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WO2024213513A1 - Compositions comprenant des polypeptides ayant une activité de phosphatase alcaline - Google Patents

Compositions comprenant des polypeptides ayant une activité de phosphatase alcaline Download PDF

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Publication number
WO2024213513A1
WO2024213513A1 PCT/EP2024/059495 EP2024059495W WO2024213513A1 WO 2024213513 A1 WO2024213513 A1 WO 2024213513A1 EP 2024059495 W EP2024059495 W EP 2024059495W WO 2024213513 A1 WO2024213513 A1 WO 2024213513A1
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Prior art keywords
seq
polypeptide
alkaline phosphatase
phosphatase activity
sequence identity
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PCT/EP2024/059495
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English (en)
Inventor
Lilian Eva Tang Baltsen
Bartlomiej Maciej KOLACZKOWSKI
Katrine THYGESEN
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Novozymes AS
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Novozymes AS
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Priority to AU2024252152A priority Critical patent/AU2024252152A1/en
Priority to KR1020257037820A priority patent/KR20250174069A/ko
Priority to CN202480028810.XA priority patent/CN121039266A/zh
Publication of WO2024213513A1 publication Critical patent/WO2024213513A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • C12N9/22—Ribonucleases [RNase]; Deoxyribonucleases [DNase]
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/12—Soft surfaces, e.g. textile
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/14—Hard surfaces
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y301/00—Hydrolases acting on ester bonds (3.1)
    • C12Y301/03—Phosphoric monoester hydrolases (3.1.3)
    • C12Y301/03001—Alkaline phosphatase (3.1.3.1)

Definitions

  • the present invention relates to polypeptides having alkaline phosphatase activity, to compositions such as cleaning compositions comprising a polypeptide having alkaline phosphatase activity and optionally a polypeptide having DNase activity, and to cleaning methods using the polypeptides and compositions.
  • washing solutions for example in laundry, there will be a mix of different soil particles present, including both organic molecules originating from living organisms and inorganic molecules.
  • Such washing solutions will invariably contain phosphate ions, which are especially important in physiology of various organisms because of their multifactorial roles.
  • phosphorylation is an intrinsic mode of action for signaling activation or deactivation of enzymes and other peptides.
  • Phospholipids are key components of cell membranes, and the DNA backbone contains phosphate groups in its structural framework. Both types of molecules are present in human and microbial cells as well as cell debris.
  • organophosphates are associated with mineral surface induced adsorption and precipitation. In a laundry washing situation most of them will be dissolved and kept in solution by the surfactants, but in some cases organophosphates are exposed to the surrounding water hardness ions such as calcium and magnesium. These ions and similar di- and trivalent cations are prone to sequestering together with the organophosphates. This happens especially by way of ion bridging with other phosphate groups or with acids of other types of functional groups in proteins and fatty acids.
  • Biofilm EPS is a polymeric conglomeration generally composed of extracellular DNA, proteins and polysaccharides.
  • extracellular DNA eDNA
  • eDNA extracellular DNA
  • DNase enzymes are known for use in e.g. laundry detergents.
  • One situation where organophosphates are exposed during wash is in connection of degradation of DNA with DNase enzymes. Hydrolysis by DNase produces 5’ ends of DNA fragments, which will tend to form ion bridging with other functional groups.
  • fatty acids become suspended in the wash solution - either by release of soil or as part of the detergent formulation - they may precipitate with DNA that has been degraded with DNase, most probably due to the formation of large molecules that are difficult to keep in solution. Such precipitation can be problematic and may result in reduced cleaning performance and/or redeposition of soil on laundry items.
  • WO 99/10466 purportedly discloses cleaning compositions comprising a phosphatase, although there are no working examples in this document, and no indication of the nature of phosphatases other than that they are said to encompass the alkaline phosphatase EC 3.1.3.1 and the acid phosphatase 3.1.3.2.
  • ALP alkaline phosphatase
  • the present invention provides in one aspect a cleaning composition
  • a cleaning composition comprising a polypeptide having DNase activity, a polypeptide having alkaline phosphatase activity and at least one detergent adjunct ingredient.
  • the invention provides a cleaning composition comprising a polypeptide having alkaline phosphatase activity and at least one detergent adjunct ingredient, wherein the polypeptide having alkaline phosphatase activity is selected from the group consisting of:
  • polypeptide derived from the polypeptide of (a) or (b), wherein the N- and/or C- terminal end has been extended by the addition of 1 to 50 amino acids, such as 1 to 40, 1 to 30 or 1 to 20 amino acids; and
  • SEQ ID NO: 1 is a polypeptide obtained from Neobacillus bataviensis having alkaline phosphatase activity.
  • SEQ ID NO: 2 is a polypeptide obtained from Parageobacillus caldoxylosilyticus having alkaline phosphatase activity.
  • SEQ ID NO: 3 is a polypeptide obtained from Geobacillus thermoleovorans having alkaline phosphatase activity.
  • SEQ ID NO: 4 is a polypeptide obtained from Sporolactobacillus sp. having alkaline phosphatase activity.
  • SEQ ID NO: 5 is a polypeptide obtained from Anoxybacillus caldiproteolyticus having alkaline phosphatase activity.
  • SEQ ID NO: 6 is a polypeptide obtained from Geobacillus thermoleovorans having alkaline phosphatase activity.
  • SEQ ID NO: 7 is a polypeptide obtained from Paenibacillus xylanexedens having alkaline phosphatase activity.
  • SEQ ID NO: 8 is a polypeptide obtained from Sporolactobacillus sp. having alkaline phosphatase activity.
  • SEQ ID NO: 9 is a polypeptide obtained from Paenibacillus panacisoli having alkaline phosphatase activity.
  • SEQ ID NO: 10 is a polypeptide obtained from Collimonas pratensis having alkaline phosphatase activity.
  • SEQ ID NO: 11 is a polypeptide obtained from Paenibacillus illinoisensis having alkaline phosphatase activity.
  • SEQ ID NO: 12 is a polypeptide obtained from Aeromonas salmonicida subsp. salmonicida having alkaline phosphatase activity.
  • SEQ ID NO: 13 is a polypeptide obtained from Paenibacillus amylolyticus having alkaline phosphatase activity.
  • SEQ ID NO: 14 is a polypeptide obtained from Serratia plymuthica having alkaline phosphatase activity.
  • SEQ ID NO: 15 is a polypeptide obtained from Cytobacillus firmus having alkaline phosphatase activity.
  • SEQ ID NO: 16 a polypeptide obtained from Priestia megaterium having alkaline phosphatase activity.
  • SEQ ID NO: 17 is a polypeptide obtained from Trichoderma citrinoviride having alkaline phosphatase activity.
  • SEQ ID NO: 18 is a polypeptide obtained from Truncatella angustata having alkaline phosphatase activity.
  • SEQ ID NO: 19 is a polypeptide obtained from Morchella semilibera having alkaline phosphatase activity.
  • SEQ ID NO: 20 is a polypeptide obtained from Serratia ficaria having alkaline phosphatase activity.
  • SEQ ID NO: 21 a polypeptide obtained from a metagenome having alkaline phosphatase activity.
  • SEQ ID NO: 22 a polypeptide obtained from a metagenome having alkaline phosphatase activity.
  • SEQ ID NO: 23 is a polypeptide obtained from a metagenome having alkaline phosphatase activity.
  • SEQ ID NO: 24 is a polypeptide obtained from a metagenome having alkaline phosphatase activity.
  • SEQ ID NO: 25 is a polypeptide obtained from a metagenome having alkaline phosphatase activity.
  • SEQ ID NO: 26 a polypeptide obtained from a metagenome having alkaline phosphatase activity.
  • SEQ ID NO: 27 is a polypeptide obtained from Sporormia fimetaria having alkaline phosphatase activity.
  • SEQ ID NO: 28 is a polypeptide obtained from Thermoascus crustaceus having alkaline phosphatase activity.
  • SEQ ID NO: 29 is a polypeptide obtained from Thielavia australiensis having alkaline phosphatase activity.
  • SEQ ID NO: 30 is a polypeptide obtained from Chaetomium thermophilum var. thermophilum having alkaline phosphatase activity.
  • SEQ ID NO: 31 is a polypeptide obtained from Aspergillus sp. having alkaline phosphatase activity.
  • SEQ ID NO: 32 is a polypeptide obtained from Colletotrichum sp. having alkaline phosphatase activity.
  • SEQ ID NO: 33 is a polypeptide obtained from chicken cecum having alkaline phosphatase activity.
  • SEQ ID NO: 34 is a polypeptide obtained from a metagenome having alkaline phosphatase activity.
  • SEQ ID NO: 35 is a polypeptide obtained from Caulobacter sp. having alkaline phosphatase activity.
  • SEQ ID NO: 36 is a polypeptide obtained from Caulobacter vibrioides having alkaline phosphatase activity.
  • SEQ ID NO: 37 is a polypeptide obtained from Serratia nematodiphila having alkaline phosphatase activity.
  • SEQ ID NO: 38 is a polypeptide obtained from Loktanella salsilacus having alkaline phosphatase activity.
  • SEQ ID NO: 39 is a polypeptide obtained from Sphingopyxis chilensis having alkaline phosphatase activity.
  • SEQ ID NO: 40 is a polypeptide obtained from Tolypocladium sp. having alkaline phosphatase activity.
  • SEQ ID NO: 41 is a polypeptide obtained from Penicillium vasconiae having alkaline phosphatase activity.
  • SEQ ID NO: 42 is a polypeptide obtained from Cladobotryum sp. having alkaline phosphatase activity.
  • SEQ ID NO: 43 is a polypeptide obtained from Taifanglania sp. having alkaline phosphatase activity.
  • SEQ ID NO: 44 is a polypeptide obtained from Achaetomium sp. having alkaline phosphatase activity.
  • SEQ ID NO: 45 is a polypeptide obtained from Chaetomium sp. having alkaline phosphatase activity.
  • SEQ ID NO: 46 is a polypeptide obtained from Fontibacillus aquaticus having alkaline phosphatase activity.
  • SEQ ID NO: 47 is a polypeptide obtained from Paenibacillus sp. having alkaline phosphatase activity.
  • SEQ ID NO: 48 is a polypeptide obtained from Paenibacillus sp. having alkaline phosphatase activity.
  • SEQ ID NO: 49 is a polypeptide obtained from Paenibacillus woosongensis having alkaline phosphatase activity.
  • SEQ ID NO: 50 is a polypeptide obtained from Lederbergia lenta having alkaline phosphatase activity and is the polypeptide described in LIS20180326020.
  • SEQ ID NO: 51 is a polypeptide obtained from a metagenome having alkaline phosphatase activity.
  • SEQ ID NO: 52 is a polypeptide obtained from Paenibacillus sp. having alkaline phosphatase activity.
  • SEQ ID NO: 53 is a polypeptide obtained from Paenibacillus castaneae having alkaline phosphatase activity.
  • SEQ ID NO: 54 is a polypeptide obtained from Paenibacillus taohuashanense having alkaline phosphatase activity.
  • SEQ ID NO: 55 is a polypeptide obtained from Hyphomonas hirschiana having alkaline phosphatase activity.
  • SEQ ID NO: 56 is a polypeptide obtained from Hyphomonas oceanitis having alkaline phosphatase activity.
  • SEQ ID NO: 57 is a polypeptide obtained from Deinococcus radiodurans having alkaline phosphatase activity.
  • SEQ ID NO: 58 is a polypeptide obtained from Deinococcus gobiensis having alkaline phosphatase activity.
  • SEQ ID NO: 59 is a polypeptide obtained from Deinococcus pimensis having alkaline phosphatase activity.
  • SEQ ID NO: 60 is a polypeptide obtained from Deinococcus sp. having alkaline phosphatase activity.
