CN115836125A - Use of cellulase for removing dust mites from textiles - Google Patents

Abstract

The present invention relates to detergent compositions comprising enzymes capable of degrading cellulosic materials and their use for removing dust mites from the surface of textiles. In one aspect, the enzyme capable of degrading cellulosic material is GH45 cellulase. In additional aspects, the GH45 cellulase is a Rhizopus terrestris endoglucanase.

Description

Use of cellulase for removing dust mites from textiles

technical field

The present invention relates to the use of enzymes capable of degrading cellulosic materials, in particular the use of cellulases for removing dust mites from textile surfaces.

References to Sequence Listings

This application contains a Sequence Listing in computer readable form. This computer readable form is incorporated herein by reference.

Background technique

Dust mites are mites (a type of arachnid such as spiders and scorpions). They are between 0.1mm and 0.5mm in size and live in all types of fibers including carpets, clothing, upholstered sofas and bed sheets. Over the past few decades, it has become clear that dust mites are highly allergenic and can trigger asthma and other allergic attacks. Attempts have been made to prevent exposure to allergens through the use of organic or inorganic acaricides, detergents or ultraviolet light. In particular, US 5672362 A uses a solution of disodium octaborate tetrahydrate (DOT) to kill dust mites. WO 9836640 discloses compositions containing benzyl benzoate and alcohol for the control of dust mites. KR 200287251 discloses a portable ultraviolet (UV) sterilizer for removing dust mites. But so far, results have been disappointing, as acaricides or cleaners may trigger new allergy flare-ups. US 2004255983 discloses a method of removing dust mites by repeatedly washing articles to a desired level. However, too many wash cycles can compromise the integrity and safety of textiles, reducing their useful life.

A new method is needed to remove dust mites from textile surfaces without introducing new allergens or reducing the useful life of textiles.

Contents of the invention

In one aspect, the invention relates to the use of one or more enzymes capable of degrading cellulosic material to reduce dust mites from textiles by adding said one or more enzymes in a wash cycle. In another aspect, the enzyme is a cellulase or hemicellulase. In additional aspects, the cellulase can be a GH45 cellulase.

In another aspect, the present invention also relates to an enzyme composition for removing dust mites. The enzyme composition comprises enzymes capable of degrading cellulosic material and can be used in any washing, cleaning and/or fabric care method, including soaking methods, pretreatment methods, methods with a rinse step (wherein a separate rinse and The composition), and post-treatment methods.

In another aspect, the enzyme composition comprises one or more cellulases or hemicellulases. Additionally, the cellulase may be a GH45 cellulase. In one aspect, the GH45 cellulase is a Thermothielavioides terrestris (T.t) endoglucanase.

In a further aspect, the T.t endoglucanase is selected from the group consisting of:

(1) T.t endoglucanase, the T.t endoglucanase comprises the mature polypeptide of SEQ ID NO: 2 or a fragment thereof, or consists of it;

(2) T.t endoglucanase, the T.t endoglucanase comprises at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 80% of the mature polypeptide of SEQ ID NO:2, 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%, or at least 99% sequence identity of amino acid sequences, or consist thereof;

(3) T.t endoglucanase, the T.t endoglucanase is encoded by a polynucleotide, and the polynucleotide comprises at least 60%, at least 65%, At least 70%, 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%, or at least 99% sequence identity, or derived therefrom composition;

(4) T.t endoglucanase, the T.t endoglucanase is encoded by a polynucleotide, and the polynucleotide is compatible with the mature polypeptide of SEQ ID NO:1 under at least high stringent conditions and very high stringent conditions The coding sequence or its full-length complement hybridizes. In another aspect, the cellulase composition further comprises one or more detergent components or fabric softeners.

In another aspect, the present application further comprises a detergent composition comprising an enzyme capable of degrading cellulosic material or comprising an enzyme composition as mentioned above.

In yet another aspect, the present application encompasses a method for reducing or removing dust mites comprising:

(1) Washing or exposing textiles with a detergent composition comprising an enzyme capable of degrading a cellulosic material or an enzyme composition comprising an enzyme capable of degrading a cellulosic material, wherein the enzyme capable of degrading a cellulosic material comprises GH45 cellulase , wherein the GH45 cellulase is a GH45 endoglucanase, in another aspect, the endoglucanase is a T.t endoglucanase;

(2) Optionally rinsing the textile.

Description of drawings

Figure 1 shows an exemplary anti-pilling experiment.

Figure 2 shows the anti-dust mite results of T.t. endoglucanase on E-252PA fabric.

Figure 3 shows the anti-dust mite results of T.t. endoglucanase on CN-42 fabric.

definition

Anti-pilling : The term "anti-pilling" means the removal of pills from the textile surface and/or the prevention of the formation of pills on the textile surface.

Cellulolytic enzyme or cellulase : The term "cellulolytic enzyme" or "cellulase" means one or more (eg, several) enzymes that hydrolyze cellulosic material. Such enzymes include one or more endoglucanases, one or more cellobiohydrolases, one or more beta-glucosidases, or combinations thereof. Two basic methods for measuring cellulolytic activity include: (1) measuring total cellulolytic activity, and (2) measuring individual cellulolytic activities (endoglucanase, cellobiohydrolase, and β -glucosidase), as reviewed by Zhang et al., Outlook for cellulase improvement: Screening and selection strategies [Cellulase Improvement Outlook: Screening and Selection Strategies], 2006, Biotechnology Advances [Biotechnology Advances] 24: 452-481. Total cellulolytic activity is typically measured using insoluble substrates, including Whatman No. 1 filter paper, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, pretreated lignocellulose, and the like. The most common total cellulolytic activity assay is a filter paper assay using Whatman No. 1 filter paper as substrate. This assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, 1987, Measurement of cellulase activities [measurement of cellulase activity], Pure Appl. Chem. [Pure and Applied Chemistry] 59:257-68) .

HPX-87H柱(伯乐实验室有限公司(Bio-Rad Laboratories,Inc.)，赫拉克勒斯，加利福尼亚州，美国)进行的糖分析。本领域已知的用于测量纤维素分解酶活性的其他方法也可以是适用的。For the purposes of the present invention, cellulolytic enzyme activity is determined by measuring the increase in hydrolysis of cellulosic material by one or more cellulolytic enzymes under the following conditions: compared to control hydrolysis without added cellulolytic enzyme protein In contrast, adding 1-50 mg cellulolytic enzyme protein/g cellulose (or other pretreated fiber Vegetarian material), for 3-7 days. Typical conditions are: 1 ml reaction, washed or unwashed PCS, 5% insoluble solids, 50 mM sodium acetate (pH 5), 1 mM MnSO ₄ , 50°C, 55°C, or 60°C, 72 hours, by

Sugar analysis was performed on an HPX-87H column (Bio-Rad Laboratories, Inc., Hercules, CA, USA). Other methods known in the art for measuring cellulolytic enzyme activity may also be suitable.

Cellulosic material: The term "cellulosic material" means any material that contains cellulose. The predominant polysaccharide in the primary cell wall of biomass is cellulose, the second most abundant is hemicellulose, and the third most abundant is pectin. The secondary cell wall produced after cells stop growing also contains polysaccharides, and it is strengthened by polymerized lignin covalently cross-linked with hemicellulose. Cellulose is a homopolymer of anhydrocellobiose, and thus a linear β-(1-4)-D-glucan, while hemicellulose includes a variety of compounds with a range of substituents in complex branched chain structures , such as xylan, xyloglucan, arabinoxylan, and mannan. Although cellulose is generally polymorphic, it is found in plant tissues primarily as an insoluble crystalline matrix of parallel glucan chains. Hemicelluloses are often hydrogen bonded to cellulose as well as other hemicelluloses, which help stabilize the cell wall matrix.

Cellulose is commonly found, for example, in vegetable food products such as salads, tomatoes, spinach, cabbage, cereals, and the like.

Detergent Component : The term "detergent component" is defined herein to mean a type of chemical that can be used in a detergent composition for, eg, laundry. Examples of detergent components are surfactants, builders, chelators or chelating agents, bleach systems or bleach components, polymers, fabric conditioners, suds boosters, suds suppressors , dyes, fragrances, tarnish inhibitors, bactericides, fungicides, soil suspending agents, corrosion inhibitors, enzyme inhibitors or stabilizers, enzyme activators, one or more transferases, hydrolases, oxidoreductases, Bluing and fluorescent dyes, antioxidants, and solubilizers.

