WO2018224544A1

WO2018224544A1 - Compositions comprising polypeptides having cellulase activity and amylase activity, and uses thereof in cleaning and detergent compositions

Info

Publication number: WO2018224544A1
Application number: PCT/EP2018/064888
Authority: WO
Inventors: Iben DAMAGER
Original assignee: Novozymes A/S
Priority date: 2017-06-08
Filing date: 2018-06-06
Publication date: 2018-12-13

Abstract

The present invention relates to compositions comprising a polypeptide having cellulase activity and a polypeptide having alpha-amylase activity. The present invention further relates to methods of using such compositions.

Description

COMPOSITIONS COMPRISING POLYPEPTIDES HAVING CELLULASE ACTIVITY AND AMYLASE ACTIVITY, AND USES THEREOF IN CLEANING AND DETERGENT COMPOSITIONS Reference to a Sequence Listing

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

BACKGROUND OF THE INVENTION

The present invention relates to compositions comprising polypeptides exhibiting cellulase activity and one or more amylases and uses thereof in cleaning or detergent applications and processes such as cleaning hard-surfaces, dish wash and laundering.

Description of the Related Art

Beta-glucans are polysaccharides consisting of glucose units linked by beta-glucosidic bonds. Cellulose is one type of beta-glucan, in which all of the glucose units are linked by beta- 1 ,4-glucosidic bonds. This feature results in the formation of insoluble cellulose micro-fibrils. Enzymatic hydrolysis of cellulose to glucose requires the use of endo beta-glucanases (e.g. EC 3.2.1.4), cellobiohydrolases (e.g. EC 3.2.1.91 ) and beta-glucosidases (e.g. EC 3.2.1.21 ).

The removal of cereal stains as oat and barley containing stains in dish wash and laundry is a recognized problem, and there is a considerable interest in finding enzymes that can degrade the beta-glucans found therein. Various Bacillus species like e.g. B. amyloliquefaciens express a beta-glucanase and various cellulases. However, some of these enzymes are generally not very suitable for alkaline applications, e.g. at pH 7.5 or above.

Alpha-amylases (alpha-1 ,4-glucan-4-glucanohydrolases, E.C. 3.2.1 .1 ) constitute a group of enzymes, which catalyses hydrolysis of starch and other linear and branched 1 ,4-gluosidic oligo- and polysaccharides. Alkaline amylases, such as AA560, form a particular group of alpha- amylases that have found use in detergents. Many of these known bacterial amylases have been modified in order to improve their functionality in a particular application.

Thus, it is an object of the present invention to provide compositions which have an improved effectiveness in removal of polysaccharides comprising beta-glucans and starch.

SUMMARY OF THE INVENTION

In one aspect, the present invention relates to a composition comprising (i) a polypeptide having cellulase activity, selected from the group consisting of:

(a) a polypeptide having at least 70% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, and

(b) a fragment of the polypeptide of (a) that has cellulase activity;

and (ii) at least one polypeptide having alpha-amylase activity.

In another aspect, the present invention relates to the use of a composition of the present invention in a cleaning process such as laundry, optionally the use is carried out under alkaline conditions having pH 7.5 or above.

In another aspect, the present invention relates to a process of degrading a cellulose- containing material comprising applying the composition of the present invention to the cellulose- containing material; optionally, the process is carried out under alkaline conditions having pH 7.5 or above.

In another aspect, the present invention relates to a method for reducing or preventing soil re-deposition using a composition of the present invention.

The present invention also relates to methods of laundering fabrics or textiles or hard surface cleaning including automated dish wash (ADW) and hand dish wash (HDW) usia composition (e.g. cleaning or detergent composition) of the invention.

OVERVIEW OF SEQU

SEQ ID NO: 1 ii s the amino acid sequence of a cellulase (Cellulase 1 ).

SEQ ID NO: 2 ii s the amino acid sequence of a cellulase (Cellulase 2).

SEQ ID NO: 3 ii s the amino acid sequence of a cellulase (Cellulase 3).

SEQ ID NO: 4 ii s the amino acid sequence of a cellulase (Cellulase 4).

SEQ ID NO: 5 ii s the amino acid sequence of a cellulase (Cellulase 5).

SEQ ID NO: 6 ii s the amino acid sequence of an alpha-amylase (AA560).

