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WO2002077242A2 - Xyloglucanases de la famille 74 - Google Patents

Xyloglucanases de la famille 74 Download PDF

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Publication number
WO2002077242A2
WO2002077242A2 PCT/DK2002/000210 DK0200210W WO02077242A2 WO 2002077242 A2 WO2002077242 A2 WO 2002077242A2 DK 0200210 W DK0200210 W DK 0200210W WO 02077242 A2 WO02077242 A2 WO 02077242A2
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Prior art keywords
enzyme
xyloglucanase
dna
seq
sequence
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WO2002077242A3 (fr
Inventor
Fiona Duffner
Carsten SJØHOLM
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Novozymes AS
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Novozymes AS
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Priority to AU2002249102A priority Critical patent/AU2002249102A1/en
Publication of WO2002077242A2 publication Critical patent/WO2002077242A2/fr
Publication of WO2002077242A3 publication Critical patent/WO2002077242A3/fr
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    • 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)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
    • 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

Definitions

  • the present invention relates to xyloglucanases belonging to family 74 of glycosyl hydrolases, preferably to enzymes exhibiting xyloglucanase activity as their major enzymatic activity in the neutral and alkaline pH ranges; to an enzyme preparation comprising the enzyme of the invention; to a method of producing such enzymes; and to methods for using such enzymes in the textile, detergent and cellulose fiber processing industries .
  • Xyloglucanase activity has not yet been included in the classification of enzymes provided by the Enzyme Nomenclature (1992) . Hitherto, this enzymatic activity has simply been classified as glucanase activity and has often been believed to be identical to cellulolytic activity (EC 3.2.1.4), i.e. activity against ⁇ -1, 4-glycosidic linkages in cellulose or cellulose derivative substrates, or at least to be a side activity in enzymes having cellulolytic activity.
  • a true xyloglucanase is a true xyloglucan specific enzyme capable of catalyzing the solubilisation of xyloglucan to xyloglucan oligosaccharides but which does not exhibit substantial cellulolytic activity, e.g. activity against the conventionally used cellulose-like substrates CMC (carboxymethylcellulose) , HE cellulose and Avicel (microcrystalline cellulose) .
  • CMC carboxymethylcellulose
  • HE cellulose HE cellulose
  • Avicel microcrystalline cellulose
  • Xyloglucanase activity is disclosed in Nincken, J.P., Beldman, G. , and Voragen, A.G.J. Substrate-specificity of endoglucanases - what determines xyloglucanase activity. Carbohydrate Research 298 (4) :299-310, 1997, wherein three different endoglucanases Endol, EndoV and EndoVI from Trichoderma viride (similar to T. reesei) are characterized. Endol, EndoV and EndoVI belongs to family 5, 7 and 12 of glycosyl hydrolases, respectively, see Henrissat, B.
  • Patent Application PCT/DKOl/00132 discloses xyloglucanases cloned from Paenibacillus pabuli (family 5) and expressed in Bacillus subtilis .
  • International Patent Application PCT/DKOl/00116 discloses xyloglucanases cloned from Paenibacillus polymyxa (family 44) and expressed in Bacillus subtilis .
  • the inventors have now found enzymes having substantial xyloglucanase activity, which enzymes belong to family 74 of glycosyl hydrolases . It is contemplated that these xyloglucanase enzymes perform excellent in conventional detergent compositions, especially in liquid detergent compositions.
  • the inventors have succeeded in cloning and expressing a family 74 xyloglucanase derived from the marine organism Jonesia.
  • the invention relates to a polypeptide exhibiting xyloglucanase activity as its major enzymatic antivity, which enzyme belongs to family 74 of glycosyl hydrolases and is endogenous to a bacterium, particularly an alkalophilic bacterium, and more particularly a bacterial strain belonging to the genus Jonesia .
  • the invention relates- to a family 74 xyloglucanase selected from one of (a) a polypeptide encoded by the DNA sequence of positions 72-2820 of SEQ ID NO: 1; (b) a polypeptide produced by culturing a cell comprising the sequence of positions 72-2820 of SEQ ID NO : 1 under conditions wherein the DNA sequence is expressed; (c) a xyloglucanase enzyme having a sequence of at least 60% identity to positions 24-940 of SEQ ID NO: 2 when identity is determined by the Clustal method with a PAM250 residue table and the default settings of the Megalign program in the Lasergene package using a GAP creation penalty of 3 and Ktuple of 1; and (d) a polypeptide encoded by a DNA sequence that hybridizes to the DNA sequence of SEQ ID NO : 1 under medium stringency conditions, wherein the medium stringency conditions comprise hybridization in 5xSSC at 45°C and washing in 2xSSC at
  • the invention provides an expression vector comprising a DNA segment which is e.g. a polynucleotide molecule of the invention; a cell comprising the DNA segment or the expression vector; and a method of producing a exhibiting xyloglucanase enzyme, which method comprises culturing the cell under conditions permitting the production of the enzyme, and recovering the enzyme from the culture .
  • the invention provides an isolated xyloglucanase enzyme being free from homologous impurities .
  • the novel enzyme of the present invention is useful for the treatment of cellulosic material, especially cellulose- containing fiber, yarn, woven or non-woven fabric.
  • the treatment can be carried out during the processing of cellulosic material into a material ready for garment manufacture or fabric manufacture, e.g. in the desizing or scouring step; or during industrial or household laundering of such fabric or garment .
  • the present invention relates to an enzyme preparation comprising a xyloglucanase enzyme of the invention and conventional fillers or stabilizers; a detergent composition comprising a xyloglucanase enzyme having substantial xyloglucanase activity in the neutral or alkaline range; and to use of the enzyme of the invention for the treatment of cellulose-containing fibers, yarn, woven or non- woven fabric .
  • the present invention has now made it possible to use a xyloglucanase in detergent compositions, preferably liquid laundry detergent compositions, for removing or bleaching certain soils or stains present on laundry, especially soils and spots resulting from xyloglucan-containing food, plants, and the like. Further, it is contemplated that treatment with detergent compositions comprising the novel enzyme can prevent binding of . certain soils to the xyloglucan left on the cellulosic material.
  • the xyloglucanase of the invention may be obtained from a bacterium belonging to a strain of the genus Jonesia, in particular a strain of Jonesia sp.
  • the xyloglucanase of this invention is obtained from the strain Jonesia sp . , DSM 14140. It is at present contemplated that a DNA sequence encoding an enzyme having similar functional properties as the xyloglucanase from with Jonesia sp . , DSM 14140 and having an amino acid sequence identity of at least 60% to this xyloglucanase may be obtained from other strains belonging to the genus Jonesia . The strain Jonesia sp .
  • the term "obtained from”, “derived from”, “obtainable from” or “derivable from”, as used herein in connection with a specific source means that the enzyme is produced or can be produced by the specific source, or by a cell in which a gene from the source have been inserted.
  • enzyme preparation is intended to mean either be a conventional enzymatic fermentation product, possibly isolated and purified, from a single species of a microorganism, such preparation usually comprising a number of different enzymatic activities; or a mixture of monocomponent enzymes, preferably enzymes derived from bacterial or fungal species by using conventional recombinant techniques, which enzymes have been fermented and possibly isolated and purified separately and which may originate from different species, preferably fungal or bacterial species; or the fermentation product of a microorganism which acts as a host cell for expression of a recombinant xyloglucanase, but which microorganism simultaneously produces other enzymes, e.g.