  • SEQ ID NO: 61 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 62 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 63 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 64 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 65 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 66 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 67 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 68 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 69 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 70 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 71 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 72 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 73 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 74 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 75 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 76 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 77 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 78 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 79 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 80 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 81 is a variant of SEQ ID NO: 1 having alkaline phosphatase activity.
  • SEQ ID NO: 82 is a polypeptide having DNase activity obtained from Metabacillus indicus.
  • SEQ ID NO: 83 is a variant of SEQ ID NO: 82 having DNase activity.
  • SEQ ID NO: 84 is a Bacillus clausii secretion signal.
  • SEQ ID NO: 85 is a His-tag.
  • SEQ ID NO: 86 is a polypeptide having DNase activity obtained from Aspergillus oryzae.
  • Alkaline phosphatase means a polypeptide having alkaline phosphatase activity that catalyzes the hydrolysis of phosphate monoesters at basic pH values.
  • Alkaline phosphatases belong to the esterases (EC number 3.1), which is a subgroup of the hydrolases, and specifically the phosphoric monoester hydrolases (EC number 3.1.3).
  • the alkaline phosphatases are classified in EC 3.1.3.1 and remove phosphate groups from different types of molecules.
  • alkaline phosphatase activity may be determined according to the alkaline phosphatase activity assay in the examples.
  • alkaline phosphatase (abbreviated “ALP”) and “a polypeptide having alkaline phosphatase activity” may be used interchangeably throughout the application.
  • Alkaline phosphatase variant is a variant of any of the alkaline phosphatase sequences disclosed herein having alkaline phosphatase activity and having one or more individual mutations (substitutions, deletion, insertion, extension) compared to the parent sequence, typically substitutions or combinations of substitutions.
  • DNase means a polypeptide having DNase (deoxyribonuclease) activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in DNA, thus degrading DNA. DNases belong to the esterases (EC number 3.1), a subgroup of the hydrolases. The DNases are classified in EC 3.1.21. For purposes of the present invention, DNase activity may be determined according to the procedure described in the DNase activity assay in the examples. The terms “DNase” and “a polypeptide with DNase activity” may be used interchangeably throughout the application.
  • DNase variant is a variant of any of a parent DNase which has and has one or more individual mutations (substitutions, deletion, insertion, extension) compared to the parent sequence, typically substitutions or combinations of substitutions.
  • Expression includes any step involved in the production of a enzyme including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification and secretion.
  • Expression vector refers to a linear or circular DNA construct comprising a DNA sequence encoding an enzyme, which coding sequence is operably linked to a suitable control sequence capable of effecting expression of the DNA in a suitable host.
  • 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.
  • extension means an addition of one or more amino acids to the amino and/or carboxyl terminus of an alkaline phosphatase or a DNase, wherein the “extended” enzyme has alkaline phosphatase activity or DNase activity.
  • fragment means an enzyme having one or more amino acids absent from the amino and/or carboxyl terminus of the enzyme, wherein the fragment has enzyme activity, e.g. alkaline phosphatase activity.
  • Host cell is an organism into which an expression vector, phage, virus, or other DNA construct, including a polynucleotide encoding an enzyme, has been introduced.
  • Exemplary host strains are microorganism cells (e.g., bacteria, filamentous fungi, and yeast) capable of expressing the polypeptide of interest.
  • Improved property means a characteristic associated with a variant that is improved compared to the parent. Such improved properties include, but are not limited to, catalytic efficiency, catalytic rate, chemical stability, oxidation stability, pH activity, pH stability, specific activity, stability under storage conditions, substrate binding, substrate cleavage, substrate specificity, substrate stability, surface properties, thermal activity, and thermostability.
  • the improved property is in particular improved stability, for example improved storage stability, including improved storage stability in a detergent composition, improved stability in use in a detergent composition, and/or improved thermostability.
  • variants may also have other improved properties such as improved alkaline phosphatase or DNase activity, e.g. improved specific activity and/or improved wash performance.
  • Isolated means a polypeptide, 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 polypeptide expressed in a host cell. Typically, an isolated polypeptide of the invention will be separated from other components in a culture broth using known protein purification methods.
  • Mature polypeptide means a polypeptide in its mature form following N-terminal processing and/or C-terminal processing (e.g., removal of signal peptide).
  • a host cell may produce a mixture of two of more different mature polypeptides (i.e., with a different C terminal and/or N terminal amino acid) expressed by the same polynucleotide. It is also known that different host cells process polypeptides differently, and thus, one host cell expressing a polynucleotide may produce a different mature polypeptide (e.g., having a different C terminal and/or N terminal amino acid) as compared to another host cell expressing the same polynucleotide.
  • Mature polypeptide coding sequence means a polynucleotide that encodes a mature polypeptide having relevant enzyme activity, i.e. in the present context alkaline phosphatase activity or DNase activity.
  • Mutant means a polynucleotide encoding a variant.
  • Native means a nucleic acid or polypeptide naturally occurring in a host cell.
  • 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 chemical modifications. 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.
  • 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.
  • operably linked means that specified components are in a relationship (including but not limited to juxtaposition) permitting them to function in an intended manner.
  • a regulatory sequence is operably linked to a coding sequence such that expression of the coding sequence is under control of the regulatory sequence.
  • parent means an enzyme, in particular an alkaline phosphatase or a DNase, in which an alteration is made to produce a variant having the same enzymatic function, e.g. an alkaline phosphatase variant will have alkaline phosphatase activity.
  • the alterations in the parent to result in the variant will typically include one or more substitutions and may also include one or more insertions and/or deletions, and/or N- or C-terminal extensions or truncations.
  • Polypeptide The enzymes disclosed herein, including alkaline phosphatases and DNases, may be referred to interchangeably as a “polypeptide” or an “enzyme”.
  • 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, polypeptide or vector that has been modified from its native state.
  • 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”.
  • Sequence identity The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”.
  • 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.
  • the Needle program 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:
  • Signal 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.
  • Variant means a polypeptide having alkaline phosphatase activity or DNase activity comprising a substitution, an insertion (including extension), and/or a deletion (e.g., truncation), at one or more positions.
  • 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.
  • naturally occurring refers to anything (e.g., proteins, amino acids, or nucleic acid sequences) that is found in nature.
  • 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 by modification of the wild- type sequence).
  • Biofilm A biofilm is any group of microorganisms in which cells stick to each other on a surface, such as a textile or a dishware or other hard surface. These adherent cells are frequently embedded within a self-produced matrix of extracellular polymeric substance (EPS).
  • EPS extracellular polymeric substance
  • Biofilm EPS is a polymeric conglomeration generally composed of extracellular DNA, proteins and polysaccharides. Biofilms may form on living or non-living surfaces.
  • the microbial cells growing in a biofilm are physiologically distinct from planktonic cells of the same organism, which, by contrast, are single cells that may float or swim in a liquid medium.
  • Biofilm producing bacteria can be found among the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Micro bacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, and Stenotrophomonas sp.
  • Stability includes storage stability and stability during use, e.g. during a wash process, and reflects the stability of an enzyme, e.g. alkaline phosphatase or variant or DNase or variant, as a function of time, e.g. how much activity is retained when the enzyme is kept in solution, in particular in a detergent solution.
  • the stability is influenced by many factors such as pH, temperature, and the detergent composition, e.g. amount of builder, surfactants etc. Stability may be measured and expressed e.g. as a melting temperature (Tm) or a half-life improvement factor (HIF) compared to the parent enzyme or a reference sequence.
  • Tm melting temperature
  • HIF half-life improvement factor
  • Improved wash performance The term “improved wash performance” may be defined as improved cleaning, for example improved deep cleaning of e.g. textiles.
  • Wash performance may be expressed as a remission value of the stained swatches. After washing and rinsing the swatches are spread out flat and allowed to air dry at room temperature overnight. All washed swatches are evaluated the day after washing. Light reflectance evaluations of the swatches is performed using a suitable instrument such as a Macbeth Color Eye 7000 reflectance spectrophotometer with a very small aperture. The measurements are made without UV in the incident light and remission value typically at 460 nm is extracted.
  • Laundering relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing e.g. a cleaning or detergent composition of the present invention.
  • the laundering process can for example be carried out using a household or an industrial washing machine or can be carried out by hand.
  • Deep cleaning refers to reduction or removal of organic materials including components of biofilm, such as EPS or parts hereof, polysaccharides, PNAG (poly-N-acetylglucosamine), proteins, DNA, soil or other components present in biofilm. Deep cleaning encompasses not only removal of visible soiling on e.g. textiles, but also e.g. organic material or malodor within a textile that may not be removed using conventional detergent compositions and enzymes. Such organic material may for example include dead cell material, skin debris, sebum, sweat, grease and other stains derived from e.g. humans (body soils) or microbes.
  • Detergent composition includes unless otherwise indicated any form of detergent or cleaning composition. These include granular or powder-form all-purpose or heavy-duty washing agents, especially cleaning detergents; liquid, gel or paste-form all-purpose washing agents, especially the so-called heavy- duty liquid (HDL) types; single unit dose (SUD) compositions such as pods, capsules, tabs, etc.
  • HDL heavy-duty liquid
  • SUV single unit dose
  • liquid fine-fabric detergents such as those of the high-foaming type
  • hand dishwashing agents or light duty dishwashing agents especially those of the high-foaming type
  • machine dishwashing agents including the various tablet, granular, liquid and rinse-aid types for household and institutional use
  • liquid cleaning and disinfecting agents including antibacterial hand-wash types, cleaning bars, soap bars, mouthwashes, denture cleaners, car or carpet shampoos, bathroom cleaners; hair shampoos and hair-rinses; shower gels, foam baths; metal cleaners; as well as cleaning auxiliaries such as bleach additives and "stain-stick" or pre-treat types.
  • detergent composition and “detergent formulation” are used in reference to mixtures which are intended for use in a wash medium for the cleaning of soiled objects.
  • the term is used in reference to laundering fabrics and/or garments (e.g., “laundry detergents”).
  • the term refers to other detergents, such as those used to clean dishes, cutlery, etc. (e.g., "dishwashing detergents”). It is not intended that the present invention be limited to any particular detergent formulation or composition.
  • detergent composition is not intended to be limited to compositions that contain surfactants.
  • the term encompasses detergents that may contain, e.g., surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferases, hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.
  • detergents may contain, e.g., surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferases, hydrolytic enzymes,
  • Fabric encompasses any textile material. Thus, it is intended that the term encompass garments, as well as fabrics, yarns, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material.
  • Textile refers to woven fabrics, as well as staple fibers and filaments suitable for conversion to or use as yarns, woven, knit, and non-woven fabrics.
  • the term encompasses yarns made from natural, as well as synthetic (e.g., manufactured) fibers.
  • textile materials is a general term for fibers, yarn intermediates, yarn, fabrics, and products made from fabrics (e.g., garments and other articles).
  • Non-fabric detergent compositions include non-textile surface detergent compositions, including but not limited to compositions for hard surface cleaning, such as dishwashing detergent compositions including manual dishwashing compositions, oral detergent compositions, denture detergent compositions, and personal cleansing compositions.
  • Hard surface cleaning comprises, in addition to dishwashing, other domestic or industrial hard surfaces, such as but not limited to domestic hard surfaces including floors, walls, tabletops, kitchen surfaces including kitchen appliance surfaces, bathroom surfaces, etc.
  • Effective amount of enzyme refers to the quantity of enzyme necessary to achieve the enzymatic activity required in the specific application, e.g., in a defined detergent composition. Such effective amounts are readily ascertained by one of ordinary skill in the art and are based on many factors, such as the particular enzyme used, the cleaning application, the specific composition of the detergent composition, and whether a liquid or dry (e.g., granular, bar) composition is required, and the like.
  • relevant washing conditions is used herein to indicate the conditions, particularly washing temperature, time, washing mechanics, detergent concentration, type of detergent and water hardness, actually used in households in a detergent market segment.
  • wash liquor refers to an aqueous solution comprising an alkaline phosphatase of the invention.