SEQ ID NO: 7 ii s the amino acid sequence of an alpha-amylase (SP722).

SEQ ID NO: 8 ii s the amino acid sequence of an alpha-amylase (TS23).

SEQ ID NO: 9 ii s the amino acid sequence of an alpha-amylase (cytophaga).

SEQ ID NO: 10 is the amino acid sequence of an alpha- -amylase (SP707).

SEQ ID NO: 1 1 is the amino acid sequence of an alpha- -amylase (LASB0000).

SEQ ID NO: 12 is the amino acid sequence of an alpha- -amylase (SP.7-7).

SEQ ID NO: 13 is the amino acid sequence of an alpha- -amylase (Termamyl).

SEQ ID NO: 14 is the amino acid sequence of an alpha- -amylase (Fusion protein).

SEQ ID NO: 15 is the amino acid sequence of an alpha- -amylase (KSM-AP1378).

SEQ ID NO: 16 is the amino acid sequence of an alpha- -amylase (KSM-K38).

SEQ ID NO: 17 is the amino acid sequence of an alpha- -amylase (BSG).

SEQ ID NO: 18 is the amino acid sequence of an alpha- -amylase (BAN).

SEQ ID NO: 19 is the amino acid sequence of an alpha- -amylase (AAI 10). SEQ ID NO: 20 is the amino acid sequence of a protease (Savinase).

Definitions

Alpha-amylase: The term "alpha-amylase" means an alpha-amylase which catalyses the hydrolysis of starch and other linear and branched 1 ,4-glucosidic oligo- and polysaccharides (enzymes of the alpha-1 ,4-glucan-4-glucanohydrolases, E.C. 3.2.1 .1 ).

Alpha-amylase activity: The term "alpha-amylase activity" means the activity of alpha-1 ,4-glucan-4-glucanohydrolases, E.C. 3.2.1.1 , which constitute a group of enzymes, which catalyze hydrolysis of starch and other linear and branched 1 ,4-alpha-glucosidic oligo- and polysaccharides. Alpha-amylase activity may be determined by pNP-G7 assay as described in the Examples herein.

Anti-redeposition: The term "anti-redeposition" or "anti-redeposition effect" means the reduction or prevention of soil from depositing back onto the textile, fabric or hard surface. The anti-redeposition effect can be determined using the Mini-LOM or Mini-TOM wash assay.

Synergistic effect: The term "synergistic effect" means a cooperative action of polypeptides such that a total combined effect of said polypeptides is greater than the sum of the individual enzymatic effects of said polypeptides. Non-limiting examples of synergistic effect include REM synergistic effect of a beta-glucanase polypeptide of the invention and one or more alpha-amylase.

REM synergistic effect: REM synergistic effect of polypeptides as used herein can be measured based on the analysis of stain removal carried out by using any suitable wash performance methodology (e.g. Wascator bottle wash method). A preferred method for determining the REM synergistic effect is disclosed in Example 2.

Beta-glucanase: The term "beta-glucanase" as used herein means an endo beta-1 ,4- glucanase activity (e.g. endo-1 ,4-3-D-glucanase) that catalyzes the hydrolyses of a beta-1 ,4- bonds connecting two glucosyl residues in a beta-glucan. Non-limiting examples of beta- glucanases as defined herein include cellulases (e.g. EC 3.2.1.4, e.g. having endo-cellulase activity on β-1 ,4 linkages between D-glucose units. For purposes of the present invention, beta- glucanase activity is determined according to the procedure described in the Examples. In one aspect of the invention, the polypeptides of the present invention have at least 20%, e.g., at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or at least 100% of the beta-glucanase activity of the polypeptide having the sequence selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ I D NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5. Beta-glucanase activity can suitably be measured using cellulose as substrate.

Beta-glucan: The term "beta-glucan" as used herein means a polysaccharide that only contains glucose as structural components, and in which the glucose units are linked by beta- glycosidic bonds. Non-limiting examples of beta-glucans include beta-D-glucans, beta-1 ,3-1 ,4 glucans, mix-linkage beta-glucans, barley beta-glucans, oatmeal beta-glucans.

Allelic variant: The term "allelic variant" means any of two or more alternative forms of a gene occupying the same chromosomal locus. Allelic variation arises naturally through mutation, and may result in polymorphism within populations. Gene mutations can be silent (no change in the encoded polypeptide) or may encode polypeptides having altered amino acid sequences. An allelic variant of a polypeptide is a polypeptide encoded by an allelic variant of a gene.