Detergent composition: The term "detergent composition" refers to a composition for removing undesired compounds from a surface to be cleaned, such as a textile surface. The detergent composition can be used, for example, for cleaning textiles, for both household cleaning and industrial cleaning. These terms encompass any material/compound selected for the particular type of cleaning composition and product form (e.g., liquid, gel, powder, granule, paste, or spray composition) desired, and include, but are not limited to, detergents Compositions (eg, liquid and/or solid laundry detergents and delicate fabric detergents; fabric refreshers; fabric softeners; and textile and laundry pre-stainers/pre-treatments). The detergent composition may contain one or more enzymes such as hemicellulase, peroxidase, protease, cellulase, xylanase, lipase, phospholipase, esterase, cutinase, pectinase , mannanase, pectin lyase, keratinase, reductase, oxidase, phenoloxidase, lipoxygenase, lignase, pullulanase, tannase, pentosanase, maranaase , beta-glucanase, arabinosidase, hyaluronidase, chondroitinase, laccase, DNase, chlorophyllase, amylase, perhydrolase, peroxidase, xanthan enzyme, and mixtures thereof. The detergent composition may further comprise detergent components such as surfactants, builders, chelating agents or chelating agents, bleaching systems or bleach components, polymers, fabric conditioners, suds boosters, suds suppressors, Dyes, fragrances, tarnish inhibitors, bactericides, fungicides, soil suspending agents, corrosion inhibitors, enzyme inhibitors or stabilizers, enzyme activators, one or more transferases, hydrolases, oxidoreductases, Blue and fluorescent dyes, antioxidants, and solubilizers.

dust mite:

Dust mites (Dermatophagoides spp.) are tiny arachnid arthropods that grow in warm (22°C-26°C) and humid (75%-80% humidity) environments. It lives on the dander and hair of humans or animals (cats or dogs). There are 16 species of dust mites in the domestic environment, including European house dust mite, American house dust mite, Maynella dust mite, sweet mite with tropical claw mite and acarid mite, Tymite mite ), etc., among which three kinds of European house dust mite (Dermatophagoides pteronyssinus), American house dust mite (Dermatophagoides farinae) and tropical claw mite (Blomia tropicalis) are allergens. In particular, the European house dust mite (Dermatophagoides spteronyssinus) is a major allergen of asthma, sneezing, allergic conjunctivitis and atopic dermatitis.

Endoglucanase: The term "endoglucanase" means endo-1,4-(1,3; 1,4)-β-D-glucan 4-glucanohydrolase ( EC3.2.1.4), which catalyze 1,4-β-D-glycosidic bonds in cellulose, cellulose derivatives (such as carboxymethylcellulose and hydroxyethylcellulose), lichenan, mixed β-1 ,3 Endohydrolysis of β-1,4 bonds in glucans such as cereal β-D-glucan or xyloglucan and other plant materials containing cellulosic components. Endoglucanase activity can be determined by measuring a decrease in substrate viscosity or an increase in reducing ends as determined by reducing sugar assays (Zhang et al., 2006, Biotechnology Advances [Biotechnology Advances] 24:452-481 ). For the purposes of the present invention, carboxymethylcellulose (CMC) was used as The substrate determines the endoglucanase activity.

Fragment: The term "fragment" means a polypeptide having one or more (eg, several) amino acids deleted from the amino and/or carboxyl terminus of a substantial portion of a mature polypeptide; wherein the fragment has enzymatic activity. In one aspect, a fragment contains at least 85% (eg, at least 90%, or at least 95%) of the amino acid residues of the mature polypeptide of the enzyme.

Hemicellulolytic enzyme or hemicellulase: The term "hemicellulolytic enzyme" or "hemicellulase" means one or more (eg, several) enzymes that can hydrolyze hemicellulosic material. See, eg, Shallom, D. and Shoham, Y., Microbial hemicellulases, Current Opinion In Microbiology, 2003, 6(3):219-228). Hemicellulases are key components in plant biomass degradation. Examples of hemicellulases include, but are not limited to: acetylmannan esterase, acetylxylan esterase, arabinanase, arabinofuranosidase, coumaric acid esterase, ferulic acid esterase, galactoside Enzyme, glucuronidase, glucuronyl esterase, mannanase, mannosidase, xylanase, and xylosidase. The substrates of these enzymes (hemicelluloses) are a heterogeneous population of branched and linear polysaccharides that bind via hydrogen bonds to the cellulose microfibrils in plant cell walls, cross-linking them into a stable network. Hemicellulose is also covalently attached to lignin, forming highly complex structures together with cellulose. The variable structure and organization of hemicellulose requires the concerted action of many enzymes for its complete degradation. The catalytic modules of hemicellulases are glycoside hydrolase (GH), which hydrolyzes glycosidic bonds, or carbohydrate esterase (CE), which hydrolyzes ester bonds of acetic or ferulic acid side groups. These catalytic modules can be assigned to GH and CE families based on their primary sequence homology. Some families (with generally similar folds) can be further grouped into clans, labeled with letters (eg, GH-A). The most detailed and up-to-date classification of these and other carbohydrate-active enzymes is available in the Carbohydrate-Active Enzymes (CAZy) database. Can be measured at a suitable temperature (eg 50°C, 55°C, or 60°C) and pH (eg 5.0 or 5.5) according to Ghose and Bisaria, 1987, Pure & Appl. Chem [Pure and Applied Chemistry], 59:1739-1752 Hemicellulolytic enzyme activity.

Improved wash performance : The term "improved wash performance" is defined herein as a wash performance exhibited by an enzyme, eg, by increased dust mite removal or increased dust mite reduction, relative to the wash performance of a similar wash without the enzyme.

Low stringency conditions: The term "low stringency conditions" means that for probes of at least 100 nucleotides in length, follow standard Southern blot procedures at 42°C in 5X SSPE, 0.3% SDS, 200 micrograms/ml shear Cut and denatured salmon sperm DNA was prehybridized and hybridized in 25% formamide for 12 to 24 hours. Finally the carrier material was washed three times at 50°C for 15 minutes each using 2X SSC, 0.2% SDS.

Mature polypeptide: The term "mature polypeptide" means a polypeptide in its final form after translation and any post-translational modifications such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, and the like. In the present invention, based on the SignalP 3.0 program that predicts that amino acids 1 to 21 of SEQ ID NO: 2 are signal peptides (Bendtsen et al., 2004, J. Mol. Biol. [Molecular Biology Journal] 340:783-795), The mature polypeptide of SEQ ID NO:2 is amino acids 22 to 300 of SEQ ID NO:2.

Mature polypeptide coding sequence: The term "mature polypeptide coding sequence" means a polynucleotide that encodes a mature polypeptide having enzymatic activity. In one aspect, the mature polypeptide coding sequence is nucleotides 64 to 858 of SEQ ID NO: 1, and SEQ ID NO: Nucleotides 1 to 63 of 1 encode a signal peptide.

Moderately stringent conditions: The term "moderately stringent conditions" means that for probes of at least 100 nucleotides in length, follow standard Southern blot procedures at 42°C in 5X SSPE, 0.3% SDS, 200 micrograms/ml shear Cut and denatured salmon sperm DNA was prehybridized and hybridized in 35% formamide for 12 to 24 hours. Finally the carrier material was washed three times at 55°C for 15 minutes each using 2X SSC, 0.2% SDS.

Medium-high stringency conditions: The term "medium-high stringency conditions" means that for probes of at least 100 nucleotides in length, following standard Southern blotting procedures, at 42°C, in 5X SSPE, 0.3% SDS, 200 Prehybridize and hybridize for 12 to 24 hours in micrograms/ml sheared and denatured salmon sperm DNA in 35% formamide. Finally the carrier material was washed three times at 60°C for 15 minutes each using 2X SSC, 0.2% SDS.

Sequence identity : The degree of relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter "sequence identity".