  • a wash liquor is a solution, e.g. found in a washing machine or dishwasher, containing water and a detergent composition comprising the alkaline phosphatase.
  • the detergent composition prior to being mixed with water to form a wash liquor, may be in any suitable form as described elsewhere herein, for example a liquid or powder.
  • Water hardness The term “water hardness” or “degree of hardness” or “dH” or “°dH” as used herein refers to German degrees of hardness. One degree is defined as 10 milligrams of calcium oxide per liter of water.
  • Adjunct materials means any liquid, solid or gaseous material selected for the particular type of detergent composition desired and the form of the product (e.g., liquid, granule, powder, bar, paste, spray, tablet, gel, or foam composition), which materials are also preferably compatible with the alkaline phosphatase enzyme used in the composition. More detailed information on adjunct materials is provided further below.
  • Low detergent concentration The term “low detergent concentration” system includes detergents where less than about 800 ppm of detergent components is present in the wash water. Asian, e.g., Japanese detergents are typically considered low detergent concentration systems.
  • Medium detergent concentration The term “medium detergent concentration” system includes detergents wherein between about 800 ppm and about 2000 ppm of detergent components is present in the wash water. North American detergents are generally considered to be medium detergent concentration systems.
  • High detergent concentration includes detergents wherein greater than about 2000 ppm of detergent components is present in the wash water. European detergents are generally considered to be high detergent concentration systems.
  • substitutions For an amino acid substitution, the following nomenclature is used: Original amino acid, position, substituted amino acid. Accordingly, the substitution of threonine at position 226 with alanine is designated as “T226A”.
  • Multiple mutations may be separated by addition marks (“+”), e.g., “G205R + S411 F”, representing substitutions at positions 205 and 411 of glycine (G) with arginine (R) and serine (S) with phenylalanine (F), respectively.
  • Multiple mutations may alternatively be indicated by a space, a comma, or a plus sign, e.g. “G205R S411 F”, “G205R, S411 F” or “G205R+S411 F”.
  • Deletions For an amino acid deletion, the following nomenclature is used: Original amino acid, position, *. Accordingly, the deletion of glycine at position 195 is designated as “G195*”. Multiple deletions are separated by addition marks (“+”), e.g., “G195* + S411*”. Insertions. For an amino acid insertion, the following nomenclature is used: Original amino acid, position, original amino acid, inserted amino acid. Accordingly, the insertion of lysine after glycine at position 195 is designated “G195GK”. 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 lysine and alanine after glycine at position 195 is indicated as “G195GKA”.
  • Variants comprising multiple alterations are separated by addition marks (“+”) as explained above, e.g., “R170Y+G195E” representing a substitution of arginine and glycine at positions 170 and 195 with tyrosine and glutamic acid, respectively.
  • the multiple alterations may be separated by a space or comma as mentioned above.
  • R170Y.E represents a substitution of arginine at position 170 with tyrosine or glutamic acid.
  • Y167G.A + R170G.A designates the following variants: “Y167G+R170G”, “Y167G+R170A”, “Y167A+R170G” and “Y167A+R170A”.
  • the present disclosure shows the surprising effect of adding a polypeptide having alkaline phosphatase activity to a washing solution containing relatively high amounts of organophosphate (OP) groups.
  • OP groups from for example 5’-DNA will precipitate with soap or surfactant in an aqueous solution having medium to high water hardness of about 5-30° dH. This can also happen in a solution with a normal to low dose of detergent solution if the detergent is not formulated with strong chelators that can bind ions such as calcium ions. This precipitation can be inhibited or reduced by adding an alkaline phosphatase to the washing solution, typically as part of the detergent.
  • the present invention thus provides cleaning compositions and methods which employ a polypeptide having alkaline phosphatase activity, advantageously together with a polypeptide having DNase activity.
  • Alkaline phosphatase polypeptides are particularly useful for cleaning compositions and methods which employ a polypeptide having alkaline phosphatase activity, advantageously together with a polypeptide having DNase activity.
  • the present invention provides, in one aspect, polypeptides having alkaline phosphatase activity, e.g. in isolated and/or purified form.
  • the polypeptides having alkaline phosphatase activity are suitable for use in the cleaning compositions and methods disclosed herein.
  • the invention thus provides, in another aspect, cleaning compositions comprising an alkaline phosphatase polypeptide as well as methods for cleaning or laundering using an alkaline phosphatase polypeptide.
  • the polypeptide having alkaline phosphatase activity is preferably selected from the group consisting of:
  • polypeptide derived from the polypeptide of (a) or (b), wherein the N- and/or C- terminal end has been extended by the addition of 1 to 50 amino acids, such as 1 to 40, 1 to 30 or 1 to 20 amino acids; and
  • the polypeptide having alkaline phosphatase activity may more particularly be selected from the group consisting of polypeptides having at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94% or at least 95% sequence identity to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21 , SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO
  • the polypeptide having alkaline phosphatase activity has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97% or at least 98% sequence identity to SEQ ID NO: 1.
  • the polypeptide having alkaline phosphatase activity is a variant of SEQ ID NO: 1 having one or more substitutions, deletions or insertions, preferably substitutions.
  • the polypeptide having alkaline phosphatase activity may for example be a variant of SEQ ID NO: 1 having a substitution in at least one position selected from the group consisting of positions 77, 90, 94, 117, 119, 148, 156, 208, 212, 216, 220, 224, 225, 228, 245, 246, 248, 270, 271 , 291 , 292, 303 and 381 , for example substitutions in two or more of these positions.
  • Preferred polypeptide variants having alkaline phosphatase activity include variants of SEQ ID NO: 1 comprising at least one substitution selected from the group consisting of A77T, N90I, A94P, I117L, H119A, N148F, M156F, K208A, R212M, M216V, K220P, K220E, E224D, T225E, D228R, Q245L, I246F, W248K, K270G, A271 R, S291G, T292A, Y303L and G381S, for example two or more of said substitutions.
  • the polypeptide having alkaline phosphatase activity is a variant of SEQ ID NO: 1 having at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 61 , SEQ ID NO: 62, SEQ ID NO: 63, SEQ ID NO: 64, SEQ ID NO: 65, SEQ ID NO: 66, SEQ ID NO: 67, SEQ ID NO: 68, SEQ ID NO: 69, SEQ ID NO: 70, SEQ ID NO: 71 , SEQ ID NO: 72, SEQ ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 76, SEQ ID NO: 77, SEQ ID NO: 78, SEQ ID NO: 79, SEQ ID NO: 80 or SEQ ID NO: 81 .
  • the polypeptide having alkaline phosphatase activity is a variant of SEQ ID NO: 1 having at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 79.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 2.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 2 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 3.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 3 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 4.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 4 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 5.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 5 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 6.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 6 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 7.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 7 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 8.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 8 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 9.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 9 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 10.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 10 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 11.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 11 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 12.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 12 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 13.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 13 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 14.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 14 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 15.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 15 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 16.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 16 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 17.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 17 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 18.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 18 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 19.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 19 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 20.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 20 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 21.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 21 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 22.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 22 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 23.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 23 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 24.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 24 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 25.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 25 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 26.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 26 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 27.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 27 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 28.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 28 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 29.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 29 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 30.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 30 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 31.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 31 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 32.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 32 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 33.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 33 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 34.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 34 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 35.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 35 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 36.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 36 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 37.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 37 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 38.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 38 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 39.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 39 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 40.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 40 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 41.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 41 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 42.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 42 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 43.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 43 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 44.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 44 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 45.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 45 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 46.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 46 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 47.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 47 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 48.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 48 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 49.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 49 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 50.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 50 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 51.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 51 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 52.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 52 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 53.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 53 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 54.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 54 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 55.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 55 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 56.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 56 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 57.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 57 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 58.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 58 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 59.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 59 or a mature polypeptide thereof.
  • the alkaline phosphatase polypeptide has a sequence identity of at least 70%, e.g., at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% to SEQ ID NO: 60.
  • the polypeptide may e.g. comprise, consist essentially of or consist of the amino acid sequence of SEQ ID NO: 60 or a mature polypeptide thereof.
  • the cleaning compositions of the invention comprising an alkaline phosphatase preferably also comprise a polypeptide having DNase activity. While it is contemplated that various polypeptides having DNase activity may be used together with the polypeptide having alkaline phosphatase activity, certain DNase polypeptides are preferred.
  • the polypeptide having DNase activity may thus be selected from the group consisting of: a) a polypeptide having 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%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 83; b) a polypeptide having 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%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 82; and c) a variant of SEQ ID NO: 82, wherein the variant has at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %
  • the polypeptide having DNase activity may be a variant of SEQ ID NO: 82, wherein the variant has 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% or at least 95% sequence identity to SEQ ID NO: 82 or SEQ ID NO: 83 and comprises, compared to SEQ ID NO: 82, one or more substitutions, preferably 2 or more, 3 or more, 4 or more, 5 or more, 6 or more, 7 or more, 8 or more, 9 or more or 10 or more substitutions, selected from the group consisting of T1 I, S13Y, T22P, S25P, S27L, S39P, D56I, S57W, S59V, T65V, V76L, T77Y, Q109R, S116D, T127V, S144P, A147H, G149N, S167L, G175D and S181 L.
  • the polypeptide having DNase activity may be a variant of SEQ ID NO: 82, wherein the variant has 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% or at least 95% sequence identity to SEQ ID NO: 82 or SEQ ID NO: 83 and comprises, compared to SEQ ID NO: 82, two or more substitutions, such as three, four, five or more substitutions, selected from the group consisting of N61 D, T65I, T65V, S82R, K107Q, T127S, T127V, G149N, S164D and L181S.
  • the polypeptide having DNase activity may optionally further comprise at least one substitution selected from the group consisting of Q14R, Q14W, K21 L, P25S, L33K, Q48D, D56I, D56L, S66Y, S68L, Y77T, S102Y, S106A, R109Q, R109T, D116S, D116W, T171W, L181T and L181W.
  • Examples of preferred combinations of substitutions relative to SEQ ID NO: 82 in this embodiment include the following: a) G149N together with at least one of the substitutions N61 D, T65I, T65V, S82R, K107Q, T127S, T127V, S164D and L181S; b) T65I or T65V together with at least two of the substitutions N61 D, S82R, K107Q, T127S, T127V, G149N, S164D and L181S; c) N61 D together with at least two of the substitutions T65I/V, S82R, K107Q, T127S/V, G149N, S164D and L181S, preferably at least two of the substitutions T65I/V, S82R, K107Q, T127S and S164D; d) S82R together with at least two of the substitutions N61 D, T65I, T65V, K107Q, T127S, T127V, G149N, S164D and L
  • DNase polypeptides described above which are based on SEQ ID NO: 82 (obtained from Metabacillus indicus, formerly known as Bacillus cibi), and variants thereof may e.g. be found in WO 2017/060475, WO 2018/011277, WO 2019/081724 and WO 2022/194668, which are hereby incorporated by reference.
  • the polypeptide having DNase activity in the cleaning compositions of the invention may alternatively be a polypeptide having 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%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 86; or to the polypeptide of SEQ ID NO: 86 which is N-terminally truncated by up to about 20 amino acid residues, for example by an N-terminal truncation of 15-17 amino acid residues such that the polypeptide comprises e.g. 206 or 204 amino acid residues rather than the 221 amino acid residues in SEQ ID NO: 86.
  • the polypeptide having DNase activity may be a variant of SEQ ID NO: 86, wherein the variant has 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% or at least 95% sequence identity to SEQ ID NO: 86 and comprises at least two alterations selected from the group consisting of S69V, Q102E, S26*, D32Q, K36C,H, G37R, F43W, D46G, A55I, N68D, A76I, K82S,T, P84D,T, K86G,L,N,Q,T,V,Y, A91 R, L92E, K95I, P97E,N, A101 E, K105N,G,Q,T,D, F112Y.W, L129K, N133Q, V138C, N140H, G141Q.R, S144E, N146A, K147N.E,
  • the polypeptide having DNase activity may be a variant of SEQ ID NO: 86, wherein the variant has 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% or at least 95% sequence identity to SEQ ID NO: 86 and comprises at least two substitutions, such as at least three substitutions, selected from the group consisting of A111 P, D32E, V35I, S69V, Q102E, K105N and G181 N.