Carbohydrate binding module: The term "carbohydrate binding module" means the region within a carbohydrate-active enzyme that provides carbohydrate-binding activity (Boraston et al., 2004, Biochem. J. 383: 769-781 ). A majority of known carbohydrate binding modules (CBMs) are contiguous amino acid sequences with a discrete fold. The carbohydrate binding module (CBM) is typically found either at the N-terminal or at the C-terminal extremity of an enzyme. Some CBMs are known to have specificity for cellulose.

Catalytic domain: The term "catalytic domain" means the region of an enzyme containing the catalytic machinery of the enzyme.

cDNA: The term "cDNA" means a DNA molecule that can be prepared by reverse transcription from a mature, spliced, mRNA molecule obtained from a eukaryotic or prokaryotic cell. cDNA lacks intron sequences that may be present in the corresponding genomic DNA. The initial, primary RNA transcript is a precursor to mRNA that is processed through a series of steps, including splicing, before appearing as mature spliced mRNA.

Cellulolytic enzyme or cellulase: The term "cellulolytic enzyme" or "cellulase" means one or more (e.g., several) enzymes that hydrolyze a cellulosic material. Such enzymes include endoglucanase(s) (e.g. EC 3.2.1.4), cellobiohydrolase(s), beta-glucosidase(s), or combinations thereof. The two basic approaches for measuring cellulolytic enzyme activity include: (1 ) measuring the total cellulolytic enzyme activity, and (2) measuring the individual cellulolytic enzyme activities (endoglucanases, cellobiohydrolases, and beta-glucosidases) as reviewed in Zhang et al., 2006, Biotechnology Advances 24: 452-481. Total cellulolytic enzyme activity can be measured using insoluble substrates, including Whatman N°1 filter paper, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, pretreated lignocellulose, etc. The most common total cellulolytic activity assay is the filter paper assay using Whatman N°1 filter paper as the substrate. The assay was established by the International Union of Pure and Applied Chemistry (lUPAC) (Ghose, 1987, Pure Appl. Chem. 59: 257-68).

Cellulolytic enzyme activity can be determined by measuring the increase in production/release of sugars during hydrolysis of a cellulosic material by cellulolytic enzyme(s) under the following conditions: 1 -50 mg of cellulolytic enzyme protein/g of cellulose in pretreated corn stover (PCS) (or other pretreated cellulosic material) for 3-7 days at a suitable temperature such as 40°C-80°C, e.g., 50°C, 55°C, 60°C, 65°C, or 70°C, and a suitable pH such as 4-9, e.g., 5.0, 5.5, 6.0, 6.5, or 7.0, compared to a control hydrolysis without addition of cellulolytic enzyme protein. Typical conditions are 1 ml reactions, washed or unwashed PCS, 5% insoluble solids (dry weight), 50 mM sodium acetate pH 5, 1 mM MnS0₄, 50°C, 55°C, or 60°C, 72 hours, sugar analysis by AMINEX® HPX-87H column (Bio-Rad Laboratories, Inc., Hercules, CA, USA).

Cellulosic material: The term "cellulosic material" means any material containing cellulose. The predominant polysaccharide in the primary cell wall of biomass is cellulose, the second most abundant is hemicellulose, and the third is pectin. The secondary cell wall, produced after the cell has stopped growing, also contains polysaccharides and is strengthened by polymeric lignin covalently cross-linked to hemicellulose. Cellulose is a homopolymer of anhydrocellobiose and thus a linear beta-(1 -4)-D-glucan, while hemicelluloses include a variety of compounds, such as xylans, xyloglucans, arabinoxylans, and mannans in complex branched structures with a spectrum of substituents. Although generally polymorphous, cellulose is found in plant tissue primarily as an insoluble crystalline matrix of parallel glucan chains. Hemicelluloses usually hydrogen bond to cellulose, as well as to other hemicelluloses, which help stabilize the cell wall matrix.