  • expression vector denotes a DNA molecule, linear or circular, that comprises a segment encoding a polypeptide of interest operably linked to additional segments that provide for its transcription.
  • additional segments may include promoter and terminator sequences, and may optionally include one or more origins of replication, one or more selectable markers, an enhancer, a polyadenylation signal, and the like.
  • Expression vectors are generally derived from plasmid or viral DNA, or may contain elements of both.
  • the expression vector of the invention may be any expression vector that is conveniently subjected to recombinant DNA procedures, and the choice of vector will often depend on the host cell into which the vector is to be introduced.
  • the vector may be an autonomously replicating vector, i.e. a vector that exists as an
  • H- 3 CQ ⁇ ⁇ ⁇ ⁇ C Q ⁇ 0 Hi Cb ⁇ ⁇ 1
  • an isolated polynucleotide of the invention will hybridize to similar sized regions of SEQ ID NO: 1 or a sequence complementary thereto, under at least medium stringency conditions.
  • polynucleotides of the invention will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO: 1 or the sequence shown in positions 72-2820 of SEQ ID NO : 1 or any probe comprising a subsequence of SEQ ID NO:l having a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail below.
  • Suitable experimental conditions for determining hybridization at medium or high stringency between a nucleotide probe and a homologous DNA or RNA sequence involve pre-soaking of the filter containing the DNA fragments or RNA to w w t t ⁇ ⁇
  • a library is then prepared from chromosomal DNA of a positive cell line.
  • a DNA sequence of the invention encoding an polypeptide having xyloglucanase activity can then be isolated by a variety of methods, such as by probing with probes designed from the sequences disclosed in the present specification and claims or with one or more sets of degenerate probes based on the disclosed sequences.
  • a DNA sequence of the invention can also be cloned using the polymerase chain reaction, or PCR (Mullis, U.S. Patent 4,683,202), using primers designed from the sequences disclosed herein.
  • the DNA library can be used to transform or transfect host cells, and expression of the DNA of interest can be detected with an antibody (monoclonal or polyclonal) raised against the xyloglucanase cloned from Jonesia sp. , e.g. from Jonesia sp . , DSM 14140, expressed and purified as described in Materials and Methods and the Examples, or by an activity test relating to a polypeptide having xyloglucanase activity.
  • an antibody monoclonal or polyclonal
  • sequence of amino acids nos. 24-940 of SEQ ID NO: 2 is a mature xyloglucanase sequence including the catalytic active domain.
  • the present invention also provides xyloglucanase polypeptides that are substantially homologous to the polypeptide of amino acids nos. 24-940 of SEQ ID NO: 2 and species homologs (paralogs or orthologs) thereof.
  • substantially homologous is used herein to denote polypeptides having 60% , preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 95%, more preferably at least 97%, and even more preferably at least 99%, sequence identity to the sequence shown in amino acids nos. 24- 940 of SEQ ID NO: 2 or their orthologs or paralogs. Such polypeptides will most preferably be 98% or more identical to the sequence shown in amino acids nos. 24-940 of SEQ ID NO : 2 or its orthologs or paralogs.
  • Percent sequence identity is determined by conventional methods, by the Clustal method (Thompson, J.D., Higgins, D.G., and Gibson, T.J., (1994) , Nucleic Acids Research 22, 4673-4680) with the default settings of the Megalign program in the Lasergene package (DNAstart Inc., 1228 South Park Street, Madison, Wisconsin 53715) .
  • the settings for multiple alignment are: GAP penalty of 10, and GAP length penalty 10; while the pair-wise alignment parameters are GAP penalty of 3 and Ktuple of 1.
  • Sequence identity of polynucleotide molecules is determined by the Clustal method (Thompson, J.D., Higgins, D.G., and Gibson, T.J., (1994) ,Nucleic Acids Research 22, 4673-4680) with the default settings of the Megalign program in the Lasergene package (DNAstart Inc., 1228 South Park Street, Madison, Wisconsin 53715) .
  • the settings for multiple alignment are: GAP penalty of 10, and GAP length penalty 10; while the pair-wise alignment parameters are GAP penalty of 5 and Ktuple of 2.
  • Substantially homologous proteins and polypeptides are characterized as having one or more amino acid substitutions, deletions or additions.
  • non-standard amino acids such as 4-hydroxyproline, 6-JV-methyl lysine, 2- aminoisobutyric acid, isovaline and a-methyl serine
  • a limited number of non-conservative amino acids, amino acids that are not encoded by the genetic code, and unnatural amino acids may be substituted for amino acid residues.
  • "Unnatural amino acids” have been modified after protein synthesis, and/or have a chemical structure in their side chain(s) different from that of the standard amino acids.
  • Unnatural amino acids can be chemically synthesized, or preferably, are commercially available, and include pipecolic acid, thiazolidine carboxylic acid, dehydroproline, 3- and 4- methylproline, and 3 , 3-dimethylproline .
  • Essential amino acids in the xyloglucanase polypeptides of the present invention can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine- scanning mutagenesis (Cunningham and Wells, Science 244 : 1081- 1085, 1989).
  • these authors disclose methods for simultaneously randomizing two or more positions in a polypeptide, or recombination/shuffling of different mutations (W095/17413, W095/22625) , followed by selecting for functional a polypeptide, and then sequencing the mutagenized polypeptides to determine the spectrum of allowable substitutions at each position.
  • Other methods that can be used include phage display (e.g., Lowman et al . , Biochem. 3_0: 10832- 10837, 1991; Ladner et al . , U.S. Patent No. 5,223,409; Huse, WIPO Publication WO 92/06204) and region-directed mutagenesis (Derbyshire et al . , Gene 46:145, 1986; Ner et al . , DNA 7:127, 1988) .
  • Mutagenesis/shuffling methods as disclosed above can be combined with high-throughput , automated screening methods to detect activity of cloned, mutagenized polypeptides in host cells.
  • Mutagenized DNA molecules that encode active polypeptides can be recovered from the host cells and rapidly sequenced using modern equipment. These methods allow the rapid determination of the importance of individual amino acid residues in a polypeptide of interest, and can be applied to polypeptides of unknown structure .
  • one of ordinary skill in the art can identify and/or prepare a variety of polypeptides that are substantially homologous to residues 24 to 940 of SEQ ID NO: 2 and retain the xyloglucanase activity of the wild-type protein.
  • the xyloglucanase enzyme of the invention may, in addition to the enzyme core comprising the catalytically domain, also comprise a cellulose binding domain (CBD) , the cellulose binding domain and enzyme core (the catalytically active domain) of the enzyme being operably linked.
  • the cellulose-binding domain (CBD) may exist as an integral part the encoded enzyme, or a CBD from another origin may be introduced into the xyloglucanase thus creating an enzyme hybrid.
  • the term "cellulose- binding domain” is intended to be understood as defined by Peter Tomme et al. "Cellulose-Binding Domains: Classification and Properties" in "Enzymatic Degradation of Insoluble
  • CBDs are found in various enzymes such as cellulases, xylanases, mannanases, arabinofuranosidases, acetyl esterases and chitinases .
  • CBDs have also been found in algae, e.g. the red alga Porphyra purpurea as a non-hydrolytic polysaccharide-binding protein, see Tomme et al . , op . ci t .