For purposes of the present invention, the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48:443-453) was used to determine the Sequence identity between amino acid sequences, the algorithm such as EMBOSS software package (EMBOSS: The European Molecular Biology Open Software Suite [European Molecular Biology Open Software Suite], Rice et al., 2000, TrendsGenet. [Genetic Trend] 16:276 -277) (preferably version 5.0.0 or newer) as implemented in the Needle program. The parameters used were a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. Needle's output labeled "longest identity" (obtained using the non-simplified option) was used as percent identity and calculated as follows:

For purposes of the present invention, the sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra), such as the EMBOSS software package (EMBOSS: Implemented in the Needle program of The European Molecular Biology Open Software Suite [European Molecular Biology Open Software Suite], Rice et al., 2000, supra) (preferably version 5.0.0 or newer). The parameters used were gap opening penalty of 10, gap extension penalty of 0.5 and EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. Needle's output labeled "longest identity" (obtained using the non-simplified option) was used as percent identity and calculated as follows:

Textiles : The term "textile" means any textile material including yarns, yarn intermediates, fibers, nonwoven materials, natural materials, synthetic materials, and any other textile material from which Fabrics and products made from fabrics (eg, clothing and other articles). The textile or fabric may be in the form of knit, woven, denim, non-woven, felt, yarn, and terry. The textile may be cellulose based, such as natural cellulose products including cotton, linen/linen, jute, ramie, sisal or coir, or artificial cellulose (e.g. derived from wood pulp) including viscose Fibers/Rayon, cellulose acetate (tricell), lyocell or blends thereof. Textiles or fabrics can also be non-cellulose based, such as natural polyamides, including wool, camel hair, cashmere, mohair, rabbit fur and silk, or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof, and blends of cellulose-based and non-cellulose-based fibers. Examples of blends are blends of cotton and/or rayon/viscose fibers with one or more accompanying materials such as wool, synthetic fibers (e.g. polyamide fibers, acrylic fibers, polyester fibers, Polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers) and/or cellulose-containing fibers (such as rayon/viscose, ramie, linen/linen, jute, cellulose acetate fibers, rayon Cell fiber). The fabric may be regular washable laundry, such as stained household laundry. When the terms fabric or garment are used, it is intended that the broad term textile is also included.

Wash cycle: The term "wash cycle" is defined herein as a washing operation in which textiles are exposed to a wash solution for a period of time by circulating a wash solution and optionally mechanically treating the textiles in order to clean the textiles and eventually remove excess wash solution. The wash cycle may be repeated one, two, three, four, five or even six times at the same or different temperatures. Thereafter, the textile is typically rinsed and dried. One of the washing cycles may be a soaking step, wherein the textile is kept soaked in a wash liquor for a period of time.

Wash liquor: The term "wash liquor" is intended to mean a solution or mixture of water and detergent components optionally including enzymes for use in eg laundry.

Dishwashing detergent composition: The term "dishwashing detergent composition" means a combination useful for removing and/or reducing undesired compounds from a surface to be cleaned, such as the surface of a ware or a surface found inside a warewashing machine things.

The warewashing detergent composition may be any composition intended for reducing and/or removing soiling of dishes, tableware, pots, pans, cutlery and for reducing and/or removing soiling of interior surfaces of dishwashing machines All forms of composition. The present invention is not limited to any particular type of warewashing detergent composition. These terms encompass any detergent component selected for the particular type of cleaning composition and product form desired (eg, liquid, gel, powder, bar, granule, paste or spray composition). The detergent composition may contain enzymes other than the amylase and/or protease contained in the composition, such as one or more additional enzymes, such as protease, amylase, lipase, cutinase, cellulase, endo Glucanase, xyloglucanase, pectinase, pectin lyase, xanthanase, peroxidase, haloperoxygenase, catalase, and mannanase, or any mixtures; and detergent components.

Dishwasher: The term "dishwasher" refers to any kind of washing machine that can be used for industrial or institutional warewashing. The term includes, but is not limited to, door warewashing machines, hood warewashing machines, conveyor belt warewashing machines, undercounter warewashing machines, glass washers, flightwarewashing machines, pot and pan warewashing machines and utensil scrubbers.

Ware : The term "ware" is intended to mean any form of tableware, kitchen utensil, dinner set or tableware such as, but not limited to, pots, pans, drinking glasses, cups, knives, forks, spoons, china, etc. Vessels may be made of any suitable material such as metal, glass, rubber, plastic, PVC, acrylic, ceramic, porcelain or porcelain.

Wash performance : The term "wash performance" is used for the ability of an enzyme to remove or reduce the presence of dust mites on the surface to be cleaned or on the textile, eg during a cleaning cycle.

Wash time: The term "wash time" is defined herein as the time taken for a complete wash process; ie one or more wash cycles and one or more rinse cycles together.

Detailed ways

The present invention relates to the use of one or more enzymes capable of degrading cellulosic material to reduce dust mites from textiles by adding the enzyme or enzymes to a detergent during the wash cycle. The inventors of the present invention have found that by adding to detergents enzymes capable of degrading cellulosic materials, the number of dust mites adhering to textiles can be significantly reduced. In one aspect, the enzyme is an enzyme composition comprising a cellulase or hemicellulase.

In another aspect, the present invention relates to an enzyme composition for removing dust mites. Wherein, the enzyme composition for removing dust mites comprises one or more cellulase or hemicellulase. Wherein, the cellulase may be GH45 cellulase. Additionally, the GH45 cellulase may be a GH45 endoglucanase. In another aspect, the cellulase is the Rhizopus terrestris endoglucanase of SEQ ID NO:2, or comprises at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity of amino acid sequences or cellulose consisting of enzyme.

In another aspect, the present application further comprises a detergent composition comprising an enzyme capable of degrading cellulosic material or comprising an enzyme composition as mentioned above.

In yet another aspect, the present application encompasses a method for removing dust mites, the method comprising:

(1) Washing or exposing textiles with a detergent composition comprising an enzyme capable of degrading a cellulosic material or an enzyme composition comprising an enzyme capable of degrading a cellulosic material, wherein the enzyme capable of degrading a cellulosic material comprises GH45 cellulase , wherein the GH45 cellulase is a GH45 endoglucanase, in another aspect, the endoglucanase is a T.t endoglucanase;

(2) Optionally rinsing the textile.

enzyme

An enzyme or enzyme composition comprising a cellulase or hemicellulase may further comprise one or more enzymes,

such as proteases, lipases, cutinases, amylases, carbohydrases, cellulases, pectinases, mannanases, arabinases, galactanases, xylanases, oxidases such as laccase, and/or peroxidase.

Generally, the properties of the selected one or more enzymes should be compatible with the selected detergent (i.e., pH optimum, compatibility with other enzyme ingredients or non-enzyme ingredients, etc.), and the one or more Enzymes should be present in effective amounts.

cellulase

Suitable cellulases include those of bacterial or fungal origin. Chemically modified mutants or protein engineered mutants are included. Suitable cellulases include enzymes from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium Cellulases of the genus Acremonium, such as Humicola insolens, Myceliophthora thermophila disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757 and WO 89/09259 and fungal cellulase produced by Fusarium oxysporum.

Particularly suitable cellulases are alkaline or neutral cellulases with color care benefits. Examples of such cellulases are the cellulases described in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940. Further 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.

Other cellulases are endo-beta-1,4-glucanases having at least 97% identity to the amino acid sequence from position 1 to position 773 of SEQ ID NO: 2 of WO 2002/099091 Identity, or a Family 44 xyloglucanase having a sequence at least 60% identical to positions 40-559 of SEQ ID NO: 2 of WO 2001/062903.

Commercially available cellulases include Celluzyme ^™ and Carezyme ^™ (Novozymes A/S), Carezyme Premium ^™ (Novozymes), Celluclean ^™ (Novozymes), Celluclean Classic ^™ (Novozymes (Novozymes), Cellusoft ^TM (Novozymes), Whitezyme ^TM (Novozymes), Clazinase ^TM and Puradax HA ^TM (Genencor International Inc.), and KAC-500(B) ^TM (Kao Corporation).

GH45 cellulase

GH family 45 cellulases (formerly known as family K) act by converting the anomeric configuration to produce the α-D anomer of the oligosaccharide as a product. It has been clarified that in the active site, one aspartate amino acid acts as a generalized acid and the other acts as a generalized base.

The three-dimensional structure of the family 45 enzyme has been elucidated (see, e.g., the structure of Humicola insolens in: Davies et al., 1996, ActaCrystallographica Section D-Biological Crystallography 52: 7-17 Part 1). These enzymes contain a beta-barrel of six strands attached to a seventh strand. The structure contains parallel and antiparallel beta strands. The active center is located in an open substrate-binding groove.

As used herein, the term "GH45 cellulase", "Family 45 cellulase" or "Cel45" means a carbohydrate-active cellulase containing a glycoside hydrolase family 45 catalytic domain classified according to EC 3.2.1.4. The term covers carbohydrate-active enzymes that hydrolyze cellulose and cellooligosaccharides using a conversion mechanism and have one of the following two characteristic sequences near the catalytic aspartate amino acid: (i) A/S/T-T-R/N/T-Y Both the first conserved signature sequence of /F/T-X-D-X-X-X-X-X-C/A-A/G/S-W/C and the second conserved signature sequence of H/Q/D/N-F/L-D-I/L/F; or (ii) have H/Q/ The second conserved signature sequence of D/N-F/L-D-I/L/F, but lacking the first conserved sequence. In one embodiment, the second conserved signature sequence is H-F-D-I.