Cellulose is generally found, for example, in the stems, leaves, hulls, husks, and cobs of plants or leaves, branches, and wood of trees. The cellulosic material can be, but is not limited to, agricultural residue, herbaceous material (including energy crops), municipal solid waste, pulp and paper mill residue, waste paper, and wood (including forestry residue) (see, for example, Wiselogel ei a/., 1995, in Handbook on Bioethanol (Charles E. Wyman, editor), pp. 105-1 18, Taylor & Francis, Washington D.C.; Wyman, 1994, Bioresource Technology 50: 3-16; Lynd, 1990, Applied Biochemistry and Biotechnology 24/25: 695-719; Mosier ei a/., 1999, Recent Progress in Bioconversion of Lignocellulosics, in Advances in Biochemical Engineering/Biotechnology, T. Scheper, managing editor, Volume 65, pp. 23-40, Springer-Verlag, New York). It is understood herein that the cellulose may be in the form of lignocellulose, a plant cell wall material containing lignin, cellulose, and hemicellulose in a mixed matrix. In one aspect, the cellulosic material is any biomass material. In another aspect, the cellulosic material is lignocellulose, which comprises cellulose, hemicelluloses, and lignin.

In an embodiment, the cellulosic material is agricultural residue, herbaceous material (including energy crops), municipal solid waste, pulp and paper mill residue, waste paper, or wood (including forestry residue).

In another embodiment, the cellulosic material is arundo, bagasse, bamboo, corn cob, corn fiber, corn stover, miscanthus, rice straw, switchgrass, or wheat straw.

In another embodiment, the cellulosic material is aspen, eucalyptus, fir, pine, poplar, spruce, or willow.

In another embodiment, the cellulosic material is algal cellulose, bacterial cellulose, cotton linter, filter paper, microcrystalline cellulose (e.g., AVICEL®), or phosphoric-acid treated cellulose.

In another embodiment, the cellulosic material is an aquatic biomass. As used herein the term "aquatic biomass" means biomass produced in an aquatic environment by a photosynthesis process. The aquatic biomass can be algae, emergent plants, floating-leaf plants, or submerged plants.

The cellulosic material may be used as is or may be subjected to pretreatment, using conventional methods known in the art, as described herein. In a preferred aspect, the cellulosic material is pretreated.

Coding sequence: The term "coding sequence" means a polynucleotide, which directly specifies the amino acid sequence of a polypeptide. The boundaries of the coding sequence are generally determined by an open reading frame, which begins with a start codon such as ATG, GTG, or TTG and ends with a stop codon such as TAA, TAG, or TGA. The coding sequence may be a genomic DNA, cDNA, synthetic DNA, or a combination thereof.

Control sequences: The term "control sequences" means nucleic acid sequences necessary for expression of a polynucleotide encoding a mature polypeptide of the present invention. Each control sequence may be native (i.e., from the same gene) or foreign (i.e., from a different gene) to the polynucleotide encoding the polypeptide or native or foreign to each other. Such control sequences include, but are not limited to, a leader, polyadenylation sequence, propeptide sequence, promoter, signal peptide sequence, and transcription terminator. At a minimum, the control sequences include a promoter, and transcriptional and translational stop signals. The control sequences may be provided with linkers for the purpose of introducing specific restriction sites facilitating ligation of the control sequences with the coding region of the polynucleotide encoding a polypeptide.

Detergent component: the term "detergent component" is defined herein to mean the types of chemicals which can be used in detergent compositions. Examples of detergent components are surfactants, hydrotropes, builders, co-builders, chelators or chelating agents, bleaching system or bleach components, polymers, fabric hueing agents, fabric conditioners, foam boosters, suds suppressors, dispersants, dye transfer inhibitors, fluorescent whitening agents, perfume, optical brighteners, bactericides, fungicides, soil suspending agents, soil release polymers, anti-redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants, and solubilizers. The detergent composition may comprise of one or more of any type of detergent component.

