Å of the positions corresponding to the} _{positions in paragraph 27a) are mutated to Glu (E) or Arg (R): 32, 44, 46, 47, 68, 69, 73, 74, 76,} 77, 78, 80, 82, 85, 86, 87, 88, 89, 91, 92, 93, 186, 189, 192, 194, 344, 346, 365, 366, 367, 395, 396, 398, 402, 441, 442, 527, 528, 530, 531, in particular Q32E,R, A44E,R, N46E,R, S47E,R, G68E,R, P69E,R, A73E,R, N74E,R, P76E,R, P77E,R, S78E,R, V80E,R, I82E,R, E85R, T86E,R, F87E,R, G88E,R, L89E,R, P91E,R, T92E,R, R93E, L186E,R, R189E, Q192E,R, Y194E,R, _{Q344E,R, S346E,R, Q365E,R, A366E,R, P367E,R, Q395E,R, E396R, G398E,R, K402E,R,} _{L441E,R, P442E,R, L527E,R, A528E,R, P530E,R, L531E,R in SEQ ID NO: 4.} _{32. The variant of any one of paragraphs 27-31, wherein one or more of the following positions} on the surface of the lipase in SEQ ID NO: 4 within 3Å of the positions corresponding in the _{positions in paragraph 27a) are mutated to Glu (E) or Arg (R): 44, 46, 69, 73, 74, 76, 78, 80, 82,} 85, 87, 88, 89, 91, 189, 192, 194, 344, 396, 398, 442, 528, 530, in particular A44E,R, N46E,R, P69E,R, A73E,R, N74E,R, P76E,R, S78E,R, V80E,R, I82E,R, E85R, F87E,R, G88E,R, L89E,R, _{P91E,R, R189E, Q192E,R, Y194E,R, Q344E,R, E396R, G398E,R, P442E,R, A528E,R, P530E,R} in SEQ ID NO: 4. 33. The variant of any one of paragraphs 27-32, wherein one or more of the following positions on the surface of the lipase in SEQ ID NO: 4 within 2Å of the positions corresponding in the _{positions in paragraph 27a) are mutated to Glu (E) or Arg (R): 44, 46, 69, 73, 74, 76, 78, 80, 82,} 85, 89, 91, 192, 194, 396, 398, 442, 528, 530, in particular A44E,R, N46E,R, P69E,R, A73E,R, N74E,R, P76E,R, S78E,R, V80E,R, I82E,R, E85R, L89E,R, P91E,R, T92E,R, Y194E,R, E396R, _{G398E,R, P442E,R, A528E,R, P530E,R in SEQ ID NO: 4.} 34. The variant of any one of paragraphs 6-33, wherein the parent has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, especially 1.00, compared to the three-dimensional structure of the lipase shown in any one of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 4, respectively, wherein the three-dimensional structure is calculated using AlphaFold; and wherein the lipase has lipase activity. 35. The variant of any one of paragraphs 6-34, having a HIF above 1.00, above 1.10, in particular above 1.50, above 2.00, above 2.50, above 3.00, above 3.50, above 4.00, above 5.00, above 6.00, above 7.00, above 8.00, above 9.00, above 10.00, above 11.00, above 12.00, above 13.00, above 14.00, above 15.00, above 16.00, above 17.00, above 18.00, above 19,00, above 20.00, above 21.00, above 22.00, above 23.00, above 24.00, above 25.00, above 26.00, above 27.00, above 28.00, above 29.00, above 30.00 such as between 1.00 and 30.00, such as between 2.00 and 25.00, such as between 3.00 and 20.00, such as between 4.00 and 15,00, such as between 5.00 and 10.00. 36. The variant according to any one of paragraphs 6-35, wherein the parent lipase is selected from the group consisting of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, and SEQ ID NO:4. 37. A polynucleotide encoding a lipase according to paragraphs 1-5 or a lipase variant ac- cording to any of paragraphs 6-36. 38. A nucleic acid construct or expression vector comprising a polynucleotide of paragraph 37. _{39. A recombinant host cell comprising in its genome a nucleic acid construct or expression} vector according to paragraph 38. 40. A method for obtaining a lipase variant according to any of paragraphs 6-36, comprising (a) introducing into a parent lipase according to any one of paragraph 1-5 one or more mutations _{at positions according to paragraphs 6-36 and optionally further introducing mutations at at least} one, two, three, e.g., at least four, at least five, at least six, at least seven, at least eight, or nine positions; and (b) optionally recovering the lipase variant. 41. A method of producing a lipase according to any one of paragraphs 1-5 or a variant ac- cording to any of paragraphs 6-36, comprising (a) cultivating the recombinant host cell of paragraph 39 under conditions suitable for expression of a lipase of any one of paragraphs 1-5 or a variant of any one of paragraphs 6-36; and (b) optionally recovering the lipase or lipase variant. 42. A composition comprising a lipase according to any one of paragraphs 1-5 or a variant according to any of paragraphs 6-36. 43. The composition according to paragraph 42, wherein the composition further comprises a surfactant; preferably wherein the composition is a detergent or cleaning composition in the form _{of a bar, a homogeneous tablet, a tablet having two or more layers, a pouch having one or more} compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact, or concentrated liquid. 44. A method of cleaning an object, comprising contacting an object with a composition ac- cording to paragraphs 42 or 43 under conditions suitable for cleaning the object; preferably wherein the object is a textile, dishware, or a hard surface; most preferably wherein the object is a textile. 45. Use of a lipase according to any one of paragraphs 1-5 or variant according to any of paragraphs 6-36 or a composition according to paragraph 42 or 43 in a cleaning process, prefer- _{ably laundry or hard surface cleaning such as hand dishwashing (HDW) or automatic dishwashing} (ADW). 46. Use of a lipase according to any one of paragraphs 1-5 or variant according to any of paragraphs 6-36 for hydrolyzing a lipase substrate. The invention described and claimed herein is not to be limited in scope by the specific aspects herein disclosed, since these aspects are intended as illustrations of several aspects of the invention. Any equivalent aspects are intended to be within the scope of this invention. Indeed, various modifications of the invention in addition to those shown and described herein will become apparent to those skilled in the art from the foregoing description. Such modifications are also intended to fall within the scope of the appended claims. In the case of conflict, the present disclosure including definitions will control.