  • Enzyme hybrids are known in the art, see e.g. WO 90/00609 and WO 95/16782, and may be prepared by transforming into a host cell a DNA construct comprising at least a fragment of DNA encoding the cellulose-binding domain Iigated, with or without a linker, to a DNA sequence encoding the xyloglucanase and growing the host cell to express the fused gene. Enzyme hybrids may be described by the following formula:
  • replicating vector i.e. a vector that exists as an extra chromosomal entity, the replication of which is independent of chromosomal replication, e.g. a plasmid.
  • the vector may be one which, when introduced into a host cell, is integrated into the host cell genome in part or in its entirety and replicated together with the chromosome (s) into which it has been integrated.
  • the vector is preferably an expression vector in which the DNA sequence encoding the enzyme of the invention is operably linked to additional segments required for transcription of the DNA.
  • the expression vector is derived from plasmid or viral DNA, or may contain elements of both.
  • operably linked indicates that the segments are arranged so that they function in concert for their intended purposes, e.g. transcription initiates in a promoter and proceeds through the DNA sequence coding for the enzyme .
  • the promoter may be any DNA sequence, which shows transcriptional activity in the host cell of choice and may be derived from genes encoding proteins either homologous or heterologous to the host cell .
  • suitable promoters for use in bacterial host cells include the promoter of the Bacillus stearothermophilus maltogenic amylase gene, the Bacillus licheniformis alpha- amylase gene, the Bacillus amyloliquefaciens alpha-amylase gene, the Bacillus subtilis alkaline protease gene, or the Bacillus pumilus xylosidase gene, or the phage Lambda P R or P L promoters or the E. coli lac, trp or tac promoters.
  • the DNA sequence encoding the enzyme of the invention may also, if necessary, be operably connected to a suitable terminator.
  • the recombinant vector of the invention may further comprise a DNA sequence enabling the vector to replicate in the host cell in question.
  • the vector may also comprise a selectable marker, e.g. a gene the product of which complements a defect in the host cell, or a gene encoding resistance to e.g. antibiotics like kanamycin, chloramphenicol, erythromycin, tetracycline, spectinomycine, or the like, or resistance to heavy metals or herbicides .
  • a selectable marker e.g. a gene the product of which complements a defect in the host cell, or a gene encoding resistance to e.g. antibiotics like kanamycin, chloramphenicol, erythromycin, tetracycline, spectinomycine, or the like, or resistance to heavy metals or herbicides .
  • a secretory signal sequence (also known as a leader sequence, prepro sequence or pre sequence) may be provided in the recombinant vector.
  • the secretory signal sequence is joined to the DNA sequence encoding the enzyme in the correct reading frame.
  • Secretory signal sequences are commonly positioned 5 ' to the DNA sequence encoding the enzyme .
  • the secretory signal sequence may be that normally associated with the enzyme or may be from a gene encoding another secreted protein.
  • the cloned DNA molecule introduced into the host cell may be either homologous or heterologous to the host in question. If homologous to the host cell, i.e. produced by the host cell in nature, it will typically be operably connected to another promoter sequence or, if applicable, another secretory signal sequence and/or terminator sequence than in its natural environment.
  • the term "homologous” is intended to include a DNA: sequence encoding an enzyme native to the host organism in question.
  • heterologous is intended to include a DNA sequence not expressed by the host cell in nature. Thus, the DNA sequence may be from another organism, or it may be a synthetic sequence .
  • the host cell into which the cloned DNA molecule or the recombinant vector of the invention is introduced may be any cell, which is capable of producing the desired enzyme and includes bacteria, yeast, fungi and higher eukaryotic cells.
  • Examples of bacterial host cells which on cultivation are w w _J _o ⁇ ⁇ o in o o in i-a TJ 0 0 03 ⁇ ⁇ 3 0 ⁇ ⁇ Cb rt ⁇ CQ 03 Cb ⁇ - 0 Co 0 TJ tr CQ CQ 0 1 to ⁇ 0 to ⁇ - ⁇ ⁇ ⁇ . ⁇ 3 ⁇ rt 0 X ⁇ CO 0 ⁇ ⁇ - tr ⁇ ⁇ ⁇ ⁇ - ⁇ 0 ⁇ 03 ⁇ 0J rt ⁇ - 0 0 0 ⁇
  • CD CD H Ct ⁇ ⁇ ⁇ ⁇ Cb rt ⁇ Cb 0 3 tr ⁇ 0 ⁇ CQ 0 ⁇ - CQ rt ⁇ rt 0 rt ⁇ t ⁇ ⁇ &- ⁇ - ⁇ - ⁇ Q rt ⁇ ⁇ - 03 rt 03 ⁇ - Hi CQ Hi ⁇ ⁇ rt tr ⁇ 0 ⁇ ⁇ CS] ⁇ - ⁇ ⁇ - k> ,0 03 ⁇ ! ⁇ ⁇ CO tr ⁇ ⁇ TJ tr 0 ⁇ 0 . 0 Hi 0 ⁇ ⁇ ⁇ - to ⁇ .
  • the 35S-CaMV promoter may be used (Franck et al . , 1980. Cell 21: 285-294).
  • Organ-specific promoters may e.g. be a promoter from storage sink tissues such as seeds, potato tubers, and fruits (Edwards & Coruzzi, 1990. Annu. Rev. Genet. 24: 275-303), or from metabolic sink tissues such as meristems (Ito et al . , 1994. Plant Mol. Biol. 24: 863- 878) , a seed specific promoter such as the glutelin, prolamin, globulin or albumin promoter from rice (Wu et al . , Plant and
  • the promoter may be a leaf specific promoter such as the rbcs promoter from rice or tomato (Kyozuka et al . , Plant Physiology Vol. 102, No. 3 pp. 991-1000 (1993), the chlorella virus adenine methyltransferase gene promoter (Mitra, A. and Higgins, DW, Plant Molecular Biology Vol. 26, No. 1 pp. 85-93 (1994) , or the aldP gene promoter from rice (Kagaya et al . , Molecular and General Genetics Vol. 248, No. 6 pp. 668-674
  • a wound inducible promoter such as the potato pin2 promoter (Xu et al, Plant Molecular Biology Vol. 22, No. 4 pp. 573-588 (1993) .
  • a promoter enhancer element may be used to achieve higher expression of the enzyme in the plant.
  • the promoter enhancer element may be an intron placed between the promoter and the nucleotide sequence encoding the enzyme.
  • Xu et al . op ci t disclose the use of the first intron of the rice actin 1 gene to enhance expression.
  • the selectable marker gene and any other parts of the expression construct may be chosen from those available in the art .
  • the DNA construct is incorporated into the plant genome according to conventional techniques known in the art, including Agrobacterium- ediated transformation, virus-mediated transformation, micro injection, particle bombardment, biolistic transformation, and electroporation (Gasser et al, Science, 244, 5 1293; Potrykus, Bio/Techn. 8, 535, 1990; Shimamoto et al, Nature, 338, 274, 1989) .
  • AsrroJacteri i ⁇ tumefaciens mediated gene transfer is the method of choice for generating transgenic dicots (for review Hooykas & Schilperoort, 1992. Plant Mol. 0 Biol. 19: 15-38), however it can also be used for transforming monocots, although other transformation methods are generally preferred for these plants.