Table 1: Family 45 cellulase subfamily B members:

Table 2: Family 45 cellulase subfamily A members:

In a preferred embodiment, the GH45 cellulase is a Thermophila terrestris endoglucanase.

In a further aspect, the T.t endoglucanase is selected from the group consisting of:

(1) T.t endoglucanase, the T.t endoglucanase comprises the mature polypeptide of SEQ ID NO: 1 or a fragment thereof, or consists of it;

(2) T.t endoglucanase, which T.t endoglucanase comprises at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 80% of the mature polypeptide of SEQ ID NO:1, 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%, or at least 99% sequence identity of amino acid sequences, or consist thereof;

(3) T.t endoglucanase, the T.t endoglucanase is encoded by a polynucleotide, and the polynucleotide comprises at least 60%, at least 65%, At least 70%, 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%, or at least 99% sequence identity, or derived therefrom composition;

(4) T.t endoglucanase, the T.t endoglucanase is encoded by a polynucleotide, and the polynucleotide is compatible with the mature polypeptide of SEQ ID NO:2 under at least high stringent conditions and very high stringent conditions The coding sequence or its full-length complement hybridizes.

detergent composition

Enzymes capable of degrading cellulosic materials may be present in laundry detergent compositions comprising at least one or more additional enzymes. Additional enzymes may be selected from the group consisting of hemicellulase, peroxidase, protease, cellulase, xylanase, lipase, phospholipase, esterase, cutinase, pectinase, mannanase Carbohydrase, pectin lyase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, lignase, pullulanase, tannase, pentosanase, maranaase, β- Dextranase, arabinosidase, hyaluronidase, chondroitinase, laccase, DNase, chlorophyllase, amylase, perhydrolase, peroxidase, xanthanase, and mixtures thereof. In one embodiment of the invention, the at least one or more additional enzymes are selected from proteases, lipases, mannanases, pectin lyases and amylases.

The detergent composition comprises a surfactant which may be selected from the group consisting of anionic, cationic, nonionic, semipolar and zwitterionic surfactants. Additionally, other detergent ingredients such as builders and polymers can be included in the detergent composition. When improving the water absorbency of a textile, it has the benefit that the item, such as a towel, can absorb more water when used to dry the skin or surface.

The present invention further encompasses a method for removing dust mites comprising subjecting a textile to an enzyme capable of degrading a cellulosic material, or to an enzyme composition comprising an enzyme capable of degrading a cellulosic material.

In one aspect, methods for removing dust mites include:

(3) Washing or exposing textiles with a detergent composition comprising an enzyme capable of degrading a cellulosic material or an enzyme composition comprising an enzyme capable of degrading a cellulosic material, wherein the enzyme capable of degrading a cellulosic material comprises GH45 cellulase , wherein the GH45 cellulase is a GH45 endoglucanase, in another aspect, the endoglucanase is a T.t endoglucanase,

(4) Optionally rinsing the textile.

The detergent composition may be, for example, a laundry detergent composition and may be in the following forms: powder, bar, uniform tablet, tablet with two or more layers, pouch with one or more chambers, regular Or compressed powder, granule, paste, gel, or regular, compressed or concentrated liquid. The composition may be a powder or granules, wherein the acidic material is coated on the powder or granules as an outer layer.

Mannanase

Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. The mannanase may be a family 5 or 26 alkaline mannanase. It may be wild-type from Bacillus or Humicola, especially from B. agaradhaerens, B. licheniformis, B. halodurans, Kraus Bacillus (B.clausii), or Humicola insolens (H.insolens). Suitable mannanases are described in WO 1999/064619. A commercially available mannanase is Mannaway (Novozymes).

peroxidase/oxidase

Suitable peroxidases/oxidases include those of plant, bacterial, or fungal origin. Chemically modified mutants or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, such as from C. cinereus, and variants thereof, as described in WO 93/24618, WO 95/10602 and those described in WO 98/15257. Commercially available peroxidases include Guardzyme ^™ (Novozymes). Peroxidases according to the invention also include haloperoxidases, such as chloroperoxidases, bromoperoxidases and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidase (EC 1.11.1.10) catalyzes the formation of hypochlorite from chloride ions.

In an embodiment, the haloperoxidase of the invention is a chloroperoxidase. Preferably, the haloperoxidase is a vanadium haloperoxidase, ie a vanadate-containing haloperoxidase. In a preferred method of the invention, a vanadate-containing haloperoxidase is combined with a source of chloride ions.

Haloperoxidases have been isolated from many different fungi, especially from the dematiaceous hyphomycete fungal group, 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. aureofaciens). enzymes.

In a preferred embodiment, the haloperoxidase may be derived from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, as described in WO Curvularia inequalis CBS 102.42 in 95/27046; or Curvularia verruculosa CBS 147.63 or Curvularia verruculosa CBS 444.70 as described in WO 97/04102; or derived from Drechslerahartlebii as described in WO 01/79459 , Dendryphiella salina as described in WO 01/79458, Phaeotrichoconis crotalarie as described in WO 01/79461, or Geniculosporium species as described in WO 01/79460.

Oxidases according to the invention include in particular any laccases encompassed by enzyme class EC 1.10.3.2 or fragments derived therefrom exhibiting laccase activity, or compounds exhibiting similar activity, such as catechol oxidase (EC 1. 10.3.1), o-aminophenol oxidase (EC 1.10.3.4) or bilirubin oxidase (EC 1.3.3.5).

protease

Suitable proteases include those of bacterial, fungal, plant, viral or animal origin, eg plant or microbial origin. Microbial origin is preferred. Chemically modified mutants or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. The serine protease may eg be a serine protease of the S1 family (eg trypsin) or the S8 family (eg subtilisin). The metalloprotease may for example be a thermolysin from eg the M4 family or other metalloproteases such as those from the M5, M7 or M8 family.

The term "subtilase" refers to a subgroup of serine proteases according to Siezen et al., Protein Engng. [Protein Engineering] 4 (1991) 719-737 and Siezen et al., Protein Science [Protein Science] 6 (1997) 501-523 . Serine proteases are a subgroup of proteases characterized by having a serine in the active site that forms a covalent adduct with a substrate. Subtilases can be divided into 6 subclasses, namely, subtilisin family, thermophilic protease family, proteinase K family, lanthionine antibiotic peptidase family, Kexin family and Pyrolysin family.

Examples of subtilases are those derived from the genus Bacillus, e.g., Bacillus lentus, B. alkalophilus, B. subtilis, B. B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii; and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 and the protease PD138 described in (WO 93/18140). Other useful proteases may be those described in WO 92/175177, WO 01/016285, WO 02/026024 and WO 02/016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and Fusarium protease (described in WO 89/06270, WO 94/25583 and WO 05/040372), and Cellulomonas ( Chymotrypsin of Cellumonas) (described in WO 05/052161 and WO 05/052146).

Further preferred proteases are alkaline proteases from Bacillus lentus DSM 5483 (as described eg in WO95/23221) and variants thereof (described in WO 92/21760, WO 95/23221, EP 1921147 and EP 1921148).

Examples of metalloproteases are neutral metalloproteases such as those derived from Bacillus amyloliquefaciens as described in WO 07/044993 (Genencor Int.).

Examples of useful proteases are the variants described in WO 92/19729, WO 96/034946, WO 98/20115, WO 98/20116, WO 99/011768, WO 01/44452, WO 03/006602, WO 04 /03186, WO 04/041979, WO 07/006305, WO 11/036263, WO 11/036264, especially variants with substitutions at one or more of the following positions: 3, 4, 9, 15, 27 ,36,57,68,76,87,95,96,97,98,99,100,101,102,103,104,106,118,120,123,128,129,130,160,167,170 , 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252, and 274, using BPN' for numbering. More preferably, the subtilase variant may comprise the following mutations: S3T, V4I, S9R, A15T, K27R, *36D, V68A, N76D, N87S, R, *97E, A98S, S99G, D, A, S99AD, S101G, M, R S103A, V104I, Y, N, S106A, G118V, R, H120D, N, N123S, S128L, P129Q, S130A, G160D, Y167A, R170S, A194P, G195E, V199M, V205I, L217D, N218D, M222VS, A2 , K235L, Q236H, Q245R, N252K, T274A (use BPN' for numbering).