  • the variant may optionally further comprise two or more substitutions selected from the group consisting of S26H, D32E, V35I, K65E, K67A, S69E, S69V, S98R, Q102E, K105N, S115T, Q150E, Q157E, T159Q, G161 R, A172E, G181 N, S182Y, S182V, K185E, V187N, K192I, A206G, Q208V and K212E.
  • DNase polypeptides which are based on SEQ ID NO: 86 (obtained from Aspergillus oryzae), and variants thereof may e.g. be found in WO 2015/155350, WO 2017/064269, WO 2022/189521 and PCT/EP2023/054907, which are hereby incorporated by reference.
  • a polypeptide having DNase activity other than those described above may be used together with an alkaline phosphatase polypeptide in the cleaning compositions of the invention.
  • Non-limiting examples of disclosures of other such suitable polypeptides having DNase activity are found in WO 2017/060493, WO 2017/060505, WO 2018/177203, WO 2018/177936, WO 2018/177938 and WO 2020/069670, which are hereby incorporated by reference.
  • the present invention also relates to polynucleotides.
  • the polynucleotide encoding an alkaline phosphatase as disclosed herein may be a genomic DNA, a cDNA, a synthetic DNA, a synthetic RNA, a mRNA, or a combination thereof.
  • the polynucleotide is isolated, preferably purified.
  • the present invention also relates to nucleic acid constructs comprising a polynucleotide encoding an alkaline phosphatase as disclosed herein 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.
  • control sequences that may be used are promoters, terminators, mRNA stabilizers, leader sequences, polyadenylation sequences, signal peptides, propeptides, regulatory sequences and transcription factors, all of which are well known in the art.
  • the polynucleotide may be manipulated in a variety of ways to provide for expression of a polypeptide. 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.
  • the present invention also relates to recombinant expression vectors comprising a polynucleotide encoding an alkaline phosphatase as disclosed herein, 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 polypeptide at such sites.
  • the polynucleotide may be expressed by inserting the polynucleotide or a nucleic acid construct comprising the polynucleotide into an appropriate vector for expression.
  • 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.
  • Expression vectors suitable for recombinant expression are well known in the art, as are e.g. methods for introducing them into a host cell.
  • the present invention also relates to recombinant host cells, comprising a polynucleotide encoding an alkaline phosphatase as disclosed herein operably linked to one or more control sequences that direct the production of a polypeptide 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 polypeptide 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 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.
  • Grampositive 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, llyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.
  • the 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.
  • a fungal host cell may be a yeast cell or a filamentous fungal cell.
  • the filamentous fungal host cell may e.g. 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.
  • Acremonium Aspergillus, Aureobasidium, Bjerkandera, Ceriporiopsis, Chrysosporium, Coprinus, Coriolus, Cryptococcus, Filibasidium, Fusarium, Humicola, Magnaporthe
  • 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.
  • the host cell is isolated, preferably purified.
  • the present invention also relates to methods of producing an alkaline phosphatase as disclosed herein, comprising (a) cultivating a recombinant host cell of the invention under conditions conducive for production of the polypeptide; and optionally (b) recovering the polypeptide.
  • the host cell is cultivated in a nutrient medium suitable for production of the polypeptide using methods known in the art.
  • 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 polypeptide 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 polypeptide is secreted into the nutrient medium, the polypeptide can be recovered directly from the medium. If the polypeptide is not secreted, it can be recovered from cell lysates.
  • the polypeptide may be detected using methods known in the art that are specific for the polypeptide, 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 polypeptide.
  • the polypeptide 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.
  • the whole fermentation broth is recovered.
  • a cell-free fermentation broth comprising the polypeptide is recovered.
  • the polypeptide may be purified by a variety of procedures known in the art to obtain substantially pure polypeptides 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).
  • polypeptide is not recovered.
  • the present invention provides cleaning compositions comprising at least one alkaline phosphatase, optionally at least one DNase, and at least one cleaning adjunct ingredient.
  • the cleaning compositions contain one or more cleaning adjunct ingredients selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co- builders, fabric hueing agents, anti-foaming agents, dispersants, processing aids, and/or pigments.
  • cleaning adjunct ingredients selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition
  • the cleaning compositions will typically contain at least a surfactant and normally other cleaning adjunct ingredients such as a builder or a clay/soil removal/anti-redeposition agent, additional enzymes, etc.
  • the cleaning adjunct ingredient may thus be one or more enzymes other than a DNase.
  • the one or more enzymes may e.g. be selected from the group consisting of proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, catalases and mannanases. Specific enzymes suitable for the detergent compositions of the invention are described below.
  • the cleaning composition may be formulated in any suitable form, such as 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.
  • the cleaning composition can thus e.g. be a liquid detergent or a powder or granular detergent, optionally in “concentrated” or "compact" form. It may also be in the form of a single unit dose composition.
  • the amount of alkaline phosphatase in the cleaning composition may vary depending on factors such as the degree of concentration or compactness of the composition and the desired enzyme concentration in the wash liquor.
  • the alkaline phosphatase will normally be included in the cleaning composition in an amount of up to about 10,000 ppm, typically up to about 5000 ppm or up to about 2000 ppm.
  • the alkaline phosphatase can e.g. be included in the cleaning composition at a level of from 1 ppm to 10,000 ppm, such as from 10 ppm to 5000 ppm, from 20 ppm to 2000 ppm, from 50 ppm to 1000 ppm, from 80 ppm to 600 ppm, or from 100 ppm to 500 ppm.
  • ppm in this context is intended to refer to mg/l for an enzyme added to a liquid composition (e.g. liquid, gel, etc.), or mg/kg for an enzyme added to a solid composition (e.g. powder, granulate, tablet, etc.).
  • a liquid composition e.g. liquid, gel, etc.
  • a solid composition e.g. powder, granulate, tablet, etc.
  • the amounts of alkaline phosphatase disclosed above also apply to the DNase.
  • the DNase may thus be included in the cleaning composition in an amount of up to about 10,000 ppm, typically up to about 5000 ppm or up to about 2000 ppm, for example at a level of from 1 ppm to 10,000 ppm, such as from 10 ppm to 5000 ppm, from 20 ppm to 2000 ppm, from 50 ppm to 1000 ppm, from 80 ppm to 600 ppm, or from 100 ppm to 500 ppm.
  • the detergent composition is a liquid or powder laundry detergent, suitable for e.g. washing at high temperature and/or pH, such as at or above 40°C and/or at or above pH 8.
  • the detergent composition is a liquid or powder laundry detergent, suitable for e.g. washing at low temperature and/or pH, such as at or below 20°C and/or pH 6.
  • the detergent may also be formulated as a unit dose detergent and/or compact detergent optionally with minimum or no water.
  • the detergent may also be a dish wash detergent.
  • the laundry and dish wash detergents may be phosphate-free.
  • a surfactant may be selected among nonionic, anionic and/or amphoteric surfactants as described above, preferably anionic or nonionic surfactants but also amphoteric surfactants may be used. In general, bleach-stable surfactants are preferred.
  • anionic surfactants are sulphate surfactants and in particular alkyl ether sulphates, especially C-9-15 alcohol ethersulfates, C12-15 primary alcohol ethoxylate, C8-C16 ester sulphates and C10-C14 ester sulphates, such as mono dodecyl ester sulphates
  • anionic surfactants include sulfates and sulfonates, in particular, linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium do
  • LAS
  • the anionic surfactants are preferably added to the detergent in the form of salts.
  • Suitable cations in these salts are alkali metal ions, such as sodium, potassium and lithium and ammonium salts, for example (2-hydroxyethyl) ammonium, bis(2-hydroxyethyl) ammonium and tris(2- hydroxyethyl) ammonium salts.
  • Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (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
  • a builder is preferably selected among phosphates, sodium citrate builders, sodium carbonate, sodium silicate, sodium aluminosilicate (zeolite). Suitable builders are alkali metal or ammonium phosphates, polyphosphates, phosphonates, polyphosphates, carbonates, bicarbonates, borates, citrates, and polycarboxylates. Citrate builders, e.g., citric acid and soluble salts thereof (particularly sodium salt), are polycarboxylate builders. Citrates can be used in combination with zeolite, silicates like the BRITESIL types, and/or layered silicate builders. The builder is preferably added in an amount of about 0-65% by weight, such as about 5% to about 50% by weight.
  • the level of builder is typically about 40-65% by weight, particularly about 50-65% by weight, particularly from 20% to 50% by weight.
  • 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 Hoechst), and (carboxymethyl)inulin (CMI), and combinations thereof.
  • builders include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid. Additional specific examples include 2,2’,2”-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N’-disuccinic acid (EDDS), methylglycine-N,N- diacetic acid (MGDA), glutamic acid-N,N -di acetic acid (GLDA), 1-hydroxyethane-1 ,1-diphosphonic acid, N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-
  • Phosphonates suitable for use herein include 1-hydroxyethane-1 ,1-diphosphonic acid (HEDP), ethylenediaminetetrakis (methylenephosphonicacid) (EDTMPA), diethylenetriaminepentakis (methylenephosphonic acid) (DTMPA or DTPMPA or DTPMP), nitrilotris (methylenephosphonic acid) (ATMP or NTMP), 2-phosphonobutane-1 ,2,4-tricarboxylic acid (PBTC), hexamethylenediaminetetrakis (methylenephosphonic acid) (HDTMP).
  • the composition may also contain 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.
  • co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly (acrylic acid) (PAA) or copoly (acrylic acid/maleic acid) (PAA/PMA) or polyaspartic acid.
  • PAA poly (acrylic acid)
  • PAA/PMA copoly (acrylic acid/maleic acid)
  • Further exemplary builders and/or co-builders are described in, e.g., WO 09/102854, US 5977053.
  • the builder is a non-phosphorus based builder such as citric acid and/or methylglycine-N, N-diacetic acid (MGDA) and/or glutamic-N, N-diacetic acid (GLDA) and/or salts thereof.
  • the liquid composition may also be phosphate free in that instance the preferred builders includes citrate and/or methylglycine-N, N-diacetic acid (MGDA) and/or glutamic- N, N-diacetic acid (GLDA) and I or salts thereof.
  • the cleaning composition may contain 0-30% by weight, such as about 1% to about 20%, of a bleaching system.
  • a bleaching system comprising components known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include sources of hydrogen peroxide; sources of peracids; and bleach catalysts or boosters.
  • Sources of hydrogen peroxide are inorganic persalts, including alkali metal salts such as sodium percarbonate and sodium perborates (usually mono- or tetrahydrate), and hydrogen peroxide— urea (1/1).
  • Peracids may be (a) incorporated directly as preformed peracids or (b) formed in situ in the wash liquor from hydrogen peroxide and a bleach activator (perhydrolysis) or (c) formed in situ in the wash liquor from hydrogen peroxide and a perhydrolase and a suitable substrate for the latter, e.g., an ester.
  • Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids such as peroxybenzoic acid and its ring-substituted derivatives, peroxy-a-naphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, e-phthalimidoperoxycaproic acid [phthalimidoperoxyhexanoic acid (PAP)], and o-carboxybenzamidoperoxycaproic acid; aliphatic and aromatic diperoxydicarboxylic acids such as diperoxydodecanedioic acid, diperoxyazelaic acid, diperoxysebacic acid, diperoxybrassylic acid, 2-decyldiperoxybutanedioic acid, and diperoxyphthalic, -isophthalic and -terephthalic acids; perimidic acids; peroxymonosulfuric acid; peroxydisulfuric acid; peroxyphosphoric acid
  • Suitable bleach activators include those belonging to the class of esters, amides, imides, nitriles or anhydrides and, where applicable, salts thereof.