Detergent composition: the term "detergent composition" refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles, dishes, and hard surfaces. The detergent composition may be used to e.g. clean textiles, dishes and hard surfaces for both household cleaning and industrial cleaning. The terms encompass any materials/compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, or spray compositions) and includes, but is not limited to, detergent compositions (e.g., liquid and/or solid laundry detergents and fine fabric detergents; hard surface cleaning formulations, such as for glass, wood, plastic, ceramic and metal counter tops and windows; carpet cleaners; oven cleaners; fabric fresheners; fabric softeners; and textile and laundry pre-spotters, as well as dish wash detergents). In addition to containing a GH5, GH7, or GH45 beta-glucanases, the detergent formulation may contain one or more additional enzymes (such as amylases, proteases, peroxidases, cellulases, betaglucanases, xyloglucanases, hemicellulases, xanthanases, xanthan lyases, lipases, acyl transferases, phospholipases, esterases, laccases, catalases, aryl esterases, amylases, alpha- amylases, glucoamylases, cutinases, pectinases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, carrageenases, pullulanases, tannases, arabinosidases, hyaluronidases, chondroitinases, xyloglucanases, xylanases, pectin acetyl esterases, polygalacturonases, rhamnogalacturonases, other endo-beta-mannanases, exo-beta- mannanases, pectin methylesterases, cellobiohydrolases, transglutaminases, and combinations thereof, or any mixture thereof), and/or components such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.

Dish wash: The term "dish wash" refers to all forms of washing dishes, e.g. by hand dish wash (HDW) or automatic dish wash (ADW). Washing dishes includes, but is not limited to, the cleaning of all forms of crockery such as plates, cups, glasses, bowls, all forms of cutlery such as spoons, knives, forks and serving utensils as well as ceramics, plastics, metals, china, glass and acrylics.

Dish washing composition: The term "dish washing composition" refers to all forms of compositions for cleaning hard surfaces. The present invention is not restricted to any particular type of dish wash composition or any particular detergent.

Expression: The term "expression" includes any step involved in the production of a polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification, and secretion.

Expression vector: The term "expression vector" means a linear or circular DNA molecule that comprises a polynucleotide encoding a polypeptide and is operably linked to control sequences that provide for its expression.

Fragment: The term "fragment" means a polypeptide or a catalytic or carbohydrate binding module having one or more (e.g., several) amino acids absent from the amino and/or carboxyl terminus of a mature polypeptide or domain; wherein the fragment has beta-glucanase or carbohydrate binding activity. In one aspect, a fragment contains at least 340 amino acid residues, or at least 230 amino acid residues, or at least 210 amino acid residues or at least 200 amino acid residues, or at least 180 amino acid residues, wherein the fragment has beta- glucanase activity.

Hard surface cleaning: The term "Hard surface cleaning" is defined herein as cleaning of hard surfaces wherein hard surfaces may include floors, tables, walls, roofs etc. as well as surfaces of hard objects such as cars (car wash) and dishes (dish wash). Dish washing includes but are not limited to cleaning of plates, cups, glasses, bowls, and cutlery such as spoons, knives, forks, serving utensils, ceramics, plastics, metals, china, glass and acrylics.

Hemicellulolytic enzyme or hemicellulase: The term "hemicellulolytic enzyme" or "hemicellulase" means one or more (e.g., several) enzymes that hydrolyze a hemicellulosic material. See, for example, Shallom and Shoham, Current Opinion In Microbiology, 2003, 6(3): 219-228). Hemicellulases are key components in the degradation of plant biomass. Examples of hemicellulases include, but are not limited to, an acetylmannan esterase, an acetylxylan esterase, an arabinanase, an arabinofuranosidase, a coumaric acid esterase, a feruloyl esterase, a galactosidase, a glucuronidase, a glucuronoyl esterase, a mannanase, a mannosidase, a xylanase, and a xylosidase. The substrates for these enzymes, hemicelluloses, are a heterogeneous group of branched and linear polysaccharides that are bound via hydrogen bonds to the cellulose microfibrils in the plant cell wall, crosslinking them into a robust network. Hemicelluloses are also covalently attached to lignin, forming together with cellulose a highly complex structure. The variable structure and organization of hemicelluloses require the concerted action of many enzymes for its complete degradation. The catalytic modules of hemicellulases are either glycoside hydrolases (GHs) that hydrolyze glycosidic bonds, or carbohydrate esterases (CEs), which hydrolyze ester linkages of acetate or ferulic acid side groups. These catalytic modules, based on homology of their primary sequence, can be assigned into GH and CE families. Some families, with an overall similar fold, can be further grouped into clans, marked alphabetically (e.g., GH-A). A most informative and updated classification of these and other carbohydrate active enzymes is available in the Carbohydrate-Active Enzymes (CAZy) database. Hemicellulolytic enzyme activities can be measured according to Ghose and Bisaria, 1987, Pure & Appl. Chem. 59: 1739-1752, at a suitable temperature such as 40°C-80°C, e.g., 50°C, 55°C, 60°C, 65°C, or 70°C, and a suitable pH such as 4-9, e.g., 5.0, 5.5, 6.0, 6.5, or 7.0.