Claims

CLAIMS 1. A lipase having i) a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, especially 1.00, compared to the three-dimensional structure of the lipase shown in any one of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or S_{EQ ID NO: 4, respectively, wherein the three-dimensional structure is calculated using Al-} phaFold; and/or ii) a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, in particular 100% identity to the amino acid sequence of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 4, respectively; and iii) lipase activity.

2. A variant of a parent lipase of claim 1, wherein the variant comprises a) one or more mutations at positions corresponding to positions: V15, S17, P18, I71, G72, P116, Q117, N122, H125, V351, S352, P353, T354, P390, T391, A395, G441, I442, P443, V446, S467, P468, L472, W526 of SEQ ID NO: 1, wherein position numbering is based on the numbering of SEQ ID NO: 1; b) one or more mutations on the surface of the lipase in SEQ ID NO: 1 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to SEQ ID NO: 1, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 1; and iii) the variant has lipase activity.

3. A variant of a parent lipase of claim 1, wherein the variant comprises: a) one or more mutations at positions corresponding to positions: _{Y494 or S500 of SEQ ID NO: 2, wherein the position numbering is based on the numbering of} SEQ ID NO: 2; and/or b) one or more mutations on the surface of the lipase in SEQ ID NO: 2 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at l_{east 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to} SEQ ID NO: 2, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 2; and iii) the variant has lipase activity.

4. A variant of a parent lipase of claim 1, wherein the variant comprises: a) one or more mutations at positions corresponding to positions: _{L38, A41, Y76, Q171, Y176, K212, K308, S325, A371, F374, V514, P515, F517, Y527, K530 of} SEQ ID NO: 3, wherein the position numbering is based on the numbering of SEQ ID NO: 3; b) one or more mutations on the surface of the lipase in SEQ ID NO: 3 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferred within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at l_{east 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to} SEQ ID NO: 3, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 3; and iii) the variant has lipase activity.

5. A variant of a parent lipase of claim 1, wherein the variant comprises a) one or more mutations at positions corresponding to positions: P45, S70, L71, P72, L75, I79, K81, V83, N84, L90, K193, L397, I443, Y529 of SEQ ID NO: 4 wherein position numbering is based on the numbering of SEQ ID NO: 4; b) one or more mutations on the surface of the lipase in SEQ ID NO: 4 within 5Å, preferably within 4Å, more preferably within 3Å, even more preferably within 2Å of the positions corresponding to the positions in a); wherein i) the variant has a TM-score of at least 0.80, e.g., at least 0.81, at least 0.82, at least 0.83, at least 0.84, at least 0.85, at least 0.86, at least 0.87, at least 0.88, at least 0.89, at least 0.90, at least 0.91, at least 0.92, at least 0.93, at least 0.94, at least 0.95, at least 0.96, at least 0.97, at least 0.98, at least 0.99, at least 0.995, at least 0.999, but less than 1.0 to SEQ ID NO: 4, compared to the three-dimensional structure of the parent lipase, wherein the three-dimensional structure is calculated using AlphaFold; and/or ii) the variant lipase has a sequence identity of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, at least 99%, but less than 100% to the amino acid sequence of SEQ ID NO: 4; and iii) the variant has lipase activity.

6. A polynucleotide encoding a lipase according to claim 1 or a lipase variant according to any of claims 2-5.

7. A nucleic acid construct or expression vector comprising a polynucleotide of claim 6. _{8. A recombinant host cell comprising a nucleic acid construct or expression vector accord-} ing to claim 7. 9. A method for obtaining a lipase variant according to any of claims 2-5, comprising _{(a) introducing into a parent lipase according to claim 1 one or more mutations at positions ac-} _{cording to claims 2-5 and optionally further introducing mutations at at least one, two, three, e.g.,} at least four, at least five, at least six, at least seven, at least eight, or nine positions; and (b) optionally recovering the lipase variant. 10. A method of producing a lipase according to claim 1 or a variant according to any of claims 2-5, comprising _{(a) cultivating the recombinant host cell of claim 8 under conditions suitable for expression of a} _{lipase of claim 1 or a variant of any one of claims 2-5; and (b) recovering the lipase or lipase} variant. 11. A composition comprising a lipase according to claim 1 or a variant according to any of claims 2-5. 12. The composition according to claim 11, wherein the composition further comprises a surfac- _{tant; preferably wherein the composition is a detergent or cleaning composition in the form of a} bar, a homogeneous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact, or concentrated liquid. 13. A method of cleaning an object, comprising contacting an object with a composition ac- _{cording to claims 11 or 12 under conditions suitable for cleaning the object; preferably wherein} the object is a textile, dishware, or a hard surface; most preferably wherein the object is a textile. _{14. Use of a lipase according to claim 1 or variant according to any of claims 2-5 or a compo-} _{sition according to claim 11 or 12 in a cleaning process, preferably laundry or hard surface clean-} ing such as hand dishwashing (HDW) or automatic dishwashing (ADW). _{15. Use of a lipase according to claim 1 or a variant according to any of claims 2-5 for hydro-} lyzing a lipase substrate.