  • Suitable examples are tetraacetylethylenediamine (TAED), sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1-sulfonate (ISONOBS), sodium 4-(dodecanoyloxy)benzene-1-sulfonate (LOBS), sodium 4- (decanoyloxy)benzene-l -sulfonate, 4-(decanoyloxy)benzoic acid (DOBA), sodium 4- (nonanoyloxy)benzene-l -sulfonate (NOBS), and/or those disclosed in WO98/17767.
  • TAED tetraacetylethylenediamine
  • ISONOBS sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1-sulfonate
  • LOBS 4-(dodecanoyloxy)benzene-1-sulfonate
  • DOBA 4-(decanoyloxy)benzo
  • ATC acetyl triethyl citrate
  • ATC or a short chain triglyceride like triacetin has the advantage that they are environmentally friendly.
  • acetyl triethyl citrate and triacetin have good hydrolytical stability in the product upon storage and are efficient bleach activators.
  • ATC is multifunctional, as the citrate released in the perhydrolysis reaction may function as a builder.
  • the bleaching system may also include a bleach catalyst or booster.
  • bleach catalysts that may be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese-collagen, cobalt-amine catalysts and manganese triazacyclononane (MnTACN) catalysts; particularly preferred are complexes of manganese with 1 ,4, 7-tri methyl- 1 ,4,7-triazacyclononane (Me3-TACN) or 1 ,2,4,7-tetramethyl-1 ,4,7-triazacyclononane (Me4-TACN), in particular Me3-TACN, such as the dinuclear manganese complex [(Me3-TACN)Mn(O)3Mn(Me3-TACN)](PF6)2, and [2, 2', 2"- nitrilotris(ethane-1 ,2-diylazanylylidene-KN
  • an organic bleach catalyst or bleach booster may be used having one of the following formulae:
  • each R1 is independently a branched alkyl group containing from 9 to 24 carbons or linear alkyl group containing from 11 to 24 carbons, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbons or linear alkyl group containing from 11 to 18 carbons, more preferably each R1 is independently selected from the group consisting of 2-propyl heptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl.
  • Suitable bleaching systems are described, e.g. in WO 2007/087258, WO 2007/087244, WO 2007/087259, EP 1867708 (Vitamin K) and WO 2007/087242.
  • Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.
  • detergent components may include, for textile care, the consideration of the type of textile 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.
  • components mentioned below are categorized by general header according to a functionality, this is not to be construed as a limitation, as a component may comprise additional functionalities as will be appreciated by the skilled artisan, including the exemplary non-limiting components shown in below. Hydrotropes
  • the detergent composition 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 hydrotrope.
  • a hydrotrope Any hydrotrope known in the art for use in detergents may be utilized.
  • Non-limiting examples 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.
  • the detergent composition 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 antiredeposition, fibre 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 (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of polyethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-/V-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole
  • polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate.
  • PEO-PPO polypropylene oxide
  • diquaternium ethoxy sulfate diquaternium ethoxy sulfate.
  • Other exemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of the above- mentioned polymers are also contemplated.
  • the detergent composition 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.
  • 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.
  • 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.
  • Suitable 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.l.) 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 WO 2005/03274, WO 2005/03275, WO 2005/03276 and EP 1876226 (hereby incorporated by reference).
  • 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 hueing 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 WO 2007/087243.
  • the detergent composition may comprise one or more additional enzymes such as a protease, lipase, cutinase, amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, hexosaminidase, licheninase, xyloglucanase, oxidase, e.g., a laccase, and/or peroxidase.
  • additional enzymes such as a protease, lipase, cutinase, amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, hexosaminidase, licheninase, xyloglucanase, oxidase, e.g.,
  • the properties of the selected enzyme(s) should be compatible with the selected detergent, (/.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.
  • Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691 ,178, US 5,776,757 and WO 89/09259.
  • cellulases are the alkaline or neutral cellulases having colour care benefits.
  • Examples of such cellulases are cellulases described in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940.
  • Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471 , WO 98/12307 and WO 99/001544.
  • 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.
  • cellulases include CelluzymeTM, and CarezymeTM (Novozymes A/S) Carezyme PremiumTM (Novozymes A/S), CellucleanTM (Novozymes A/S), Celluclean ClassicTM (Novozymes A/S), CellusoftTM (Novozymes A/S), WhitezymeTM (Novozymes A/S), ClazinaseTM, and Puradax HATM (Genencor International Inc.), and KAC-500(B)TM (Kao Corporation).
  • Suitable proteases may be of any origin, but are preferably of bacterial or fungal origin, optionally in the form of protein engineered or chemically modified mutants.
  • the protease 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 a subtilisin.
  • a metalloprotease may for example be a thermolysin, e.g. from the M4 family, or another metalloprotease such as those from the M5, M7 or M35 families.
  • subtilases refers to a sub-group of serine proteases according to Siezen et al., Protein Eng. 4 (1991) 719-737 and Siezen et al., Protein Sci. 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 six subdivisions, the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
  • proteases suitable for detergent use may be obtained from a variety of organisms, including fungi such as Aspergillus
  • detergent proteases have generally been obtained from bacteria and in particular from Bacillus.
  • Bacillus species from which subtilases have been derived include Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus and Bacillus gibsonii.
  • Particular subtilisins include subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, subtilisin BPN’, subtilisin 309, subtilisin 147 and subtilisin 168 and e.g. protease PD138 (described in WO 93/18140).
  • Other useful proteases are e.g. those described in WO 01/16285 and WO 02/16547.
  • trypsin-like proteases examples include the Fusarium protease described in WO 94/25583 and WO 2005/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 2005/052161 and WO 2005/052146.
  • metalloproteases include the neutral metalloproteases described in WO 2007/044993 such as those derived from Bacillus amyloliquefaciens, as well as e.g. the metalloproteases described in WO 2015/158723 and WO 2016/075078.
  • proteases examples include the protease variants described in WO 89/06279 WO 92/19729, WO 96/34946, WO 98/20115, WO 98/20116, WO 99/11768, WO 01/44452, WO 03/006602, WO 2004/003186, WO 2004/041979, WO 2007/006305, WO 2011/036263, WO 2014/207227, WO 2016/087617 and WO 2016/174234.
  • Preferred protease variants may, for example, comprise one or more of the mutations selected from the group consisting of: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V102I, V102Y, V102N, S104A, G116V, G116R, H118D, H118N, A120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V
  • Protease variants having one or more of these mutations are preferably variants of the Bacillus lentus protease (Savinase®, also known as subtilisin 309) shown in SEQ ID NO: 1 of WO 2016/001449 or of the Bacillus amyloliquefaciens protease (BPN’) shown in SEQ ID NO: 2 of WO 2016/001449.
  • Bacillus lentus protease (Savinase®, also known as subtilisin 309) shown in SEQ ID NO: 1 of WO 2016/001449 or of the Bacillus amyloliquefaciens protease (BPN’) shown in SEQ ID NO: 2 of WO 2016/001449.
  • Such protease variants preferably have at least 80% sequence identity to SEQ ID NO: 1 or to SEQ ID NO: 2 of WO 2016/001449.
  • protease of interest is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO 91/02792, and variants thereof which are described for example in WO 92/21760, WO 95/23221 , EP 1921147, EP 1921148 and WO 2016/096711 .
  • the protease may alternatively be a variant of the TY145 protease having SEQ ID NO: 1 of WO 2004/067737, for example a variant comprising a substitution at one or more positions corresponding to positions 27, 109, 111 , 171 , 173, 174, 175, 180, 182, 184, 198, 199 and 297 of SEQ ID NO: 1 of WO 2004/067737, wherein said protease variant has a sequence identity of at least 75% but less than 100% to SEQ ID NO: 1 of WO 2004/067737.
  • TY145 variants of interest are described in e.g. WO 2015/014790, WO 2015/014803, WO 2015/014804, WO 2016/097350, WO 2016/097352, WO 2016/097357 and WO 2016/097354.
  • proteases examples include:
  • variants of SEQ ID NO: 1 of WO 2016/001449 comprising two or more substitutions selected from the group consisting of S9E, N43R, N76D, Q206L, Y209W, S259D and L262E, for example a variant with the substitutions S9E, N43R, N76D, V205I, Q206L, Y209W, S259D, N261W and L262E, or with the substitutions S9E, N43R, N76D, N185E, S188E, Q191 N, A194P, Q206L, Y209W, S259D and L262E, wherein position numbers are based on the numbering of SEQ ID NO: 2 of WO 2016/001449;
  • Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, DuralaseTM, DurazymTM, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, PrimaseTM, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Blaze Evity® 200T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® In, Progress® Key and Progress® Excel (Novozymes A/S), those sold under the tradename MaxataseTM, MaxacaiTM, Maxapem®, Purafect® Ox, Purafect® OxP, Puramax®, FN2TM, FN3TM, FN4 ex TM, Excellase®, Excell
  • 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 EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96/13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp.
  • Thermomyces e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216
  • cutinase from Humicola e.g. H
  • strain SD705 (W095/06720 & W096/27002), P. wisconsinensis (WO96/12012), GDSL-type Streptomyces lipases (W010/065455), cutinase from Magnaporthe grisea (WO10/107560), cutinase from Pseudomonas mendocina (US5,389,536), lipase from Thermobifida fusca (W011/084412), Geobacillus stearothermophilus lipase (W011/084417), lipase from Bacillus subtilis (W011/084599), and lipase from Streptomyces griseus (WO11/150157) and S. pristinaespiralis (W012/137147).
  • lipase variants such as those described in EP407225, WO92/05249, WO94/01541 , WO94/25578, WO95/14783, WO95/30744, WO95/35381 , WO95/22615, W096/00292, W097/04079, W097/07202, WO00/34450, WO00/60063, W001/92502, W007/87508 and WO09/109500.
  • Preferred commercial lipase products include LipolaseTM, LipexTM; LipolexTM and LipocleanTM (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades).
  • lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10/111143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), 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 (W010/100028).
  • Suitable amylases which can be used together with the alkaline phosphatases and optional DNases 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.
  • Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 1 thereof.
  • variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, 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.
  • amylases having SEQ ID NO: 6 in WO 02/010355 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.
  • amylases which are suitable are hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase obtained 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, 1201 , A209 and Q264.
  • amylase variants such as those described in WO 2011/098531, WO 2013/001078 and WO 2013/001087.
  • amylases include DuramylTM, TermamylTM, FungamylTM, StainzymeTM, Stainzyme PlusTM, NatalaseTM, Liquozyme X and BANTM (from Novozymes A/S), and RapidaseTM, PurastarTM/EffectenzTM, Powerase and Preferenz S100 (from Genencor International Inc./DuPont).
  • Detergent compositions comprising an alkaline phosphatase and optional DNase of the invention may also include one or more hexosaminidases.
  • hexosaminidase includes “dispersin’’ and the abbreviation “Dsp”, which means a polypeptide having hexosaminidase activity, EC 3.2.1.-, that catalyzes the hydrolysis of p-1,6-glycosidic linkages of N-acetyl- glucosamine polymers found e.g. in biofilm.
  • the term hexosaminidase includes polypeptides having N-acetylglucosaminidase activity and p-N-acetylglucosaminidase activity.
  • a polypeptide having hexosaminidase activity may be obtained from microorganisms of any genus, in particular from bacteria or fungi.
  • the hexosaminidase e.g. a dispersin
  • the hexosaminidase is obtained from Terribacillus, Curtobacterium, Aggregatibacter, Haemophilus or Actinobacillus, preferably Terribacillus.
  • the hexosaminidase may also be a variant of a polypeptide obtained from any of these or other organisms.
  • Suitable hexosaminidases include those disclosed in WO2017186936, WO2017186937, WQ2017186943, WQ2017207770, WQ2018184873, WQ2019086520, WQ2019086528, WQ2019086530, WQ2019086532, WQ2019086521, WQ2019086526, WQ2020002604, W02020002608, W02020007863, W02020007875, W02020008024, W02020070063, W02020070249, W02020088957, W02020088958 and W02020207944.