Host cell: The term "host cell" means any cell type that is susceptible to transformation, transfection, transduction, or the like with a nucleic acid construct or expression vector comprising a polynucleotide of the present invention. The term "host cell" encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that occur during replication, as well as a recombinant host cell, an isolated host cell (e.g., an isolated recombinant host cell), an isolated host cell that is not a human embryonic stem cell.

Isolated: The term "isolated" means a substance in a form or environment that does not occur in nature. Non-limiting examples of isolated substances include (1 ) any non-naturally occurring substance, (2) any substance including, but not limited to, any enzyme, variant, nucleic acid, protein, peptide or cofactor, that is at least partially removed from one or more or all of the naturally occurring constituents with which it is associated in nature; (3) any substance modified by the hand of man relative to that substance found in nature; or (4) any substance modified by increasing the amount of the substance relative to other components with which it is naturally associated (e.g., recombinant production in a host cell; multiple copies of a gene encoding the substance; and use of a stronger promoter than the promoter naturally associated with the gene encoding the substance). A fermentation broth produced by culturing a recombinant host cell expressing the polynucleotide of the invention will comprise the polypeptide of the invention in an isolated form.

Laundering: The term "laundering" relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a cleaning or detergent composition of the present invention. The laundering process can for example be carried out using e.g. a household or an industrial washing machine or can be carried out by hand.

Mature polypeptide: The term "mature polypeptide" means a polypeptide in its final form following translation and any post-translational modifications, such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc.

It is known in the art that a host cell may produce a mixture of two of more different mature polypeptides (i.e., with a different C-terminal and/or N-terminal amino acid) expressed by the same polynucleotide. It is also known in the art that different host cells process polypeptides differently, and thus, one host cell expressing a polynucleotide may produce a different mature polypeptide (e.g., having a different C-terminal and/or N-terminal amino acid) as compared to another host cell expressing the same polynucleotide.

Nucleic acid construct: The term "nucleic acid construct" means a nucleic acid molecule, either single- or double-stranded, which is isolated from a naturally occurring gene or is modified to contain segments of nucleic acids in a manner that would not otherwise exist in nature or which is synthetic, which comprises one or more control sequences.

Operably linked: The term "operably linked" means a configuration in which a control sequence is placed at an appropriate position relative to the coding sequence of a polynucleotide such that the control sequence directs expression of the coding sequence.

Sequence identity: The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter "sequence identity". For purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled "longest identity" (obtained using the -nobrief option) is used as the percent identity and is calculated as follows:

(Identical Residues x 100)/(Length of Alignment - Total Number of Gaps in Alignment) For purposes of the present invention, the sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), preferably version 5.0.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. The output of Needle labeled "longest identity" (obtained using the -nobrief option) is used as the percent identity and is calculated as follows:

(Identical Deoxyribonucleotides x 100)/(Length of Alignment - Total Number of Gaps in Alignment)

Subsequence: The term "subsequence" means a polynucleotide having one or more

(e.g., several) nucleotides absent from the 5' and/or 3' end of a mature polypeptide coding sequence; wherein the subsequence encodes a fragment having cellulase activity.

Textile: The term "textile" means any textile material including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material, fabrics made of these materials and products made from fabrics (e.g., garments and other articles). The textile or fabric may be in the form of knits, wovens, denims, non-wovens, felts, yarns, and towelling. The textile may be cellulose based such as natural cellulosics, including cotton, flax/linen, jute, ramie, sisal or coir or manmade cellulosics (e.g. originating from wood pulp) including viscose/rayon, ramie, cellulose acetate fibers (tricell), lyocell or blends thereof. The textile or fabric may also be non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabit and silk or synthetic polymer such as nylon, aramid, polyester, acrylic, polypropylen and spandex/elastane, or blends thereof as well as blend of cellulose based and non-cellulose based fibers. Examples of blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fibers (e.g. polyamide fibers, acrylic fibers, polyester fibers, polyvinyl alcohol fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and cellulose-containing fibers (e.g. rayon/viscose, ramie, flax/linen, jute, cellulose acetate fibers, lyocell). Fabric may be conventional washable laundry, for example stained household laundry. When the term fabric or garment is used, it is intended to include the broader term textiles as well.