Duralase^Tm、Durazym^Tm、

(诺维信公司)，以下列商品名出售的那些：

(丹尼斯克集团(Danisco)/杜邦公司(DuPont))、Axapem^TM(吉斯特-布罗卡德斯公司(Gist-Brocases N.V.))、BLAP(US 5352604的图29中所示的序列)及其变体(汉高公司(Henkel AG))和来自花王株式会社(Kao)的KAP(嗜碱芽孢杆菌(Bacillus alkalophilus)枯草杆菌蛋白酶)。Suitable commercially available proteases include those sold under the following tradenames:

Duralase ^Tm , Durazym ^Tm ,

(Novozymes), those sold under the following trade names:

(Danisco/DuPont), Axapem ^™ (Gist-Brocases NV), BLAP (sequence shown in Figure 29 of US 5352604) and Variants thereof (Henkel AG) and KAP (Bacillus alkalophilus subtilisin) from Kao.

Lipase and cutinase

Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified mutant enzymes or protein engineered mutant enzymes are included. Examples include those from the genus Thermomyces, for example from T. lanuginosus (earlier named Humicola lanuginosa) as described in EP258068 and EP 305216. ) lipases; cutinases from Humicola, such as Humicola insolens (H. insolens) (WO 96/13580); strains from Pseudomonas (some of these are now renamed Burkholderia (Burkholderia)), such as Pseudomonas alcaligenes (P.alcaligenes) or pseudoalcaligenes (P.pseudoalcaligenes) (EP 218272), Pseudomonas cepacia (P. cepacia) (EP 331376), Pseudomonas strain SD705 (WO 95/06720 and WO 96/27002), lipase from P. wisconsinensis (WO96/12012); GDSL-type Streptomyces Streptomyces lipase (WO 10/065455); Cutinase from Magnaporthe grisea (WO 10/107560); Cutinase from Pseudomonas mendocina (US 5,389,536); Lipase from Thermobifida fusca (WO 11/084412); Lipase from Geobacillus stearothermophilus (WO 11/084417); Lipase from Bacillus subtilis (WO 11/ 084599); and lipases from Streptomyces griseus (WO 11/150157) and S. pristinaespiralis (WO 12/137147).

Other examples are lipase variants such as EP 407225, WO 92/05249, WO 94/01541, WO 94/25578, WO 95/14783, WO 95/30744, WO 95/35381, WO 95/22615, WO 96/ 00292, WO 97/04079, WO 97/07202, WO 00/34450, WO 00/60063, WO 01/92502, WO 07/87508 and WO 09/109500.

Preferred commercial lipase products include Lipolase ^™ , Lipex ^™ ; Lipolex ^™ and Lipoclean ^™ (Novozymes), Lumafast (originally from Genencor), and Lipomax (originally from Gist-Bro Cardes Corporation (Gist-Brocades)).

Still other examples are lipases sometimes called acyltransferases or perhydrolases, such as the acylase with homology to Candida antarctica lipase A (WO 10/111143), from Smegmatis Acyltransferase from Mycobacterium smegmatis (WO 05/56782), perhydrolase from CE 7 family (WO 09/67279) and variants of Mycobacterium smegmatis perhydrolase (particularly from Huntsman The S54V variant used in the commercial product Gentle Power Bleach by Huntsman Textile Effects Pte Ltd) (WO 10/100028).

Amylase

Suitable amylases that may be used with the enzyme preparations of the invention may be alpha-amylases or glucoamylases and may be of bacterial or fungal origin. Chemically modified mutants or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from specific strains of Bacillus, eg Bacillus licheniformis (described in more detail in GB 1,296,839).

Suitable amylases include those having SEQ ID NO:2 in WO 95/10603 or variants thereof having 90% sequence identity to SEQ ID NO:3. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and WO 99/019467 in SEQ ID NO: 4, as variants with substitutions at 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.

Various suitable amylases include 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 with deletions in positions 181 and 182 and substitutions in position 193.

Other suitable amylases are alpha-amylases derived from Bacillus amyloliquefaciens comprising residues 1-33 of SEQ ID NO: 6 shown in WO 2006/066594 and SEQ ID NO: A hybrid alpha-amylase of residues 36-483 of the Bacillus licheniformis alpha-amylase in 4 or a variant thereof having 90% sequence identity. Preferred variants of this hybrid alpha-amylase are those with substitutions, deletions or insertions at one or more of the following positions: G48, T49, G107, H156, A181, N190, M197, I201, A209 , and Q264. Hybrid alpha-amylase comprising residues 1-33 of an alpha-amylase derived from Bacillus amyloliquefaciens shown in SEQ ID NO:6 of WO 2006/066594 and residues 36-483 of SEQ ID NO:4 Most preferred are variants with the following substitutions:

M197T;

H156Y+A181T+N190F+A209V+Q264S; or

G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S.

Another suitable amylase is the amylase having SEQ ID NO:6 in WO 99/019467 or a variant thereof having 90% sequence identity to SEQ ID NO:6. Preferred variants of SEQ ID NO: 6 are those having substitutions, deletions, or insertions in one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216, and K269. Particularly preferred amylases are those having deletions in positions R181 and G182, or positions H183 and G184.

Additional amylases that may be used are those having SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:2 or SEQ ID NO:7 of WO 96/023873 or in combination with SEQ ID NO:1, SEQ ID NO: 2. A variant thereof having 90% sequence identity to SEQ ID NO: 3 or SEQ ID NO: 7. Preferred variants of SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, or SEQ ID NO:7 are those with substitutions, deletions or insertions at one or more of the following positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304, and 476 (numbered using SEQ ID 2 of WO 96/023873). More preferred variants are those with deletions in two positions selected from 181, 182, 183, and 184 (eg, 181 and 182, 182 and 183, or positions 183 and 184). Most preferred amylase variants of SEQ ID NO:1, SEQ ID NO:2, or SEQ ID NO:7 have deletions in positions 183 and 184 and have deletions at positions 140, 195, 206, 243, 260, 304, and 476 with substitutions at one or more positions.

Other amylases that may be used are those having SEQ ID NO: 2 of WO 08/153815, SEQ ID NO: 10 of WO 01/66712, or having 90% sequence identity to SEQ ID NO: 2 of WO 08/153815 A variant thereof, or an amylase of a variant thereof having 90% sequence identity to SEQ ID NO: 10 in WO01/66712. Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those with substitutions, deletions or insertions at one or more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211, and 264.

Another suitable amylase is the amylase having SEQ ID NO:2 of WO 09/061380 or a variant thereof having 90% sequence identity to SEQ ID NO:2. Preferred variants of SEQ ID NO: 2 are those with C-terminal truncations, and/or substitutions, deletions or insertions at one or more of the following positions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444, and G475. More preferred variants of SEQ ID NO: 2 are those having substitutions at one or more of the following positions: Q87E, R, Q98R, S125A, N128C, T131I, T165I, K178L, T182G, M201L, F202Y, N225E, R, N272E, R, S243Q, A, E, D, Y305R, R309A, Q320R, Q359E, K444E, and G475K, and/or those with deletions in positions R180 and/or S181 or T182 and/or G183 . The most preferred amylase variants of SEQ ID NO: 2 are those with the following substitutions:

N128C+K178L+T182G+Y305R+G475K;

N128C+K178L+T182G+F202Y+Y305R+D319T+G475K;

S125A+N128C+K178L+T182G+Y305R+G475K; or

S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K, wherein these variants are C-terminally truncated and optionally further comprise a substitution at position 243 and/or at position 180 and/or position Deletion at 181.

Another suitable amylase is the amylase having SEQ ID NO: 1 of WO 13184577 or a variant thereof having 90% sequence identity to SEQ ID NO: 1 . Preferred variants of SEQ ID NO: 1 are those with substitutions, deletions or insertions at one or more of the following positions: K176, R178, G179, T180, G181 , E187, N192, M199, I203, S241 , R458, T459, D460, G476 and G477. More preferred variants of SEQ ID NO: 1 are those having substitutions at one or more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241QADN, R458N, T459S, D460T, G476K, and G477K , and/or those with deletions in positions R178 and/or S179 or T180 and/or G181. The most preferred amylase variants of SEQ ID NO: 1 are those with the following substitutions:

E187P+I203Y+G476K

E187P+I203Y+R458N+T459S+D460T+G476K

Wherein these variants optionally further comprise a substitution at position 241 and/or a deletion at position 178 and/or position 179.

Another suitable amylase is the amylase having SEQ ID NO: 1 of WO 10104675 or a variant thereof having 90% sequence identity to SEQ ID NO: 1 . Preferred variants of SEQ ID NO: 1 are those with substitutions, deletions or insertions at one or more of the following positions: N21, D97, V128, K177, R179, S180, I181, G182, M200, L204 , E242, G477 and G478. More preferred variants of SEQ ID NO: 1 are those having substitutions at one or more of the following positions: N21D, D97N, V128I, K177L, M200L, L204YF, E242QA, G477K, and G478K, and/or Those with deletions in positions R179 and/or S180 or I181 and/or G182. The most preferred amylase variants of SEQ ID NO: 1 are those with the following substitutions:

N21D+D97N+V128I

Wherein these variants optionally further comprise a substitution at position 200 and/or a deletion at position 180 and/or position 181.