  • a peroxidase may be comprised by the enzyme classification EC 1.11.1.7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment obtained therefrom, exhibiting peroxidase activity.
  • Suitable peroxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinopsis, e.g., from C. cinerea (EP 179,486), and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.
  • a peroxidase may also include a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity.
  • Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.11.1.10) catalyze formation of hypochlorite from chloride ions.
  • the haloperoxidase may be a chloroperoxidase.
  • the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase.
  • the vanadate- containing haloperoxidase is combined with a source of chloride ion.
  • Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
  • Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S.
  • the haloperoxidase is derivable from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97/04102; or from Drechslera hartlebii as described in WO 01/79459, Dendryphiella salina as described in WO 01/79458, Phaeotrichoconis crotalarie as described in WO 01/79461 , or Geniculosporium sp. as described in WO 01/79460.
  • Curvularia sp. in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147
  • An oxidase includes any laccase enzyme comprised by the enzyme classification EC 1 .10.3.2, or any fragment obtained therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1), an o-aminophenol oxidase (EC 1.10.3.4), or a bilirubin oxidase (EC 1.3.3.5).
  • a catechol oxidase EC 1.10.3.1
  • an o-aminophenol oxidase EC 1.10.3.4
  • a bilirubin oxidase EC 1.3.3.5
  • Preferred laccase enzymes are enzymes of microbial origin.
  • the enzymes may be obtained from plants, bacteria or fungi (including filamentous fungi and yeasts).
  • Suitable examples from fungi include a laccase derivable from a strain of Bacillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Pomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinopsis, e.g., C. cinerea, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P.
  • papilionaceus Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2238885).
  • Suitable examples from bacteria include a laccase derivable from a strain of Bacillus.
  • a laccase obtained from Coprinopsis or Myceliophthora is preferred; a laccase obtained from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora thermophila, as disclosed in WO 95/33836.
  • the detergent compositions of the present invention can also contain dispersants.
  • 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.
  • the 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 /V-oxide polymers, copolymers of N- vinylpyrrolidone and /V-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.
  • 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 agents Fluorescent whitening agents
  • the detergent composition may 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 0.5%.
  • 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-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives.
  • diaminostilbene-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-(/V-methyl-/ ⁇ /-2-hydroxy- ethylamino)-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1 ,2,3-triazol-2- yl)stilbene-2,2'-disulfonate and sodium 5-(2/7-naphtho[1 ,2-d][1 ,2,3]triazol-2-yl)-2-[((2-
  • 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-2,2'-disulfonate.
  • Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl)-disulfonate.
  • fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India.
  • Tinopal CBS-X is a 4.4'-bis-(sulfostyryl)-biphenyl disodium salt also known as Disodium Distyrylbiphenyl Disulfonate.
  • 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%.
  • the detergent compositions may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, 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 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).
  • 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 deriviatives such as those described in EP 1867808 or WO 2003/040279 (both are hereby incorporated by reference).
  • the detergent compositions of the present invention may also include one or more antiredeposition 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.
  • CMC carboxymethylcellulose
  • PVA polyvinyl alcohol
  • PVP polyvinylpyrrolidone
  • PEG polyethyleneglycol
  • 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 antiredeposition agents.
  • the detergent 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, hydroxyfunctional materials, polymeric rheology modifiers which impart shear thinning characteristics to the agueous liguid matrix of a liguid 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.
  • adjunct materials include, but are not limited to, anti-shrink agents, antiwrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liguid detergents and/or structure elasticizing agents.
  • any detergent components known in the art for use in the cleaning composition of the invention 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 detergents may be utilized. The choice of such ingredients is well within the skill of the artisan.
  • the detergent composition may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid.
  • Other detergent formulation forms include single unit dose forms such as layered forms and pouches.
  • Pouches can be configured as single or multicompartments. They can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing release of the composition from the pouch prior to water contact.
  • the pouch is made from water soluble film which encloses an inner volume, which can be divided into compartments.
  • 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).
  • the level of polymer in a film such as is at least about 60%.
  • 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 plus plasticisers such as glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof.
  • the pouches can comprise a solid laundry cleaning composition or part components and/or a liquid cleaning composition or part components separated by the water-soluble film. Compartments for liquid components can be different in composition than compartments containing solids; see e.g. US 2009/0011970 A1.
  • Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets, thereby avoiding negative storage interaction between components. 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, or up to about 35% water.
  • Concentrated liquid detergents may have lower water contents, for example not more than about 30% or not more than about 20%, e.g. in the range of about 1% to about 20%, such as from about 2% to about 15%.
  • 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 alternatively be non-aqueous.
  • Liquid detergent compositions may be formulated to have a moderate pH of e.g. from about 6 to about 10, such as about pH 7, about pH 8 or about pH 9, or they may be formulated to have a higher pH of e.g. from about 10 to about 12, such as about pH 10, about pH 11 or about pH 12.
  • liquid as used herein should be understood to encompass any kind of liquid detergent composition, for example concentrated liquids, gels, or the liquid or gel part of e.g. a pouch with one or more compartments.
  • Detergent enzymes may be included in a detergent composition by adding separate additives containing one or more enzymes, or by adding a combined additive comprising these enzymes.
  • a detergent additive i.e., a separate additive or a combined additive, can be formulated, for example, as a granulate, liquid, slurry, etc.
  • Preferred detergent additive formulations are granulates, non-dusting granulates, liquids, stabilized liquids and slurries.
  • Non-dusting granulates may be produced, e.g. as disclosed in US 4,106,991 and 4,661,452 and may optionally be coated by methods known in the art.
  • 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.
  • film-forming coating materials suitable for application by fluid bed techniques are given in GB 1483591.
  • Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according to established methods.
  • Protected enzymes may be prepared according to the method disclosed in EP 238216.
  • Enzymes 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.
  • 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.
  • a 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).
  • PEG polyethylene glycol
  • MHPC methyl hydroxy-propyl cellulose
  • PVA polyvinyl alcohol
  • 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 DNase may be formulated as a granule for example as a co-granule that combines one or more enzymes. Each enzyme will then be present in more granules securing a more uniform distribution of enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes.
  • Methods for producing multi-enzyme co-granulate for the detergent industry is disclosed in the IP.com disclosure IPCOM000200739D.
  • WO 2013/188331 Another example of formulation of enzymes using co-granulates are disclosed in WO 2013/188331 , which relates to a detergent composition comprising (a) a multi-enzyme co- granule; (b) less than 10 wt zeolite (anhydrous basis); and (c) less than 10 wt phosphate salt (anhydrous basis), wherein said enzyme co-granule comprises from 10 to 98 wt% moisture sink components and the composition additionally comprises from 20 to 80 wt% detergent moisture sink components.
  • WO 2013/188331 also relates to a method of treating and/or cleaning a surface, preferably a fabric surface comprising the steps of (i) contacting said surface with the detergent composition as claimed and described herein aqueous wash liquor, (ii) rinsing and/or drying the surface.
  • the present invention also relates to liquid compositions comprising an alkaline phosphatase and optional DNase 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).
  • an enzyme stabilizer 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).
  • fillers or carrier materials 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.
  • 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:
  • the invention relates to liquid formulations comprising:
  • 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 sulfate, potassium sulfate, magnesium sulfate, sodium thiosulfate, calcium carbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol, lactose, starch, PVA, acetate and phosphate, preferably selected from the group consisting of sodium sulfate, dextrin, cellulose, sodium thiosulfate, kaolin and calcium carbonate.
  • a formulating agent selected from the group consisting of polyol, sodium chloride, sodium benzoate, potassium sorbate, sodium sulfate, potassium sulfate, magnesium sulfate, sodium thiosulfate, calcium carbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol, lactose, starch, PVA,
  • 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.
  • MPG propylene glycol
  • the liquid formulation comprises 20-80% polyol (/.e., total amount of polyol), e.g., 25-75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% polyol.
  • 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.
  • MPG propylene glycol
  • the liquid formulation comprises 20-80% polyol (/.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).
  • polyol is selected from the group consisting of glycerol, sorbitol and propylene glycol (MPG).
  • the preservative is selected from the group consisting of sodium sorbate, potassium sorbate, sodium benzoate and potassium benzoate or any combination thereof.
  • 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.
  • the liquid formulation comprises 0.001-2% w/w preservative (/.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.
  • the liquid formulation further comprises one or more additional enzymes, e.g. as described above.
  • the alkaline phosphatase and optional DNase of the invention are suitable for use in a cleaning process, for example for laundry or hard surface cleaning, in particular for laundry.
  • one aspect of the invention relates a method for laundering an item, wherein the item is a textile, the method comprising: a) exposing the item to a wash liquor comprising a polypeptide having alkaline phosphatase activity and a polypeptide having DNase activity; b) completing at least one wash cycle; and optionally c) rinsing the item.
  • the invention relates to a method for laundering an item, wherein the item is a textile, the method comprising: a) exposing the item to a wash liquor comprising a polypeptide having alkaline phosphatase activity as defined elsewhere herein, and optionally further comprising a polypeptide having DNase activity; b) completing at least one wash cycle; and optionally c) rinsing the item.
  • polypeptide having alkaline phosphatase activity for use in these methods herein is preferably an alkaline phosphatase polypeptide as disclosed elsewhere herein.
  • polypeptide having DNase activity is also preferably a DNase polypeptide as defined elsewhere herein.
  • the pH of the liquid wash liquor solution is typically in the range about 5.5 to about 10, more typically in the range of about 7 to about 9, such as in the range of about 7 to about 8.5 or about 7 to about 8.
  • the wash liquor may have a temperature in the range of 5°C to 95°C, or in the range of 10°C to 80°C, in the range of 10°C to 70°C, in the range of 10°C to 60°C, in the range of 10°C to 50°C, in the range of 15°C to 40°C or in the range of 20°C to 30°C.
  • the concentration of the alkaline phosphatase in the wash liquor is typically in the range of from 0.0001 mg/l to 10 mg/l enzyme protein, from 0.0002 mg/l to 10 mg/l, from 0.001 mg/l to 10 mg/l, from 0.002 mg/l to 10 mg/l, from 0.01 mg/l to 10 mg/l, from 0.02 mg/l to 10 mg/l, from 0.1 mg/l to 10 mg/l, from 0.2 mg/l to 10 mg/l, or from 0.2 mg/l to 5 mg/l.
  • concentration of a DNase, when included, in the wash liquor will typically be in the same ranges as for the alkaline phosphase.
  • a cleaning composition comprising a polypeptide having DNase activity, a polypeptide having alkaline phosphatase activity and at least one detergent adjunct ingredient.
  • SEQ ID NO: 3 SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO:
  • SEQ ID NO: 28 SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31 , SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41 , SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51 , SEQ ID NO: 52, SEQ ID NO: 53, SEQ ID NO: 54, SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO: 61 , SEQ ID NO: 62, SEQ ID
  • polypeptide derived from the polypeptide of (a) or (b), wherein the N- and/or C- terminal end has been extended by the addition of 1 to 50 amino acids, such as 1 to 40, 1 to 30 or 1 to 20 amino acids; and
  • polypeptide having alkaline phosphatase activity is selected from the group consisting of polypeptides having at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94% or at least 95% sequence identity to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ
  • SEQ ID NO: 26 SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO:
  • the cleaning composition of paragraph 3, wherein the polypeptide having alkaline phosphatase activity has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97% or at least 98% sequence identity to SEQ ID NO: 1.
  • polypeptide having alkaline phosphatase activity is a variant of SEQ ID NO: 1 having a substitution in at least one position selected from the group consisting of positions 77, 90, 94, 117, 119, 148, 156, 208, 212, 216, 220, 224, 225, 228, 245, 246, 248, 270, 271 , 291 , 292, 303 and 381.