  • the method of choice for generating transgenic monocots is particle bombardment (microscopic gold or tungsten particles coated with the 5 transforming DNA) of embryonic calli or developing embryos (Christou, 1992. Plant J. 2: 275-281; Shimamoto, 1994. Curr. Opin. Biotechnol. 5: 158-162; Vasil et al .
  • transformants having incorporated the expression construct are selected and regenerated into whole plants according to methods well known in 5 the art .
  • the present invention relates to an enzyme composition comprising the xyloglucanase of the 0 invention.
  • the enzyme composition of the invention may, in addition to the xyloglucanase of the invention, comprise one or more other enzyme types, for instance hemicellulase such as xylanase and mannanase, cellulase or endo- ⁇ -1, -glucanase components, 5 chitinase, lipase, esterase, pectinase, cutinase, phytase, oxidoreductase (peroxidase, haloperoxidase, oxidase, laccase) , protease, amylase, reductase, phenoloxidase, ligninase, pullulanase, pectate lyase, pectin acetyl esterase, polygalacturonase, rhamnogalacturonase, pectin lyase, pectin methylesterase, cello
  • the enzyme composition may be prepared in accordance with methods known in the art and may be in the form of a liquid or a dry composition.
  • the enzyme composition may be in granulate or microgranulate form.
  • the enzyme to be included in the composition may be stabilized in accordance with methods known in the art .
  • Xyloglucanases have potential uses in a lot of different industries and applications. Examples are given below of preferred uses of the enzyme composition of the invention.
  • the dosage of the enzyme composition of the invention and other conditions under which the composition is used may be determined based on methods known in the art .
  • the xyloglucanase or xyloglucanase composition according to the invention may be useful for at least one of the following purposes .
  • colour clarification is meant the partly restoration of the initial colours of fabric or garment throughout multiple washing cycles.
  • de-pilling denotes removing of pills from the fabric surface.
  • soaking liquor denotes aqueous liquor in which laundry may be immersed prior to being subjected to a conventional washing process.
  • the soaking liquor may contain one or more ingredients conventionally used in a washing or laundering process.
  • washing liquor denotes aqueous liquor in which laundry is subjected to a washing process, i.e. usually a combined chemical and mechanical action either manually or in a w ⁇ t t ⁇ ⁇ in o Ul o O Ul
  • inventions comprise as a surfactant one or more of the non-ionic and/or anionic surfactants described herein.
  • Polyethylene, polypropylene, and polybutylene oxide conden-sates of alkyl phenols are suitable for use as the non- ionic surfactant of the surfactant systems of the present invention, with the polyethylene oxide condensates being preferred.
  • These compounds include the condensation products of alkyl phenols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 8 to about 14 carbon atoms, in either a straight chain or branched-chain configuration with the alkylene oxide.
  • the ethylene oxide is present in an amount equal to from about 2 to about 25 moles, more preferably from about 3 to about 15 moles, of ethylene oxide per mole of alkyl phenol.
  • non-ionic surfactants of this type include IgepalTM CO- 630, marketed by the GAF Corporation; and TritonTM X-45, X-114, X-100 and X-102, all marketed by the Rohm & Haas Company. These surfactants are commonly referred to as alkyl phenol alkoxylates (e.g., alkyl phenol ethoxylates) .
  • alkyl phenol alkoxylates e.g., alkyl phenol ethoxylates
  • the condensation products of primary and secondary aliphatic alcohols with about 1 to about 25 moles of ethylene oxide are suitable for use as the non-ionic surfactant of the non-ionic surfactant systems of the present invention.
  • the alkyl chain of the aliphatic alcohol can either be straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms.
  • About 2 to about 7 moles of ethylene oxide and most preferably from 2 to 5 moles of ethylene oxide per mole of alcohol are present in said condensation products.
  • Examples of commercially available non-ionic surfactants of this type include TergitolTM 15-S-9 (The condensation product of C ⁇ :1.
  • the glycosyl is preferably derived from glucose.
  • the alcohol or alkylpolyethoxy alcohol is formed first and then reacted with glucose, or a source of glucose, to form the glucoside (attachment at the 1-position) .
  • the additional glycosyl units can then be attached between their 1-position and the preceding glycosyl units 2-, 3-, 4-, and/or 6-position, preferably predominantly the 2-position.
  • the condensation products of ethylene oxide with a hydrophobic base formed by the condensation of propylene oxide with propylene glycol are also suitable for use as the additional non-ionic surfactant systems of the present invention.
  • the hydrophobic portion of these compounds will preferably have a molecular weight from about 1500 to about 1800 and will exhibit water insolubility.
  • the addition of polyoxyethylene moieties to this hydrophobic portion tends to increase the water solubility of the molecule as a whole, and the liquid character of the product is retained up to the point where the polyoxyethylene content is about 50% of the total weight of the condensation product, which corresponds to condensation with up to about 40 moles of ethylene oxide.
  • Examples of compounds of this type include certain of the commercially available PluronicTM surfactants, marketed by BASF.
  • non-ionic surfactant of the non-ionic surfactant system of the present invention are the condensation products of ethylene oxide with the product resulting from the reaction of propylene oxide and ethylenediamine.
  • the hydrophobic moiety of these products consists of the reaction product of ethylenediamine and excess propylene oxide, and generally has a molecular weight of from about 2500 to about 3000.
  • This hydrophobic moiety is condensed with ethylene oxide to the extent that the condensation product contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight of from about 5,000 to about 11,000.
  • this type of non-ionic surfactant include certain of the commercially available TetronicTM compounds, marketed by BASF.
  • Preferred for use as the non-ionic surfactant of the surfactant systems of the present invention are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide, alkyl polysaccharides, and mixtures hereof. Most preferred are C 8 -C 14 alkyl phenol ethoxylates having from 3 to 15 ethoxy groups and C ⁇ -C x8 alcohol ethoxylates (preferably C 10 avg.) having from 2 to 10 ethoxy groups, and mixtures thereof.
  • Highly preferred non-ionic surfactants are polyhydroxy fatty acid amide surfactants of the formula
  • R 1 wherein R 1 is H, or R 1 is C ⁇ . 4 hydrocarbyl, 2-hydroxyethyl, 2- hydroxypropyl or a mixture thereof, R 2 is C 5 . 31 hydrocarbyl, and Z is a polyhydroxy hydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxylated derivative thereof.
  • R 1 is methyl
  • R 2 is straight C :1 . 15 alkyl or C 16 . 18 alkyl or alkenyl chain such as coconut alkyl or mixtures thereof
  • Z is derived from a reducing sugar such as glucose, fructose, maltose or lactose, in a reductive amination reaction.
  • Highly preferred anionic surfactants include alkyl alkoxylated sulfate surfactants.
  • Examples hereof are water soluble salts or acids of the formula RO(A) m S03M wherein R is an unsubstituted C 1Q -C- 24 alkyl or hydroxyalkyl group having a C 1Q -C 24 alkyl component, preferably a C ⁇ 2 -C 20 alkyl or hydro-xyalkyl, more preferably C 12 -C 18 alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than zero, typically between about 0.5 and about 6, more preferably between about 0.5 and about 3, and M is H or a cation which can be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or substituted-ammonium cation.
  • R is an unsubstituted C 1Q -C- 24 alkyl or
  • Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein.