Other suitable amylases are alpha-amylases having SEQ ID NO: 12 in WO 01/66712 or variants having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants are those having substitutions, deletions or insertions at one or more of the following positions of SEQ ID NO: 12 in WO 01/66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particularly preferred amylases include variants having deletions of D183 and G184 and having substitutions R118K, N195F, R320K and R458K, and additionally variants having substitutions at one or more positions selected from the group consisting of: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345, and A339, most preferred are variants that additionally have substitutions at all of these positions.

Other examples are amylase variants such as those described in WO 2011/098531 , WO 2013/001078 and WO 2013/001087.

Commercially available amylases are Duramyl ^™ , Termamyl ^™ , Fungamyl ^™ , Stainzyme ^™ , StainzymePlus ^™ , Natalase ^™ , Liquozyme X and BAN ^™ (from Novozymes), as well as Rapidase ^™ , Purastar ^™ /Effectenz ^™ , Powerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Genencor International/DuPont).

Enzyme concentration

In one embodiment of the invention, the enzyme capable of degrading cellulosic material of the invention may be used in a detergent composition in an amount corresponding to: 0.001-200 mg of protein, such as 0.005-100 mg, per liter of washing liquor The protein, preferably 0.01-50 mg of protein, more preferably 0.05-20 mg of protein, even more preferably 0.1-10 mg of protein.

The one or more enzymes of the detergent compositions of the invention may be stabilized using conventional stabilizers such as polyols such as propylene glycol or glycerol, sugars or sugar alcohols, lactic acid, boric acid or boric acid derivatives such as Aromatic borate esters, or phenylboronic acid derivatives, such as 4-formylphenylboronic acid, and the composition can be formulated as described in, for example, WO 92/19709 and WO 92/19708.

Surfactant

Laundry detergent compositions may comprise one or more surfactants, which may be anionic and/or cationic and/or nonionic and/or semi-polar and/or zwitterionic, or mixtures thereof .

In a particular embodiment, the detergent composition comprises a mixture of one or more nonionic surfactants and one or more anionic surfactants. One or more surfactants are typically present at a level of from about 0.1% to 60% by weight, such as from about 1% to about 40%, or from about 3% to about 20%, or from about 3% to about 10%. exist. The one or more surfactants are selected based on the desired cleaning application, and can include any one or more conventional surfactants known in the art.

When included therein, the detergent will generally contain from about 1% to about 40% by weight of anionic surfactants, such as from about 5% to about 30%, including from about 5% to about 15%, Or from about 15% to about 20%, or from about 20% to about 25% anionic surfactant. Non-limiting examples of anionic surfactants include sulfates and sulfonates, especially linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), benzene Alkane sulfonates, α-olefin sulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2,3-diyl bis(sulfates), hydroxy alkane sulfonates and Disulfonates, alkyl sulfates (AS) (such as sodium dodecyl sulfate (SDS)), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ether sulfates (AES or AEOS or FES, also known as alcohol ethoxy sulfate or fatty alcohol ether sulfate), secondary alkane sulfonate (SAS), paraffin sulfonate (PS), ester sulfonate, sulfonated fatty acid glycerides, Alpha-sulfo fatty acid methyl ester (α-SFMe or SES) (including methyl ester sulfonate (MES)), alkyl or alkenyl succinic acid, dodecenyl/tetradecenyl succinic acid (DTSA) , fatty acid derivatives of amino acids, diesters and monoesters or fatty acid salts (soaps) of sulfosuccinic acid, and combinations thereof.

When included therein, the detergent will generally contain from about 1% to about 40% by weight of cationic surfactants, for example from about 0.5% to about 30%, especially from about 1% to about 20% , from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%. Non-limiting examples of cationic surfactants include alkyl dimethyl ethanol quaternary amines (ADMEAQ), cetyl trimethyl ammonium bromide (CTAB), dimethyl distearoyl ammonium chloride (DSDMAC), and Alkylbenzyldimethylammoniums, alkylquats, alkoxylated quaternary ammonium (AQA) compounds, esterquats, and combinations thereof.

When included therein, the detergent will generally contain from about 0.2% to about 40% by weight of nonionic surfactants, such as from about 0.5% to about 30%, especially from about 1% to about 20% by weight. %, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%. Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters (such as ethoxylated oxylated and/or propoxylated fatty acid alkyl esters), alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkyl polyglycosides (APG), alkoxylated amines , fatty acid monoethanolamide (FAM), fatty acid diethanolamide (FADA), ethoxylated fatty acid monoethanolamide (EFAM), propoxylated fatty acid monoethanolamide (PFAM), polyhydroxyalkyl fatty acid amides, or glucose N-acyl N-alkyl derivatives of amines (glucamides (GA), or fatty acid glucamides (FAGA)), and products available under the SPAN and TWEEN trade names, and combinations thereof.

When included therein, detergents will generally contain from about 0% to about 20% by weight of semi-polar surfactants. Non-limiting examples of semi-polar surfactants include amine oxides (AO), such as alkyldimethylamine oxides, N-(cocoalkyl)-N,N-dimethylamine oxides, and N-( Tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxides and combinations thereof.

When included therein, detergents will generally contain from about 0% to about 20% by weight of zwitterionic surfactants. Non-limiting examples of zwitterionic surfactants include betaines, such as alkyldimethylbetaines, sultaines, and combinations thereof.

The polypeptides of the invention may also be incorporated into detergent formulations as disclosed in WO 97/07202, which is hereby incorporated by reference.

Builders and co-builders

The detergent composition may comprise from about 0% to 10% by weight, such as from about 0.1% to about 5%, of a builder or co-builder, or mixtures thereof. In softeners, builder levels are typically from 0% to 1%, especially 0% to 0.5%. Builders and/or co-builders may in particular be chelating agents which form water-soluble complexes with Ca and Mg. Any builder and/or co-builder known in the art for use in softeners can be used. 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 (eg SKS-6 from Hoechst), ethanolamines such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2'-imino Diethan-1-ol), triethanolamine (TEA, also known as 2,2',2"-nitrilotriethan-1-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

The detergent composition may also comprise from 0% to 5%, such as from about 0% to about 2%, by weight of a detergent co-builder. The detergent compositions may include co-builders alone, or in combination with builders such as zeolite builders. Non-limiting examples of co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA). Additional non-limiting examples include citrates, chelating agents such as aminocarboxylates, aminopolycarboxylates, and phosphonates, and alkylsuccinic, or alkenylsuccinic acids. 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 diacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1 , 1-diphosphonic acid (HEDP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), diethylenetriaminepenta(methylenephosphonic acid) (DTMPA or DTPMPA), N-(2- Hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)-aspartic acid (SMAS), N-(2-sulfoethyl)-aspartic acid (SEAS), N-(2-sulfomethyl)-glutamic acid (SMGL), N-(2-sulfoethyl)-glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), α-Alanine-N,N-diacetic acid (α-ALDA), Serine-N,N-diacetic acid (SEDA), Isoserine-N,N-diacetic acid (ISDA), Phenylalanine-N, N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N-diacetic acid (SLDA), taurine-N,N-diacetic acid (TUDA) and Sulfomethyl-N,N-diacetic acid (SMDA), N-(2-hydroxyethyl)-ethylenediamine-N,N',N"-triacetate (HEDTA), diethanolglycine ( DEG), diethylenetriaminepenta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP) and combinations and salts thereof. Additional exemplary builders and/or co-builders are described, for example, in WO 09/102854, US 5977053.

polymer

The detergent may comprise 0-10% by weight (eg 0.5%-5%, 2%-5%, 0.5%-2% or 0.2%-1%) polymer. Any polymer known in the art for use in softeners can be used. The polymers can function as co-builders as mentioned above, or can provide anti-redeposition, fiber protection, soil release, dye transfer inhibition, antifoam properties, perfume encapsulation and lubricity. 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 polyquaternium, melamine polymers, siloxanes, silicones, (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), Poly(ethylene glycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethylinulin (CMI), and polycarboxylates (such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymer), hydrophobically modified CMC (HM-CMC), copolymer of terephthalic acid and oligoethylene glycol, poly(para Copolymer of ethylene phthalate) and poly(oxyethylene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (PVPVI). Additional exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO), and diquaternary ammonium ethoxysulfate. Other exemplary polymers are disclosed eg in WO2006/130575. Salts of the above-mentioned polymers are also contemplated.