Variant: The term "variant" means a polypeptide having alpha-amylase activity comprising an alteration, i.e., a substitution, insertion, and/or deletion of one or more (several) amino acid residues at one or more (several) positions. A substitution means a replacement of an amino acid occupying a position with a different amino acid; a deletion means removal of an amino acid occupying a position; and an insertion means adding 1 -3 amino acids adjacent to an amino acid occupying a position. The variants of the present invention have at least 20%, e.g., at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or at least 100% of the alpha-amylase activity of the polypeptide of sequence selected from the group consisting of: SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 1 1 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ I D NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, and SEQ ID NO: 19.

Wild-type cellulase: The term "wild-type" cellulase means a cellulase expressed by a naturally occurring microorganism, such as a bacterium, yeast, or filamentous fungus found in nature.

Wash performance: The term "wash performance" is defined herein as the ability of an enzyme or a blend of enzymes to remove stains present on an object to be cleaned during e.g. wash or hard surface cleaning relative to the wash performance without one or more on the enzymes present.

DETAILED DESCRIPTION OF THE INVENTION

The present invention provides the use cellulases and at least one amylase for compositions which have a benefit in removing stains and which can be used in cleaning or detergent applications or for processes such as cleaning hard-surfaces, dish wash and laundering. The cellulases show synergistic effect with one or more amylases (e.g. wherein a preferred method for determining the REM synergistic effect is disclosed in the Examples).

In an embodiment, the present invention relates to a composition comprising (i) a polypeptide having cellulase activity, selected from the group consisting of:

(a) a polypeptide having at least 70% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ

ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, and

(b) a fragment of the polypeptide of (a) that has cellulase activity;

and (ii) at least one polypeptide having alpha-amylase activity.

As it can be seen from the Examples, using a cellulase and an alpha-amylase in combination, a synergistic effect can be observed on the stains used in the experiment.

In an embodiment, the present invention relates to compositions comprising polypeptides having cellulase activity and having at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5, and at least one amylase. In one embodiment, the present invention relates to a composition comprising a cellulase having at least 75% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5.

An embodiment of the present invention is a composition (e.g. a cleaning or detergent composition) comprising the cellulase polypeptide and one or more amylases.

In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6.

In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the present invention relates to a composition comprising a cellulase having at least 80% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5.

In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 80% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the present invention relates to a composition comprising a cellulase having at least 85% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5.

In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the present invention relates to a composition comprising a cellulase having at least 90% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ I D NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5.

In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 90% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the present invention relates to a composition comprising a cellulase having at least 95% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ I D NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5.

In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1 . In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 95% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the present invention relates to a composition comprising a cellulase having at least 100% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ I D NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5.

In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ I D NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 1 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 85% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 2 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO:

3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 3 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO:

4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 4 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 6. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 7. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 8. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 9. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 10. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 1 1. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 12. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 13. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 14. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 15. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 16. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 17. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase having at least 100% sequence identity to the polypeptide of SEQ ID NO: 5 and an amylase having at least 75% sequence identity to the polypeptide of SEQ ID NO: 19.

In another embodiment, a polypeptide having cellulase activity and at least one polypeptide having amylase activity has a synergistic effect; preferably said synergistic effect is a REM synergistic effect, further preferably said REM synergistic effect is of more than 4.5 at about 40°C for about 30 minutes, further preferably said REM synergistic effect is of more than 6.2 at about 40°C for about 30 minutes.

In another embodiment a pH optimum of a polypeptide of the present invention is selected in the range from about 6 to about 9. In another embodiment a pH optimum of a polypeptide of the present invention is selected from the group consisting of: 6, 6.5, 7, 7.5, 8, 8.5, 9. In another embodiment a pH optimum of a polypeptide of the present invention is at least 6 (or at least 6.5, or at least 7, or at least 7.5, or at least 8, or at least 8.5, or at least 9). In another embodiment a pH optimum of a polypeptide of the present invention is more than 6 (or more than 6.5, or more than 7, or more than 7.5, or more than 8, or more than 8.5, or more than 9).