  • Specific examples of substituted ammonium cations include methyl-, dimethyl, trimethyl-ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and those derived from alkylamines such as ethylamine, diethyl amine, triethylamine, mixtures thereof, and the like.
  • Exemplary surfactants are C 12 -C 18 alkyl polyethoxylate (1.0) sulfate (C 12 -C 1S E (1.0)M) , C 12 -C 18 alkyl polyethoxylate (2.25) sulfate (C 12 -C 18 (2.25) M, and C 12 -C 18 alkyl polyethoxylate (3.0) sulfate (C 12 -C 1S E (3.0) M) , and C 12 -C 18 alkyl polyethoxylate (4.0) sulfate (C 12 -C 18 E (4.0) M) , wherein M is conveniently selected from sodium and potassium.
  • Suitable anionic surfactants to be used are alkyl ester sulfonate surfactants including linear esters of C 8 -C 20 carboxylic acids (i.e., fatty acids), which are, sulfonated with gaseous S0 3 according to "The Journal of the American Oil Chemists Society", 52 (1975), pp. 323-329. Suitable starting materials would include natural fatty substances as derived from tallow, palm oil, etc.
  • the preferred alkyl ester sulfonate surfactant, especially for laundry applications comprise alkyl ester sulfonate surfactants of the structural formula:
  • R 3 is a C 8 -C 20 hydrocarbyl, preferably an alkyl, or combination thereof
  • R 4 is a hydrocarbyl, preferably an alkyl, or combination thereof
  • M is a cation, which forms a water-soluble salt with the alkyl ester sulfonate.
  • Suitable salt-forming cations include metals such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium cations, such as monoethanolamine, diethanolamine, and triethanolamine.
  • R 3 is C 10 -C ⁇ alkyl
  • R 4 is methyl, ethyl or isopropyl .
  • methyl ester sulfonates wherein R 3 is C 10 -C X6 alkyl.
  • alkyl sulfate surfactants which are water soluble salts or acids of , the formula ROS0 3 M wherein R preferably is a C 10 -C 24 hydrocarbyl, preferably an alkyl or hydroxyalkyl having a C 10 -C 20 alkyl component, more preferably a C 12 -C 18 alkyl or hydroxyalkyl, and M is H or a cation, e.g., an alkali metal cation (e.g. sodium, potassium, lithium), or ammonium or substituted ammonium (e.g.
  • R preferably is a C 10 -C 24 hydrocarbyl, preferably an alkyl or hydroxyalkyl having a C 10 -C 20 alkyl component, more preferably a C 12 -C 18 alkyl or hydroxyalkyl
  • M is H or a cation, e.g., an alkali metal cation (e.g. sodium, potassium, lithium), or ammonium or
  • alkylamines such as ethylamine, diethylamine, triethylamine, and mixtures thereof, and the like.
  • alkyl chains of C 12 -C 16 are preferred for lower wash temperatures (e.g. below about 50 °C) and C 16 -C 18 alkyl chains are preferred for higher wash temperatures (e.g. above about 50°C) .
  • anionic surfactants useful for detersive purposes can also be included in the laundry detergent compositions of the present invention.
  • Theses can include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono- di- and triethanolamine salts) of soap, C 8 - C 22 primary or secondary alkanesulfonates, C 8 -C 24 olefinsulfonates, sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline earth metal citrates, e.g., as described in British patent specification No.
  • alkylpolyglycolethersulfates (containing up to 10 moles of ethylene oxide) ; alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty oleyl glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates, alkyl phosphates, isethionates such as the acyl isethionates, N-acyl taurates, alkyl succinamates and sulfosuccinates, monoesters of sulfosuccinates (especially saturated and unsaturated C 12 -C 18 monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated C ⁇ -C 12 diesters), acyl sarcosinates, sulfates of alkylpolysaccharides such as the
  • Alkylbenzene sulfonates are highly preferred. Especially preferred are linear (straight-chain) alkyl benzene sulfonates (LAS) wherein the alkyl group preferably contains from 10 to 18 carbon atoms .
  • LAS linear (straight-chain) alkyl benzene sulfonates
  • the laundry detergent compositions of the present invention typically comprise from about 1% to about 40%, preferably from about 3% to about 20% by weight of such anionic surfactants.
  • the laundry detergent compositions of the present invention may also contain cationic, ampholytic, zwitterionic, and semi-polar surfactants, as well as the nonionic and/or anionic surfactants other than those already described herein.
  • Cationic detersive surfactants suitable for use in the laundry detergent compositions, of the present invention are those having one long-chain hydrocarbyl group.
  • cationic surfactants include the ammonium surfactants such as alkyltrimethylammonium halogenides, and those surfactants having the formula :
  • R 2 is an alkyl or alkyl benzyl group having from about 8 to about 18 carbon atoms in the alkyl chain
  • each R 3 is selected form the group consisting of -CH 2 CH 2 -, -CH 2 CH (CH 3 ) - , - CH 2 CH(CH 2 0H) -, -CH 2 CH 2 CH 2 -, and mixtures thereof
  • each R 4 is selected from the group consisting of C 3. -C 4 alkyl, C1 .
  • R 6 is any hexose or hexose polymer having a molecular weight less than about 1000, and hydrogen when y is not 0;
  • R 5 is the same as R 4 or is an alkyl chain, wherein the total number of carbon atoms or R 2 plus R 5 is not more than about 18; each y is from 0 to about 10, and the sum of the y values is from 0 to about 15; and
  • X is any compatible anion.
  • Highly preferred cationic surfactants are the water soluble quaternary ammonium compounds useful in the present composition having the formula:
  • R x is C 8 -C ⁇ 6 alkyl
  • each of R 2 , R 3 and R 4 is independently C ! -C 4 alkyl, C-Ci hydroxy alkyl, benzyl, and -(C 2 H 40 ) X H where x has a value from 2 to 5, and X is an anion.
  • R 2 , R 3 or R 4 should be benzyl.
  • the preferred alkyl chain length for R x is C 12 -C 15 , particularly where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat or is derived synthetically by olefin build up or 0X0 alcohols synthesis.
  • Preferred groups for R 2 R 3 and R 4 are methyl and hydroxyethyl groups and the anion X may be selected from halide, methosulphate, acetate and phosphate ions.
  • Suitable quaternary ammonium compounds of formulae (i) for use herein are: coconut trimethyl ammonium chloride or bromide ; coconut methyl dihydroxyethyl ammonium chloride or bromide; decyl triethyl ammonium chloride; decyl dimethyl hydroxyethyl ammonium chloride or bromide; C 12 _ 15 dimethyl hydroxyethyl ammonium chloride or bromide; coconut dimethyl hydroxyethyl ammonium chloride or bromide; myristyl trimethyl ammonium methyl sulphate; lauryl dimethyl benzyl ammonium chloride or bromide ; lauryl dimethyl (ethenoxy) 4 ammonium chloride or bromide; choline esters (compounds of formula (i) wherein R x is
  • laundry detergent compositions of the present invention typically comprise from 0.2% to about ⁇ ⁇ to t ⁇ ⁇ ⁇
  • Semi-polar nonionic detergent surfactants include the amine oxide surfactants having the formula :
  • R 3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures thereof containing from about 8 to about 22 carbon atoms
  • R 4 is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof
  • x is from 0 to about 3
  • each R 5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups .
  • the R 5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to form a ring structure .
  • amine oxide surfactants in particular include C 10 -C 18 alkyl dimethyl amine oxides and C 8 -C 12 alkoxy ethyl dihydroxy ethyl amine oxides .
  • the laundry detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such semi-polar nonionic surfactants.
  • compositions according to the present invention may further comprise a builder system.
  • a builder system Any conventional builder system is suitable for use herein including aluminosilicate materials, silicates, polycarboxylates and fatty acids, materials such as ethylenediamine tetraacetate, metal ion sequestrants such as aminopolyphosphonates, particularly ethylenediamine tetramethylene phosphonic acid and diethylene triamine pentamethylenephosphonic acid.
  • a builder system is suitable for use herein including aluminosilicate materials, silicates, polycarboxylates and fatty acids, materials such as ethylenediamine tetraacetate, metal ion sequestrants such as aminopolyphosphonates, particularly ethylenediamine tetramethylene phosphonic acid and diethylene triamine pentamethylenephosphonic acid.
  • Polymers of this type are disclosed in GB-A-1, 596 , 756.
  • Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of from 20,000 to 70,000, especially about 40,000.
  • Detergency builder salts are normally included in amounts of from 5% to 80% by weight of the composition. Preferred levels of builder for liquid detergents are from 5% to 30%.
  • Preferred detergent compositions in addition to the enzyme preparation of the invention, comprise other enzyme (s) which provides cleaning performance and/or fabric care benefits .
  • enzymes include proteases, lipases, cutinases, amylases, cellulases, peroxidases, oxidases (e.g. laccases) .
  • protease suitable for use in alkaline solutions can be used. Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically or genetically modified mutants are included.
  • the protease may be a serine protease, preferably an alkaline microbial protease or a trypsin-like protease.
  • alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279) .
  • trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270.
  • Preferred commercially available protease enzymes include those sold under the trade names Alcalase, Savinase, Primase, Durazym, and Esperase by Novozymes A/S, those sold under the tradename Maxatase, Maxacal, Maxapem, Properase, Purafect and Purafect OXP by Genencor International, and those sold under the tradename Opticlean and Optimase by Solvay Enzymes.
  • Protease enzymes may be incorporated into the compositions in accordance with the invention at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
  • Lipases Any lipase suitable for use in alkaline solutions can be used. Suitable lipases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • useful lipases include a Humicola lanuginosa lipase, e.g., as described in EP 258 068 and EP 305 216, a Rhizomucor miehei lipase, e.g., as described in EP 238 023, a Candida lipase, such as a C. antarctica lipase, e.g., the C. antarctica lipase A or B described in EP 214 761, a Pseudomonas lipase such as a P. alcaligenes and P. pseudoalcaligenes lipase, e.g., as described in EP 218 272, a P.
  • a Humicola lanuginosa lipase e.g., as described in EP 258 068 and EP 305 216
  • a Rhizomucor miehei lipase e.g., as described in EP 238 023
  • cepacia lipase e.g., as described in EP 331 376, a P. stutzeri lipase, e.g., as disclosed in GB 1,372,034, a P. fluorescens lipase, a Bacillus lipase, e.g., a B. subtilis lipase (Dartois et al . , (1993), Biochemica et Biophysica acta 1131, 253-260), a B. stearo- thermophilus lipase (JP 64/744992) and a B. pumilus lipase (WO 91/16422) .
  • cloned lipases may be useful, including the Penicillium camembertii lipase described by Yamaguchi et al . , (1991), Gene 103, 61-67), the Geotricum candidum lipase (Schimada, Y. et al . , (1989), J. Biochem., 106, 383-388) , and various Rhizopus lipases such as a R. delemar lipase (Hass, M.J et al . , (1991), Gene 109, 117-113), a R. niveus lipase (Kugimiya et al . , (1992), Biosci .
  • a cutinases may also be useful, e.g., a cutinase derived from Pseudomonas mendocina as described in WO 88/09367, or a cutinase derived from Fusarium solani pisi (e.g. described in WO 90/09446) .
  • lipases such as Ml LipaseTM, Luma fastTM and LipomaxTM (Genencor) , LipolaseTM and Lipolase UltraTM (Novozymes A/S) , and Lipase P "Amano” (Amano Pharmaceutical Co. Ltd.) .
  • the lipases are normally incorporated in the detergent J to t ⁇ ⁇
  • Cellulases are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
  • Peroxidases/Oxidases Peroxidase enzymes are used in combination with hydrogen peroxide or a source thereof (e.g. a percarbonate, perborate or persulfate) . Oxidase enzymes are used in combination with oxygen. Both types of enzymes are used for "solution bleaching", i.e. to prevent transfer of a textile dye from a dyed fabric to another fabric when said fabrics are washed together in a wash liquor, preferably together with an enhancing agent as described in e.g. WO 94/12621 and WO 95/01426. Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • Peroxidase and/or oxidase enzymes are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
  • Mixtures of the above mentioned enzymes are encompassed herein, in particular a mixture of a protease, an amylase, a lipase and/or a cellulase.
  • the enzyme of the invention is normally incorporated in the detergent composition at a level from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level from 0.01% to 0.2% of enzyme w w to to ⁇ ⁇ o Ul o in o Ul
  • a suds suppressor exemplified by silicones, and silica-silicone mixtures.
  • Silicones can generally be represented by alkylated polysiloxane materials, while silica is normally used in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. Theses materials can be incorporated as particulates, in which the suds suppressor is advantageously releasably incorporated in a water-soluble or waterdispersible, substantially non surface-active detergent impermeable carrier.
  • the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying on to one or more of the other components.
  • a preferred silicone suds controlling agent is disclosed in US 3,933,672.
  • Other particularly useful suds suppressors are the self-emulsifying silicone suds suppressors, described in German Patent Application DTOS 2,646,126.
  • An example of such a compound is DC-544, commercially available form Dow Corning, which is a siloxane-glycol copolymer.
  • Especially preferred suds controlling agent are the suds suppressor system comprising a mixture of silicone oils and 2-alkyl-alkanols .
  • Suitable 2 -alkyl- alkanols are 2-butyl-octanol which are commercially available under the trade name Isofol 12 R.
  • Such suds suppressor system are described in European Patent Application EP 0 593 841.
  • Especially preferred silicone suds controlling agents are described in European Patent Application No. 92201649.8.
  • Said compositions can comprise a silicone/ silica mixture in combination with fumed nonporous silica such as Aerosil R .
  • the suds suppressors described above are normally employed at levels of from 0.001% to 2% by weight of the composition, preferably from 0.01% to 1% by weight.
  • encapsulating materials are water soluble capsules which consist of a matrix of polysaccharide and polyhydroxy compounds such as described in GB 1,464,616.
  • Suitable water soluble encapsulating materials comprise dextrins derived from ungelatinized starch acid esters of substituted dicarboxylic acids such as described in US 3,455,838. These acid-ester ⁇ dextrins are, preferably, prepared from such starches as waxy maize, waxy sorghum, sago, tapioca and potato. Suitable examples of said encapsulation materials include N-Lok manufactured by National Starch. The N-Lok encapsulating material consists of a modified maize starch and glucose. The starch is modified by adding monofunctional substituted groups such as octenyl succinic acid anhydride.