  • the polypeptide having alkaline phosphatase activity comprises at least one substitution selected from the group consisting of A77T, N90I, A94P, I117L, H119A, N148F, M156F, K208A, R212M, M216V, K220P, K220E, E224D, T225E, D228R, Q245L, I246F, W248K, K270G, A271 R, S291G, T292A, Y303L and G381S. 7.
  • polypeptide having alkaline phosphatase activity is a variant of SEQ ID NO: 1 having at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 61 , SEQ ID NO: 62, SEQ ID NO: 63,
  • composition comprises a polypeptide having DNase activity selected from the group consisting of: a) a polypeptide having 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% or at least 95% sequence identity to SEQ ID NO: 83; b) a polypeptide having 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% or at least 95% sequence identity to SEQ ID NO: 82; and c) a variant of SEQ ID NO: 82, wherein the variant has 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% or at least 95% sequence identity to SEQ I D NO: 82 or SEQ
  • the polypeptide having DNase activity is a variant of SEQ ID NO: 82, wherein the variant has 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% or at least 95% sequence identity to SEQ ID NO: 82 or SEQ ID NO: 83 and comprises, compared to SEQ ID NO: 82, one or more substitutions, preferably 2 or more, 3 or more, 4 or more, 5 or more, 6 or more, 7 or more, 8 or more, 9 or more or 10 or more substitutions, selected from the group consisting of T1 I, S13Y, T22P, S25P, S27L, S39P, D56I, S57W, S59V, T65V, V76L, T77Y, Q109R, S116D, T127V, S144P, A147H, G149N, S167L, G175D and S181 L.
  • the polypeptide having DNase activity is a variant of SEQ ID NO: 82, wherein the variant has 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% or at least 95% sequence identity to SEQ ID NO: 82 or SEQ ID NO: 83 and comprises, compared to SEQ ID NO: 82, comprises two or more substitutions, such as three, four, five or more substitutions, selected from the group consisting of N61 D, T65I, T65V, S82R, K107Q, T127S, T127V, G149N, S164D and L181S.
  • polypeptide having DNase activity further comprises at least one substitution selected from the group consisting of Q14R, Q14W, K21 L, P25S, L33K, Q48D, D56I, D56L, S66Y, S68L, Y77T, S102Y, S106A, R109Q, R109T, D116S, D116W, T171W, L181T and L181W.
  • the polypeptide having DNase activity comprises a set of substitutions selected from the group consisting of: a) G149N together with at least one of the substitutions N61 D, T65I, T65V, S82R, K107Q, T127S, T127V, S164D and L181S; b) T65I or T65V together with at least two of the substitutions N61 D, S82R, K107Q, T127S, T127V, G149N, S164D and L181S; c) N61 D together with at least two of the substitutions T65I/V, S82R, K107Q, T127S/V, G149N, S164D and L181S, preferably at least two of the substitutions T65I/V, S82R, K107Q, T127S and S164D; d) S82R togetherwith at least two of the substitutions N61 D, T65I, T65V, K107Q, T127S, T127V,
  • composition of any of paragraphs 1-8, wherein the composition comprises a polypeptide having DNase activity having 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% or at least 95% sequence identity to SEQ ID NO: 86; or to the polypeptide of SEQ ID NO: 86 which is N- terminally truncated by up to about 20 amino acid residues, for example by an N-terminal truncation of 15-17 amino acid residues.
  • the polypeptide having DNase activity is a variant of SEQ ID NO: 86, wherein the variant comprises at least two alterations selected from the group consisting of S69V, Q102E, S26*, D32Q, K36C,H, G37R, F43W, D46G, A55I, N68D, A76I, K82S,T, P84D,T, K86G,L,N,Q,T,V,Y, A91 R, L92E, K95I, P97E,N, A101 E, K105N,G,Q,T,D, F112Y.W, L129K, N133Q, V138C, N140H, G141Q.R, S144E, N146A, K147N.E, V148I, A149D,E,F, Q150D, P153D.V, S154E, K155E,F,L,S,T, Q157D.E, Q158D, T159Q, K160D, T1
  • the polypeptide having DNase activity is a variant of SEQ ID NO: 86, wherein the variant comprises at least two substitutions, such as at least three substitutions, selected from the group consisting of A111 P, D32E, V35I, S69V, Q102E, K105N and G181 N; and optionally wherein the variant further comprises two or more substitutions selected from the group consisting of S26H, D32E, V35I, K65E, K67A, S69E, S69V, S98R, Q102E, K105N, S115T, Q150E, Q157E, T159Q, G161 R, A172E, G181 N, S182Y, S182V, K185E, V187N, K192I, A206G, Q208V and K212E.
  • a cleaning composition comprising a polypeptide having alkaline phosphatase activity and at least one detergent adjunct ingredient, wherein the polypeptide having alkaline phosphatase activity is selected
  • SEQ ID NO: 3 SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO:
  • SEQ ID NO: 28 SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31 , SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41 , SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51 , SEQ ID NO: 52, SEQ ID NO: 53, SEQ ID NO: 54, SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO: 61 , SEQ ID NO: 62, SEQ ID
  • polypeptide having at least 70% sequence identity such as at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97% or at least 98% sequence identity, to SEQ ID NO: 1 ;
  • polypeptide derived from the polypeptide of (a) or (b), wherein the N- and/or C- terminal end has been extended by the addition of 1 to 50 amino acids, such as 1 to 40, 1 to 30 or 1 to 20 amino acids; and
  • polypeptide having alkaline phosphatase activity comprises at least one substitution selected from the group consisting of A77T, N90I, A94P, I117L, H119A, N148F, M156F, K208A, R212M, M216V, K220P, K220E, E224D, T225E, D228R, Q245L, I246F, W248K, K270G, A271 R, S291G, T292A, Y303L and G381S.
  • polypeptide having alkaline phosphatase activity is a variant of SEQ ID NO: 1 having at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 61 , SEQ ID NO: 62, SEQ ID NO:
  • the cleaning composition of any of the preceding paragraphs comprising one or more cleaning adjunct ingredients selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, other enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric hueing agents, anti-foaming agents, dispersants, processing aids, and/or pigments.
  • cleaning adjunct ingredients selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, other enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources
  • composition in the form of 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 or concentrated liquid.
  • a method for laundering an item, wherein the item is a textile comprising: a) exposing the item to a wash liquor comprising a polypeptide having alkaline phosphatase activity and a polypeptide having DNase activity; b) completing at least one wash cycle; and optionally c) rinsing the item.
  • a method for laundering an item, wherein the item is a textile comprising: a) exposing the item to a wash liquor comprising a polypeptide having alkaline phosphatase activity as defined in any of paragraphs 17-21 ; b) completing at least one wash cycle; and optionally c) rinsing the item.
  • a method for laundry or hard surface cleaning comprising exposing a textile or a hard surface to a cleaning composition according to any of paragraphs 1-24.
  • polypeptide having alkaline phosphatase activity wherein the polypeptide is selected from the group consisting of:
  • SEQ ID NO: 3 SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO:
  • SEQ ID NO: 28 SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31 , SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41 , SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51 , SEQ ID NO: 52, SEQ ID NO: 53, SEQ ID NO: 54, SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO: 61 , SEQ ID NO: 62, SEQ ID
  • 1 to 120 amino acids such as 1 to 100, 1 to 80, 1 to 60 or 1 to 40 amino acids;
  • polypeptide derived from the polypeptide of (a) or (b), wherein the N- and/or C- terminal end has been extended by the addition of 1 to 50 amino acids, such as 1 to 40, 1 to 30 or 1 to 20 amino acids; and
  • polypeptide having alkaline phosphatase activity of paragraph 32 wherein the polypeptide is as defined in any of paragraphs 3-8.
  • 34 A polynucleotide encoding a polypeptide having alkaline phosphatase activity as defined in any of paragraphs 2-8, a nucleic acid construct comprising said polynucleotide, or an expression vector comprising said polynucleotide.
  • a recombinant host cell comprising a polynucleotide encoding a polypeptide having alkaline phosphatase activity as defined in any of paragraphs 2-8 operably linked to one or more control sequences that direct production of the polypeptide.
  • a method of producing a polypeptide having alkaline phosphatase activity comprising (a) cultivating the recombinant host cell of paragraph 35 under conditions conducive for production of the polypeptide; and optionally (b) recovering the polypeptide.
  • 75 pl phosphatase-containing enzyme solution (diluted in MQ water with 0.01 % (v/w) Triton X-100) is dispensed in a microtiter plate well, e.g. a NUNC 269620 96-well plate, and 75 pl substrate is added (for preparing the substrate, two 5 mg p-nitrophenyl phosphate tablets (Sigma- Aldrich, Cat.No. 20-106) are dissolved in 10 ml 50 mM Hepes, 100 mM NaCI, 1mM CaCI2, 1 mM MgCI2, 1 mM ZnCI2, pH 7.0). The plate is sealed and incubated for 15 minutes, and shaken at 750 rpm at 37°C.
  • 75 pl stop-reagent (0.5 M NaOH) is added and the absorbance at 405 nm is measured in a microtiter plate spectrophotometer.
  • a blank (75 pl 0.01 % (v/w) Triton X-100 + 75 pl substrate solution) is also incubated for 15 minutes, 75 pl stopreagent is added, and the absorbance at 405 nm is measured. This value is subtracted from the phosphatase readings.
  • One phosphatase unit is defined as the enzyme activity that releases 1 pmol phosphate/min under the given reaction conditions (buffer blind subtracted).
  • the absorbance of 1 pmol p-nitrophenol is determined to be 56 AU (absorbancy units) under assay conditions.
  • DNase activity may be determined on DNase Test Agar with Methyl Green (BD, Franklin Lakes, NJ, USA), prepared according to the supplier’s manual. Briefly, 21 g of agar is dissolved in 500 ml water and then autoclaved for 15 min at 121 °C. Autoclaved agar is temperated to 48°C in water bath, and 20 ml of agar is poured into petri dishes and allowed to solidify by incubation overnight at room temperature. On solidified agar plates, 5 pl of enzyme solutions are added and DNase activity is observed as colorless zones around the spotted enzyme solutions.
  • DNase Test Agar with Methyl Green BD, Franklin Lakes, NJ, USA
  • a Terg-O-ToMeter is an apparatus that simulates “top-loader/vertical drum” washing machine, using a series of metal beakers with a volume of typically 1-2 liters, each fitted with an agitator which rotates in a back-and-forth manner at a controlled speed (e.g. 120 rpm) to simulate the agitation mode occurring in commercial top-loader washing machines.
  • the mini- TOM works as a TOM apparatus, but with a reduced volume of 0.2L.
  • the assay is used to test several conditions on several swatches at the time. Swatches are cut into 2cm diameter pieces and added into the beakers containing water and detergent. The agitation speed and the temperature are controlled during the wash time. After washing, the swatches are rinsed, dried for 24 hours, and the intensity (remission, determined as explained in Example 5 below) of the swatch is measured.
  • Alkaline phosphatase genes derived from fungal strains were isolated from environmental samples by standard microbiological isolation techniques.
  • Chromosomal DNA from individual strains was isolated by DNeasy® Plant Maxi Kit (Qiagen, Hilden, Germany). 5 pg of chromosomal DNA were sent for full genome sequencing using Illumina technology. Genome sequencing, the subsequent assembly of reads and the gene discovery (i.e. annotation of gene functions) is known to the person skilled in the art and the service can be purchased commercially. The genome sequences were analyzed for putative ALP from the PFAM database families PF00245. This analysis identified genes encoding putative ALP, which were subsequently cloned and recombinantly expressed in Aspergillus oryzae.
  • the ALP genes were amplified by PCR from above isolated genomic DNA.
  • the purified PCR product was cloned into the previously digested pCaHj505 or pDAU724 by ligation with an IN-FUSIONTM CF Dry-down Cloning Kit (Clontech Laboratories, Inc., Mountain View, CA, USA) according to the manufacturer's instructions.