Accessories

Any detergent ingredient known in the art for use in softeners may also be utilized. Other optional softener components include solvents (including isopropanol, propylene glycol, alkanes/cycloalkanes), antishrink agents, anti-soil redeposition agents, anti-wrinkle agents, bactericides, preservatives (including benzisothiazoline ketones, methylisothiazolinone, and/or lactic acid), binders, dyes, enzyme stabilizers (including boric acid, borates, CMC, and/or polyols such as propylene glycol), emulsion stabilizers, defoamers ( including simethicone), skin conditioners (including caprylic/capric glyceryl, ethylhexyl stearate, or coconut oil), alone or in combination. Any ingredient known in the art for use in softeners can be used. Selection of such ingredients is well within the skill of the skilled artisan.

The present invention is further described by the following examples, which should not be construed as limiting the scope of the present invention.

anti redeposition agent

The detergent composition of the present invention may also comprise one or more anti-redeposition agents, such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and/or Polyethylene glycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimines. The cellulose-based polymers described above under soil release polymers can also function as anti-redeposition agents.

Formulation of detergent products

The detergent compositions of the present invention may be in any conventional form, such as bars, uniform tablets, tablets with two or more layers, sachets with one or more chambers, regular or compressed powders, granules, Paste, gel, or regular, compressed, or concentrated liquid.

Bags can be configured as single or multi-chambered. It may be of any form, shape and material suitable for holding the composition, eg, without releasing the composition from the pouch, prior to contact with water. The bag is made of a water-soluble film, which contains an inner volume. The internal volume can be divided into chambers of bags. Preferred films are polymeric materials, preferably polymers forming films or sheets. Preferred polymers, copolymers or derivatives thereof are selected polyacrylates, and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethyl Cellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylates, most preferably polyvinyl alcohol copolymers, and hydroxypropylmethylcellulose (HPMC). Preferably, the level of polymer in the film, such as PVA, is at least about 60%. The preferred average molecular weight will typically be from about 20,000 to about 150,000. The films may also be blend compositions comprising blends of hydrolytically degradable and water-soluble polymers such as polylactic acid and polyvinyl alcohol (known under trade reference M8630, as established by the State of Indiana, USA MonoSol LLC (MonoSol LLC) plus plasticizers like glycerin, ethylene glycol, propylene glycol, sorbitol and mixtures thereof. The pouch may contain a solid laundry cleaning composition or fractions and/or a liquid cleaning composition or fractions separated by a water soluble film. The chamber for liquid components may differ in composition from the chamber containing solids: US2009/0011970 A1.

The detergent ingredients may be physically separated from each other by compartments in the water soluble pouch or in different layers of the tablet. Thus, undesirable storage interactions between components can be avoided. Different dissolution profiles for each compartment can also cause delayed dissolution of selected components in the wash solution.

The non-unit dose liquid or gel detergent may be aqueous, typically containing at least 20% and up to 95% water by weight, such as up to about 70% water, up to about 65% water, up to about 55% water water, up to about 45% water, up to about 35% water. Other types of liquids including but not limited to alkanols, amines, glycols, ethers, and polyols may be included in the aqueous liquid or gel. Aqueous liquid or gel detergents can contain from 0-30% organic solvents.

Liquid or gel detergents can be non-aqueous.

Enzyme formulations in co-granules

The enzymes of the invention may be formulated as granules, eg, as co-granules combining one or more enzymes. Each enzyme will then be present in multiple granules which ensure a more even distribution of the enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes. A method for producing multi-enzyme co-granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

Another example of formulation of enzymes by using co-granules is disclosed in WO 2013/188331, which relates to detergent compositions comprising: (a) multi-enzyme co-granules; (b) less than 10 wt zeolite (anhydrous basis above); and (c) less than 10wt phosphate (anhydrous basis), wherein the enzyme co-granules comprise from 10wt% to 98wt% of water sink component (sink component), and the composition additionally Contains from 20wt% to 80wt% detergent water sink component.

WO 2013/188331 also relates to a method of treating and/or cleaning a surface, preferably a textile surface, comprising the steps of: (i) subjecting said surface to washing in an aqueous washing solution with as claimed and described herein contact with the agent composition, (ii) rinse and/or dry the surface.

Multi-enzyme co-granules may comprise the enzyme of the present invention and (a) one or more enzymes selected from the group consisting of: first wash lipase, cleaning cellulase, xyloglucanase, Perhydrolase, peroxidase, lipoxygenase, laccase, and mixtures thereof; and (b) one or more enzymes selected from the group consisting of hemicellulase, protease, care cellulase, Cellobiose dehydrogenase, xylanase, phospholipase, esterase, cutinase, pectinase, mannanase, pectin lyase, keratinase, reductase, oxidase, phenoloxidase, lignase , pullulanase, tannase, pentosanase, lichenase, dextranase, arabinosidase, hyaluronidase, chondroitinase, amylase, and mixtures thereof.

example

cleaning method

The compositions of the present invention are useful in essentially any washing, cleaning and/or fabric care method including, but not limited to, soaking methods, pretreatment methods, methods with a rinse step (wherein a separate rinse and composition ), and post-processing methods.

The methods described herein contact the fabrics with the wash solution in the usual manner and are exemplified hereinafter. Conventional laundry methods treat soiled fabrics with an aqueous liquid having dissolved or dispersed therein an effective amount of a laundry detergent and/or fabric care composition. The method of the invention is conveniently carried out during the cleaning process. The cleaning method is preferably carried out at temperatures between 5°C and 95°C, especially between 10°C and 60°C. The pH of the treatment solution is 6-12, preferably 7-10.

The following examples are intended to illustrate compositions of the invention, but are not necessarily intended to limit or otherwise limit the scope of the invention. In detergent compositions, enzyme levels are expressed by pure enzyme by weight of the total composition, and unless otherwise stated, detergent ingredients by weight of the total composition mean detergent ingredient levels.

Materials and methods

Test enzyme:

Thermophila terrestris endoglucanase of SEQ ID NO: 2 obtained according to WO 2012/089024;

Fabric:

CN-42, knitted cotton, commercially purchased from the Center for Testmaterials BV (Center for Testmaterials B.V, CFT), Netherlands;

E-252, striped colored cotton, commercially available from Test Materials BV Centre, Netherlands;

E-252PA, striped colored cotton, derived from E-252 mentioned above, was prepared by pretreating E-252 in a Wascator automatic washing machine at 40°C for 12 hours to produce visible pilling;

Standard Detergent A:

Prepare Standard Detergent A with the following ingredients:

method:

cleaning method

Terg-O-tometer (TOM) washing assay

Terg-O-tometer (TOM) is a medium-scale standard washing system, which can be applied to test 16 different washing conditions simultaneously. TOMs are basically large temperature-controlled water baths into which up to 16 open metal beakers are submerged. Each beaker constituted a small top-loading washer and during the experiment, each beaker contained a solution of a specific detergent/enzyme system and the performance of cotton fabrics was tested. Use a rotating stirrer arm to achieve the desired mechanical stress. The arm stirs the liquid in each beaker. Because the TOM beaker has no lid, it is possible to retrieve the sample and analyze the information online during the TOM experiment.

Equipment: A water bath with 16 steel beakers each holding 1000 mL of detergent solution and 1 rotating stirrer was used. Set the temperature to 40 °C. Fill the water bath with water. The rotational speed was set at 200 rpm/min.

1. Set the temperature in the Terg-O-Tometer to 40°C and start the rotation in the water bath. The temperature was maintained at 40 +/- 0.5°C.

2. Prepare a wash solution by adding the required amount of detergent to the solution and place it in a bucket with magnetic stirring for 10 min at 40+/- 0.5°C and 14dH. The washing solution should be used within 30 to 60 minutes after preparation.

3. Add 1000ml of wash solution to the TOM beaker.

4. Start stirring at 200 rpm and optionally add enzyme to the beaker.

5. Sprinkle the fabric into the beaker and put in the ballast load.

6. Start time measurement when the swatch and ballast are added to the beaker.

7. Wash for 70 minutes.

8. Stop stirring.

9. Transfer wash load from TOM beaker to sieve and rinse with cold tap water.

10. Separate the test material from the ballast load. Under running water, the test material was transferred to a 5 L beaker containing cold tap water.

11. Set the timer for 5 minutes.

12. Gently press out the water by hand and place the test swatch on a tray covered with a sheet of paper. Add another sheet of paper to the top of the small swatch.