  • Antiredeposition and soil suspension agents suitable herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or co-polymeric polycarboxylic acids or their salts .
  • Polymers of this type include the polyacrylates and maleic anhydride-acrylic acid copolymers previously mentioned as builders, as well as copolymers of maleic anhydride with ethylene, methylvinyl ether or methacrylic acid, the maleic anhydride constituting at least 20 mole percent of the copolymer. These materials are normally used at levels of from 0.5% to 10% by weight, more preferably form 0.75% to 8%, most preferably from 1% to 6% by weight of the composition.
  • Preferred optical brighteners are anionic in character, examples of which are disodium 4, 4 ' -bis- (2-diethanolamino-4- anilino -s- triazin-6-ylamino) stilbene-2 :2 ' disulphonate, disodium 4, - 4 ' -bis- (2-morpholino-4-anilino-s-triazin-6- ylamino-stilbene-2 : 2 ' - disulphonate, disodium 4,4' - bis- (2,4- dianilino-s-triazin-6-ylamino) stilbene-2 : 2 ' - disulphonate, monosodium 4 ',4'' - bis- (2 , -dianilino-s-tri-azin-6 ylamino) stilbene-2-sulphonate, disodium 4,4' -bis- (2-anilino-4- (N-methyl-N-2-hydroxyethylamino) -s-tri
  • polyethylene glycols particularly those of molecular weight 1000-10000, more particularly 2000 to 8000 and most preferably about 4000. These are used at levels of from 0.20% to 5% more preferably from 0.25% to 2.5% by weight. These polymers and the previously mentioned homo- or co-polymeric poly-carboxylate salts are valuable for improving whiteness maintenance, fabric ash deposition, and cleaning performance on clay, proteinaceous and oxidizable soils in the presence of transition metal impurities.
  • Soil release agents useful in compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid with ethylene glycol and/or propylene glycol units in various arrangements. Examples of such polymers are disclosed in US 4,116,885 and 4,711,730 and EP 0 272 033.
  • a particular preferred polymer in accordance with EP 0 272 033 has the formula :
  • PEG is -(OC 2 H 4 )0-
  • PO is (OC 3 H 6 0)
  • T is (pOOC 6 H 4 CO) .
  • modified polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1, 2-propanediol, the end groups consisting primarily of sulphobenzoate and secondarily of mono esters of ethylene glycol and/or 1, 2-propanediol .
  • the target is to obtain a polymer capped at both end by sulphobenzoate groups, "primarily", in the present context most of said copolymers herein will be endcapped by sulphobenzoate groups.
  • polyesters herein contain about 46% by weight of dimethyl terephthalic acid, about 16% by weight of 1,2- propanediol, about 10% by weight ethylene glycol, about 13% by weight of dimethyl sulfobenzoic acid and about 15% by weight of sulfoisophthalic acid, and have a molecular weight of about 3.000.
  • the polyesters and their method of preparation are described in detail in EP 311 342.
  • Fabric softening agents can also be incorporated into laundry detergent compositions in accordance with the present invention. These agents may be inorganic or organic in type. Inorganic softening agents are exemplified by the smectite clays disclosed in GB-A-1 400898 and in US 5,019,292. Organic fabric softening agents include the water insoluble tertiary amines as disclosed in GB-A1 514 276 and EP 0 011 340 and their combination with mono C 12 -C 14 quaternary ammonium salts are disclosed in EP-B-0 026 528 and di-long-chain amides as disclosed in EP 0 242 919. Other useful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials as disclosed in EP 0 299 575 and 0 313 146.
  • Levels of smectite clay are normally in the range from 5% to 15%, more preferably from 8% to 12% by weight, with the material being added as a dry mixed component to the remainder of the formulation.
  • Organic fabric softening agents such as the water-insoluble tertiary amines or dilong chain amide materials are incorporated at levels of from 0.5% to 5% by weight, normally from 1% to 3% by weight whilst the high molecular weight polyethylene oxide materials and the water soluble cationic materials are added at levels of from 0.1% to 2%, normally from 0.15% to 1.5% by weight.
  • These materials are normally added to the spray dried portion of the composition, although in some instances it may be more convenient to add them as a dry mixed particulate, or spray them as molten liquid on to other solid components of the composition.
  • Polymeric dye-transfer inhibiting agents may also comprise from 0.001% to 10%, preferably from 0.01% to 2%, more preferably form 0.05% to 1% by weight of polymeric dye- transfer inhibiting agents. Said polymeric dye- ⁇ w t to ⁇ ⁇
  • 03 s 03 ⁇ ⁇ - 0 ⁇ - 1 ⁇ rt Cb 03 Cb 03 ⁇ - 1 ⁇ . 0 0 ⁇ ⁇ - 0 Cb ⁇ 0 ⁇ CQ ⁇ ⁇ - ⁇ . ⁇ - ⁇ - ⁇ ⁇ - 1 0 ⁇ ; O 03 Hi ⁇ H" s- a Cb 0 ⁇ tr 0 ⁇ - ⁇ 1 rt 03 Cb tr rt ⁇ - 0 H 1 ⁇ !
  • the liquid detergent compositions according to the present invention can also be in "concentrated form", in such case, the liquid detergent compositions according to the present invention will contain a lower amount of water, compared to conventional liquid detergents.
  • the water content of the concentrated liquid detergent is less than 30%, more preferably less than 20%, most preferably less than 10% by weight of the detergent compositions.
  • compositions of the invention may for example, be formulated as hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use in the pretreatment of stained fabrics, rinse added fabric softener compositions, and compositions for use in general household hard surface cleaning operations and dishwashing operations .
  • the following examples are meant to exemplify compositions for the present invention, but are not necessarily meant to limit or otherwise define the scope of the invention.