  • the ligation mixture was used to transform E. coli TOP10 chemically competent cells. Colonies containing the corresponding ALP genes were selected and verified by DNA sequencing (by SinoGenoMax Company Limited, Beijing, China).
  • the correct ALP containing colony was cultivated overnight in 3 ml of LB medium supplemented with 100 pg of ampicillin per ml.
  • Plasmid DNA was purified using a Qiagen Spin Miniprep kit (Cat. 27106) (QIAGEN GmbH, Hilden, Germany) according to the manufacturer’s instructions.
  • Protoplasts of Aspergillus oryzae MT3568 were prepared according to W095/002043.
  • Protoplasts of Aspergillus oryzae DALI785 were prepared according to WO2018/113745. 100 pl of protoplasts were mixed with 2.5-10 pg of the Aspergillus expression vector (above extracted plasmid) comprising the ALP gene and 250 pl of 60% PEG 4000, 10mM CaCh, and 10mM Tris- HCI, pH 7.5 and gently mixed.
  • the mixture was incubated at 37°C for 30 minutes and the protoplasts were spread onto COVE sucrose plates for selection. After incubation for 4-7 days at 37°C spores of 4 transformants were inoculated into 3 ml of Dap4C medium.
  • the DNA encoding sequences of alkaline phosphatase mature peptides were ordered as synthetic genes at Twist Bioscience.
  • the synthetic DNA fragments were directionally assembled to a Bacillus expression vector described in WO2012/025577 by the standard Golden Gate cloning method using Bsal and T4 DNA ligase enzymes. Briefly, the DNA encoding the mature peptide of the gene was cloned in frame to a Bacillus clausii secretion signal (BcSP; with the following amino acid sequence: MKKPLGKIVASTALLISVAFSSSIASA (SEQ ID NO: 84). BcSP replaced the native secretion signal in the gene.
  • BcSP Bacillus clausii secretion signal
  • an affinity tag sequence was introduced to ease the purification process (His-tag; with the following amino acid sequence: HHHHHHPR (SEQ ID NO: 85).
  • the gene that was expressed therefore comprised the BcSP sequence followed by the His-tag sequence followed by the mature wild-type alkaline phosphatase gene sequence.
  • the final expression plasmid (BcSP-His-tag-alkaline phosphatase) was transformed into a Bacillus subtilis expression host.
  • the alkaline phosphatase BcSP-fusion gene was integrated by homologous recombination into the Bacillus subtilis host cell genome upon transformation.
  • the gene construct was expressed under the control of a triple promoter system (as described in WO 99/43835).
  • the gene coding for chloramphenicol acetyltransferase was used as marker (as described in Diderichsen et al., 1993, Plasmid 30: 312-315)). Transformants were selected on LB media agar supplemented with 6 microgram of chloramphenicol per ml. One recombinant Bacillus subtilis clone containing the alkaline phosphatase expression construct was selected and was cultivated on a rotary shaking table in 500 ml baffled Erlenmeyer flasks each containing 100 ml yeast extract-based media. After 3 days cultivation time at 30 °C, the enzyme containing supernatant was harvested by centrifugation and the enzyme was purified by His-tag purification.
  • alkaline phosphatase (ALP) from culture broth was firstly applied with hydrophobic interaction chromatography on an AKTA Chromatography system (Cytiva), then if needed, ion exchange chromatography was applied. The difference for all the molecules was buffer type, pH and salt concentration.
  • the conductivity of culture supernatant of recombinant ALP was adjusted to about 190 mS/cm by adding ammonium sulfate, then the culture broth was loaded into Phenyl Sepharose High Performance column (Cytiva, 17108203) equilibrated with 20mM Tris-HCI at pH7.0 containing 2.0M ammonium sulfate. A gradient decrease of ammonium sulfate concentration from 2.0M to 0 was set up as elution condition. The elution fractions and flow-through faction were assayed by SDS-PAGE. ALP activity was determined as described below.
  • fractions with enzyme activity were pooled together and then diafiltrated with 20mM PBS at pH7.0.
  • the protein concentration was determined by QubitTM Protein Assay Kit (Invitrogen, Q33212).
  • His-tagged alkaline phosphatases were purified by immobilized metal chromatography (IMAC) using Ni 2+ as the metal ion on 5 mL HisTrap Excel columns (GE Healthcare Life Sciences). The purification took place at pH 7 and the bound protein was eluted with imidazole. The purity of the purified enzymes was checked by SDS-PAGE and the concentration of the enzyme determined by absorbance at 280 nm after a buffer exchange in 50mM HEPES, 100 mM NaCI, pH 7.0 Example 5
  • wash performance assays were performed using the mini-TOM apparatus described above to test the efficacy of an alkaline phosphatase and a DNase individually and in combination.
  • the assays were performed on different commercial stain swatches using one of two different detergents, a conventional detergent (detergent 1) and a detergent containing a plant-based surfactant (detergent 2).
  • a conventional detergent detergent 1
  • a detergent containing a plant-based surfactant detergent 2
  • Information on the swatches used and other details of the assay setup are provided in Table 1 below.
  • Information on the composition of detergents 1 and 2 is provided in Tables 2 and 3.
  • Stain sheets were cut into swatches with a diameter of 2 cm.
  • the mini-TOM beakers were prepared with 200 ml of detergent solution and placed in the TOM apparatus, after which the mechanical rotation and temperature regulation was turned on. Enzymes and swatches were added when the wash temperature was reached. After 30 minutes of washing, swatches were transferred to a strainer to drain the wash load. After a quick rinse under running water, the swatches were squeeze and transferre to 5L beakers containing cold tap water. The swatches washed in blank conditions without enzyme were rinsed separately from the samples containing enzymes. Swatches were left to dry on blotting paper at room temperature in the dark for 24 h.
  • the dried swatches were evaluated using a Digi-Eye colour measurement and imaging system by VeriVide.
  • the DigiEye is a controlled digital imaging system for measuring color and capturing repeatable images.
  • the results of the mini-TOM assays are provided below in Tables 4, 5, 6, 7, 8 and 9 as remission values for individual enzyme treatments and delta remission (A Remission) values based on a reference treatment for each table.
  • the delta remission values are calculated as the remission value of a particular enzyme treatment, typically ALP alone or ALP with a DNase and/or Medley® Brilliant, minus the remission value of the reference treatment for the table in question, where the reference treatment can be a blank (no enzyme) or another enzyme treatment as indicated in the tables.
  • Table 4 shows wash performance in the conventional detergent (i.e., containing conventional surfactants; Detergent 1) on two stains, where the effect of different dosages of the alkaline phosphatase (ALP; SEQ ID NO: 79) is compared with a DNase (SEQ ID NO: 82) dosed at 0.2 ppm and with the Medley® Brilliant enzyme mixture dosed at 0.025 mg/L (0.025 ppm). Delta remission values in Table 4 are calculated based on a blank (no enzyme).
  • ALP alkaline phosphatase
  • Table 4 Wash performance of ALP compared to DNase or Medley® Brilliant on stain swatches in Detergent 1 (conventional detergent). A Remission is remission minus the blank value.
  • Table 5 shows wash performance in the conventional detergent on two different stains, where the effect of different dosages of the alkaline phosphatase (ALP; SEQ ID NO: 79) either alone or together with the Medley® Brilliant enzyme mixture dosed at 0.025 mg/L (0.025 ppm) is determined. Delta remission values in Table 5 are calculated based on the remission of the Medley® Brilliant treatment alone.
  • ALP alkaline phosphatase
  • Table 5 Wash performance of ALP alone or with Medley® Brilliant on stain swatches in Detergent 1 (conventional detergent). A Remission is remission minus Medley® Brilliant value.
  • Table 6 shows wash performance in the conventional detergent on one stain, where the effect of different dosages of the alkaline phosphatase (ALP; SEQ ID NO: 79) together with a DNase (SEQ ID NO: 82) dosed at 0.2 ppm and with the Medley® Brilliant enzyme mixture dosed at 0.025 mg/L (0.025 ppm) is determined. Delta remission values in Table 6 are calculated based on the remission of the treatment with the DNase and Medley® Brilliant without the alkaline phosphatase. Table 6: Wash performance of ALP with DNase and Medley® Brilliant on stain swatches in Detergent 1 (conventional detergent). A Remission is remission minus Medley® Brilliant + DNase value.
  • Table 7 shows wash performance in the plant-based detergent on two different stains, where the effect of different dosages of the alkaline phosphatase (ALP; SEQ ID NO: 79) either alone or together with a DNase (SEQ ID NO: 82) dosed at 0.2 ppm is determined. Delta remission values in Table 7 are calculated based on the remission of the DNase treatment alone. Table 7: Wash performance of ALP alone or with DNase on stain swatches in Detergent 2 (plant-based detergent). A Remission is remission minus DNase value.
  • ALP alkaline phosphatase
  • Table 8 shows wash performance in the plant-based detergent on two different stains, where the effect of different dosages of the alkaline phosphatase (ALP; SEQ ID NO: 79) together with the Medley® Brilliant enzyme mixture dosed at 0.025 mg/L (0.025 ppm) is determined. Delta remission values in Table 8 are calculated based on the remission of the treatment with Medley® Brilliant alone.
  • ALP alkaline phosphatase
  • Table 8 Wash performance of of ALP alone or with Medley® Brilliant on stain swatches in Detergent 2 (plant-based detergent). A Remission is remission minus Medley® Brilliant value.
  • Example 6 Wash performance of of ALP alone or with Medley® Brilliant on stain swatches in Detergent 2 (plant-based detergent). A Remission is remission minus Medley® Brilliant value.
  • a Pseudomonas fluorescens isolate from Iceland was used as a model microorganism in the present example.
  • Pseudomonas fluorescens was re-streaked on Tryptone Soya Agar (TSA) (pH 7.3) (CM0131 ; Oxoid Ltd, Basingstoke, UK) and incubated for 3 days at 30°C.
  • TSA Tryptone Soya Agar
  • CM0131 Oxoid Ltd, Basingstoke, UK
  • a single colony was inoculated into 10 mL of TSB and the culture was incubated for 19 hours at 30°C with shaking (BenchTop Orbital Shaker MaxQ 4000 at 200rpm).
  • the culture was diluted to an OD of 0.03 in fresh TSB and 1 .65 mL aliquots were added to the wells of 12-well polystyrene flat-bottom culture plates (3512; Costar, Corning Incorporated, Corning, N.Y., USA), in which round swatches (diameter 2 cm) of sterile textile (WFK10A, 100% cotton) had been placed.
  • WFK10A sterile textile
  • Sterile TSB was added to control wells.
  • the plates were incubated at 30°C and 150 rpm on an orbital shaker (Titramax 1000, Heidolph Instruments GmbH & Co. KG, Germany). After 72 h, the swatches were rinsed twice with 2 mL 0.9% (w/v) NaCI.
  • Sebum swatches (sebum tracers) were prepared by spotting 50 L of 1 % (w/v) sebum solution on round swatches (diameter 2 cm) textile (WFK20A) and drying overnight.
  • the 1 % (w/v) sebum solution was prepared by adding melted Sebum Bey (CFT, Center For Testmaterials BV, Netherlands) in MiliQ water with 0.4% (w/v) Tween® 80.
  • the combination of alkaline phosphatase and DNase provides superior anti-redeposition properties in model J detergent as compared to the individual enzymes.

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Abstract

La présente invention concerne des polypeptides ayant une activité de phosphatase alcaline, des compositions de nettoyage comprenant un polypeptide ayant une activité de phosphatase alcaline et éventuellement un polypeptide ayant une activité de DNase, et l'utilisation des compositions dans un processus de nettoyage tel que le nettoyage du linge.
PCT/EP2024/059495 2023-04-12 2024-04-08 Compositions comprenant des polypeptides ayant une activité de phosphatase alcaline Ceased WO2024213513A1 (fr)

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