13. Place the swatches in a tumble dryer to dry and measure with the Color Eye as described below.

Determination of anti-pilling effect

E-252PA was measured by Color Eye equipment (CE7000/CE7000A, Largo AB). The L value was used to quantify the anti-pilling benefit. L indicates a change in white/black from 0 to 100 levels, and a decrease in L means an increase in black (decrease in white), and an increase in L means an increase in white (decrease in black). Therefore, the lower the L value, the better the anti-pilling effect.

CN-42 was evaluated by a sensory panel, and 8-12 panelists were invited to evaluate the anti-pilling effect. The higher the score, the better the effect of CN-42.

Anti-dust mite experiment:

The test procedures and materials are as follows:

Dust mites: Dermatophagoides farina Hughhes

Steps to test dust mite reduction effectiveness:

1. Sample preparation: Cut CN-42 into 6*6cm size, and wash according to the previous washing method. Each sample was cut into a circle with a diameter of 58 mm.

2. Preventive test plan: Put a sponge with a side length of 200mm and a height of 10mm into a plastic container with a cover (side length 200-300mm, height 50-100mm, with a vent hole in the middle, a diameter of 50±10mm, covered with a PTFE film , the PTFE membrane was fixed on the plastic container lid by adhesive tape), and then the saturated NaCl solution was injected into the sponge (the sponge was immersed in the saturated NaCl solution).

3. Use 7 petri dishes, one of which is placed in the center and the other 6 petri dishes are placed in the peripheral area. Bridge every 2 adjacent Petri dishes with scotch tape. All 7 Petri dishes were then fixed on the plate.

4. Put 3 test samples and 3 reference samples into the peripheral 6 Petri dishes. Each test sample is adjacent to a reference sample. Place 0.05 g of dust mite feed in each Petri dish (see Figure 1).

5. Put 2000±200 live dust mites into the petri dish in the center.

6. Transfer the plate with the Petri dish on top to the sponge in the container. Put the lid on. The container is placed in a temperature and humidity chamber with a temperature of 25°C±2°C and a humidity of 75%±5%.

7. After incubation for 24 hours, the samples were taken out, and the number of dust mites was counted with a dissecting lens.

Example 1. Fabric treatment in the presence of cellulase

Add 2 grams of standard detergent A to the Terg-o-tometer wash assay. Herein, Rhizoctonia terrestris of SEQ ID NO: 2 was used. The enzyme protein concentration in the detergent is 0.005%. Dilute each detergent to 1 L with water. Ballast is required to fill wash items to 40g.

Fabric E-252PA with dimensions 8*8cm2 was used to evaluate the anti-pilling effect of the test enzymes. This fabric was mixed with standard detergent A diluted in the Terg-o-tometer washing assay and washed at 40°C for 3 cycles for 70 min. The L* value is used to indicate the anti-pilling effect. The result is shown in Figure 2. Figure 2 shows that a better anti-pilling effect is achieved in the presence of cellulase compared to those without cellulase treatment (blank). The L value dropped from greater than 34.1 to about 27.9.

Fabric CN-42 with a size of 10*10cm2 was used to evaluate the anti-dust mite effect. This fabric was mixed with standard detergent A diluted in the Terg-o-tometer washing assay and washed at 40°C for 3 cycles for 70 min. Figure 3 shows the results of the anti-dust mite experiment compared to the experiment without cellulase treatment (blank). As can be seen in Figure 3, the number of dust mites has been reduced to one-third of that of the blank (from 157 to 48).

sequence listing

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Claims (20)

CLAIMS 1. Use of an enzyme capable of degrading cellulosic material for reducing/removing dust mites on textiles. 2. Use according to claim 1, wherein the enzyme capable of degrading cellulosic material is a GH45 cellulase. 3. The use according to claim 1, wherein the enzyme capable of degrading cellulosic material is any one or more GH45 cellulase selected from the following table:

. 4. The use according to claim 3, wherein the GH45 cellulase is a Rhizopus terrestris endoglucanase. 5. The use according to claim 4, wherein the Rhizopus terrestris endoglucanase is selected from the group consisting of: (1) T.t endoglucanase, the T.t endoglucanase comprises the mature polypeptide of SEQ ID NO: 2 or a fragment thereof, or consists of it; (2) T.t endoglucanase, the T.t endoglucanase comprises at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 80% of the mature polypeptide of SEQ ID NO:2, 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%, or at least 99% sequence identity of amino acid sequences, or consist thereof; (3) T.t endoglucanase, the T.t endoglucanase is encoded by a polynucleotide, and the polynucleotide comprises at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity, or consist of nucleotide sequences ; (4) T.t endoglucanase, the T.t endoglucanase is encoded by a polynucleotide, and the polynucleotide is compatible with the mature polypeptide of SEQ ID NO:1 under at least high stringent conditions and very high stringent conditions The coding sequence or its full-length complement hybridizes. In another aspect, the cellulase composition further comprises one or more detergent components or fabric softeners. 6. An enzyme composition for reducing or removing dust mites from textiles, the enzyme composition comprising an enzyme capable of degrading cellulosic material. 7. The enzyme composition of claim 6, wherein the enzyme capable of degrading cellulosic material is a GH45 cellulase. 8. The enzyme composition of claim 6, wherein the enzyme capable of degrading cellulosic material is a GH45 cellulase selected from the following table:

. 9. The enzyme composition of claim 8, wherein the GH45 cellulase is a Rhizopus terrestris endoglucanase. 10. The enzyme composition of claim 9, wherein the Rhizopus terrestris endoglucanase is selected from the group consisting of: (1) T.t endoglucanase, the T.t endoglucanase comprises the mature polypeptide of SEQ ID NO: 2 or a fragment thereof, or consists of it; (2) T.t endoglucanase, the T.t endoglucanase comprises at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 80% of the mature polypeptide of SEQ ID NO:2, 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%, or at least 99% sequence identity of amino acid sequences, or consist thereof; (3) T.t endoglucanase, the T.t endoglucanase is encoded by a polynucleotide, and the polynucleotide comprises at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity, or consist of nucleotide sequences ; (4) T.t endoglucanase, the T.t endoglucanase is encoded by a polynucleotide, and the polynucleotide is compatible with the mature polypeptide of SEQ ID NO:1 under at least high stringent conditions and very high stringent conditions coding sequence or its full-length complement; in another aspect, the cellulase composition further comprises one or more detergent components or fabric softeners. 11. The enzyme composition of claim 6, further comprising at least one or more additional enzymes selected from the group consisting of hemicellulase , peroxidase, protease, cellulase, xylanase, lipase, phospholipase, esterase, cutinase, pectinase, mannanase, pectin lyase, keratinase, reductase, oxidation Enzyme, phenoloxidase, lipoxygenase, lignase, pullulanase, tannase, pentosanase, maranaase, beta-glucanase, arabinosidase, hyaluronidase, cartilage Sulfase, laccase, DNase, chlorophyllase, amylase, perhydrolase, peroxidase, xanthanase, and mixtures thereof. 12. The enzyme composition of claim 11, wherein the at least one or more additional enzymes are selected from the group consisting of proteases, lipases, mannanases, pectate lyases and amylases. 13. A detergent composition for reducing or removing dust mites from textiles, comprising an enzyme composition as claimed in any one of claims 6-12, a surfactant, a builder and polymer. 14. A detergent composition according to claim 13, wherein said surfactant is selected from the group consisting of anionic, cationic, nonionic, semipolar and zwitterionic surfactants. 15. The detergent composition according to claim 13 or 14, further comprising one or more components selected from the group consisting of: bleaching system, bleach activator, bleach catalyst, silicic acid Salt and dyes. 16. A detergent composition as claimed in any one of the preceding claims, wherein the composition is in the form of a powder, a bar, a uniform tablet, a tablet with two or more layers, a tablet with one or more Individual compartment bags, regular or compressed powders, granules, pastes, gels, or regular, compressed or concentrated liquids. 17. A detergent composition as claimed in any one of the preceding claims, wherein the amount of enzyme composition used in the detergent composition corresponds to the following: 0.001-200 mg of protein per liter of wash liquor, such as 0.005-100 mg The protein, preferably 0.01-50 mg of protein, more preferably 0.05-20 mg of protein, even more preferably 0.1-10 mg of protein. 18. A method for reducing or removing dust mites from textiles, the method comprising: (1) washing or exposing the textile with any detergent composition as described in claims 13-17 or with any enzyme composition as described in claims 6-12; (2) Optionally rinsing the textile. 19. The method of claim 18, wherein the method is performed by hand or by machine. 20. A method as claimed in any one of claims 18-19, wherein the method is a laundry or washing method, or a warewashing method.

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