  • the abbreviated component identifications have the following meanings :
  • TAS Sodium tallow alkyl sulphate
  • 25EY A C 12 - C 15 predominantly linear primary alcohol condensed with an average of Y moles of ethylene oxide
  • 45EY A C 14 - C 15 predominantly linear primary alcohol condensed with an average of Y moles of ethylene oxide
  • XYEZS C 1X - C 1Y sodium alkyl sulfate condensed with an average of Z moles of ethylene oxide per mole
  • Nonionic C 13 - C 15 mixed ethoxylated/propoxylated fatty alcohol with an average degree of ethoxylation of 3.8 and an average degree of propoxylation of 4.5 sold under the tradename Plurafax LF404 by BASF Gmbh
  • CFAA C 12 - C 14 alkyl N-methyl glucamide
  • TFAA C 16 - C 18 alkyl N-methyl glucamide
  • NaSKS-6 Crystalline layered silicate of formula d-Na 2 Si 2 O s
  • MA/AA Copolymer of 1:4 maleic/acrylic acid, average molecular weight about 80,000
  • Polyacrylate Polyacrylate homopolymer with an average molecular weight of 8,000 sold under the tradename PA30 by BASF
  • Zeolite A Hydrated Sodium Aluminosilicate of formula Na 12 (Al0 2 Si0 2 ) 12 . 27H 2 0 having a primary particle size in the range from 1 to 10 micrometers
  • Perborate Anhydrous sodium perborate monohydrate bleach, empirical formula NaB0 2 .H 2 0 2
  • TAED Tetraacetyl ethylene diamine
  • CMC Sodium carboxymethyl cellulose
  • DETPMP Diethylene triamine penta (methylene phosphonic acid) , marketed by Monsanto under the Tradename Dequest 2060
  • Granular Suds suppressor 12% Silicone/silica, 18% stearyl alcohol, 70% starch in granular form
  • Sulphate Anhydrous sodium sulphate
  • HMWPEO High molecular weight polyethylene oxide
  • TAE 25 Tallow alcohol ethoxylate (25)
  • a granular fabric cleaning composition in accordance with the invention may be prepared as follows : Sodium linear C 12 alkyl 6.5 benzene sulfonate
  • Zeolite A 26.0 Sodium nitrilotriacetate 5.0
  • Enzyme of the invention 0.1
  • a compact granular fabric cleaning composition (density 800 g/1) in accord with the invention may be prepared as follows :
  • Enzyme of the invention 0.1
  • Granular suds suppressor 3.5 water/minors Up to 100%
  • Granular fabric cleaning compositions in accordance with the invention which are especially useful in the laundering of coloured fabrics were prepared as follows
  • Enzyme of the invention 0.10 0.05
  • Granular fabric cleaning compositions in accordance with the invention which provide "Softening through the wash” capability may be prepared as follows :
  • Zeolite A 15.0 15.0 MA/AA 4.0 4.0
  • Enzyme of the invention 0.10 0.05
  • Heavy duty liquid fabric cleaning compositions in accordance with the invention may be prepared as follows
  • Enzyme of the invention 0.10 0.05
  • xyloglucan from tamarind seeds supplied by Megazyme, Ireland has a complex branched structure with glucose, xylose, galactose and arabinose in the ratio of 45:36:16:3. Accordingly, it is strongly believed that an enzyme showing catalytic activity on this xyloglucan also has catalytic activity on other xyloglucan structures from different sources (angiosperms or gymnosperms) .
  • E. coli hosts XLl-lue MRF- and XL0LR E. coli strains were provided by Stratagene Inc . (USA) and used according to the manufaturer' s instructions.
  • PBK-CAMV Stratagene Inc., La Jolla, California, USA.
  • Bacteriophage ZAP Express Stratagene Inc., La Jolla, California, USA.
  • LB agar (Ausubel, F. M. et al . (Eds.) "Current protocols in Molecular Biology”. John Wiley and Sons, 1995) .
  • LBPG is LB agar supplemented with 0.5% Glucose and 0.05 M potassium phosphate, pH 7.0
  • AZC -xyloglucan is added to LBPG-agar to 0.5 %.
  • AZCL- xyloglucan is from Megazyme, Ireland.
  • BPX media is described in EP 0 506 780 (WO 91/09129) .
  • NZY agar (per litre) 5 g of NaCl, 2 g of MgS04 , 5 g of yeast extract, 10 g of NZ amine (casein hydrolysate) , 15 g of agar; add de-ionized water to 1 litre, adjust pH with NaOH to pH 7.5 and autoclave
  • NZY broth (per litre) 5 g of NaCl, 2 g of MgS04, 5 g of yeast extract, 10 g of NZ amine (casein hydrolysate) ; add deionized water to 1 litre, adjust pH with NaOH to pH 7.5 and autoclave NZY Top Agar (per litre) 5 g of NaCl, 2 g of MgS04 , 5 g of yeast extract, 10 g of NZ amine (casein hydrolysate), 0.7 % (w/v) agarose; add de-ionized water to 1 litre, adjust pH with NaOH to pH 7.5 and autoclave .
  • the xyloglucanase activity is measured using AZCL- xyloglucan from Megazyme, Ireland, (htt : //www. megazyme . com/purchase/index. html) as substrate .
  • a solution of 0.2 % of the blue substrate is suspended in a 0.1 M phosphate buffer pH 7.5 under stirring.
  • the solution is distributed under stirring to 1.5 ml Eppendorf tubes (0.75 ml to each) , 50 ⁇ l enzyme solution is added and they are incubated in an Eppendorp Thermomixer model 5436 for 20 minutes at 40 °C with a mixing of 1200 rpm. After incubation the colored solution is separated from the solid by 4 minutes centrifugation at 14,000 rpm and the absorbance of the supernatant is measured at 600 nm.
  • One XyloU unit is defined as the amount of enzyme resulting in an absorbance of 0.24 in a 1 cm cuvette at 600 nm.
  • the strain Jonesia sp . , DSM 14140 was propagated in liquid TY medium. After 16 hours incubation at 30 °C and 300 rpm, the cells were harvested, and genomic DNA was isolated by the method describe by Duffner, F., Fitzsim ons, A., Brophy, G., O'Kiely, P, O'Connell, M. Journal Appl . Bact . 76: 583-591 (1994) "Dominance of Lactobacillus plantarum strains in grass silage as demonstrated by a novel competition assay".
  • a Lambda ZAP library was prepared from genomic DNA of the strain Jonesia sp . , DSM 14140.
  • the ZAP Express cloning kit used was with BamHI digested and dephosphorylated arms from Stratagene. Isolated DNA was partially digested with Sau3A and size fractionated on a 1% agarose gel. DNA was excised from the agarose gel between 3 and 10 Kb and purified using Qiaspin DNA fragment purification procedure (Qiagen GmbH) . 100 ng of purified, fractionated DNA was Iigated with 1 ⁇ g of BamHI dephosphorylated ZAPexpress vector arms (4 degrees overnight) . Ligation reaction was packaged directly with GigaPacklll Gold according to the manufacturers instructions (Stratagene) . Phage libraries were titered with XLlblue mrf" (Stratagene) . Screening for xyloglucanase clones by functional expression in lambda ZAP Express
  • plaque-forming units from the genomic library were plated on NZY-agar plates containing 0.1 % AZCL-xyloglucan (MegaZyme, Ireland) , using E. coli XLl-Blue MRF' (Stratagene, USA) as a host, followed by incubation of the plates at 37 °C for 24 hours.
  • Xyloglucanase-positive lambda clones were identified by the formation of blue hydrolysis halos around the positive phage clones. These were recovered from the screening plates by coring the TOP-agar slices containing the plaques of interest into 500 ⁇ l of SM buffer and 20 ⁇ l of chloroform.
  • the xyloglucanase-positive lambda ZAP Express clones were plaque-purified by plating an aliquot of the cored phage stock on NZY plates containing 0.1 % AZCL-xyloglucan as above.
  • Single xyloglucanase-positive lambda clones were cored into 500 ⁇ l of SM buffer and 20 ⁇ l of chloroform, and purified by one more plating round as described above.
  • E. coli XLl-Blue cells (Stratagene, La Jolla Ca.) were prepared and resuspended in lOmM MgS04 as recommended by
  • coli cells and bacteriophage lambda the phagemids being resistant to heating.

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Abstract

L'invention concerne des xyloglucanases appartenant à la famille 74 des glycosyl hydrolases et qui sont dérivées du genre Jonesia, notamment de la souche Jonesia sp, DSM 14140. Les xyloglucanases présentent des performances élevées dans des compositions de détergents classiques.
PCT/DK2002/000210 2001-03-27 2002-03-27 Xyloglucanases de la famille 74 Ceased WO2002077242A2 (fr)

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AU2002249102A AU2002249102A1 (en) 2001-03-27 2002-03-27 Family 74 xyloglucanases

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