In an embodiment, the polypeptide having cellulase activity has been isolated. A polypeptide of the present invention preferably comprises or consists of the amino acid sequence selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, or an allelic variant thereof; or is a fragment thereof having cellulase activity. In another aspect, the polypeptide comprises or consists of the mature polypeptide of sequence selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, or SEQ ID NO: 5. An embodiment of the present invention is a composition (e.g. a cleaning or detergent composition) comprising said cellulase polypeptide and one or more amylases.

In another embodiment, the composition comprising a cellulase as described herein is capable of:

i) having cellulase activity for at least 15 minutes in an aqueous solution with a pH selected in the range from about 7.5 to about 13.5, wherein said aqueous solution optionally comprises a bleaching agent, preferably said pH is selected in the range from about 7.5 to about 12.5, further preferably said pH is selected in the range from about 8.5 to about 1 1.5, most preferably said pH is selected in the range from about 9.5 to about 10.5; and/or

ii) having cellulase activity for at least 15 minutes in an aqueous solution at a temperature selected in the range from about 20°C to about 75°C, wherein said aqueous solution optionally comprises a bleaching agent.

In another embodiment, the composition comprising the cellulase is capable of having cellulase activity in an aqueous solution at a temperature selected in the range from about 20°C to about 75°C, wherein said aqueous solution optionally comprises a bleaching agent, preferably said temperature is selected in the range from about 40°C to about 60°C.

In one embodiment, the composition comprising a cellulase as described herein, also comprises a polypeptide having alpha-amylase activity. Thus, in one embodiment, the polypeptide having alpha-amylase activity is selected from the group consisting of a polypeptide sequence having at least 75% sequence identity to any of the polypeptide sequences selected from the group consisting of: SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 1 1 , SEQ ID NO: 12, SEQ I D NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, and SEQ ID NO: 19.

In one embodiment, the polypeptide comprised in the composition of the present invention, has cellulose activity is beta-1 ,4-glucanase EC 3.2.1.4 activity.

In one embodiment, the polypeptide having alpha-amylase activity comprised in the composition of the present invention, is alpha-1 ,4-glucan-4-glucanohydrolase E.C. 3.2.1 .1 activity.

In a further embodiment, the composition further comprises (i) one or more detergent components; and/or (ii) one or more additional enzymes.

In one embodiment, the composition has a pH of 7.5 or above and optionally comprises a bleaching agent; preferably said pH is in the range from about 7.5 to about 13.5, further preferably said pH is in the range from about 7.5 to about 12.5, most preferably said pH is in the range from about 8.5 to about 1 1 .5, further most preferably said pH is in the range from about 9.5 to about 10.5.

In one embodiment, the composition is a cleaning or a detergent composition, wherein said cleaning or a detergent composition is a dish wash composition or a laundry composition.

In another embodiment, the composition comprising a cellulase polypeptide and one or more amylases, the alpha-amylase is selected from the group consisting of:

(a) a polypeptide having at least 75% sequence identity to SEQ ID NO: 6, optionally, wherein the polypeptide comprises a modification in one or more of positions: 9, 15, 23, 105, 106, 1 18, 124, 128, 133, 149, 154, 156, 178, 179, 181 , 182, 183, 184, 186, 188, 190, 195, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 246, 257, 264, 295, 299, 304, 305, 320, 323, 339, 391 , 408, 444, 445, and/or 458;

(b) a polypeptide having at least 75% sequence identity to SEQ ID NO: 7, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 7, 109, 140, 181 , 182, 183, 184, 195, 206, 243, 260, 280, 304, 391 and/or 476,

(c) a polypeptide having at least 75% sequence identity to SEQ ID NO: 8, optionally, wherein the polypeptide comprises a modification in one or more of positions: 180, 181 , 182, 183, 243, and/or 475;

(d) a polypeptide having at least 75% sequence identity to SEQ ID NO: 9, optionally, wherein the polypeptide comprises a modification in one or more of positions: 126,

153, 178, 179, 180, 181 , 187, 203, 458, 459, 460, and/or 476;

(e) a polypeptide having at least 75% sequence identity to SEQ ID NO: 10, optionally, wherein the polypeptide comprises a modification in position 202;

(f) a polypeptide having at least 75% sequence identity to SEQ ID NO: 1 1 , optionally, wherein the polypeptide comprises a modification in one or more of positions: 181 , 182, 183, 184, 405, 421 , 422, and/or 428;

(g) a polypeptide having at least 75% sequence identity to SEQ ID NO: 12;

(h) a polypeptide having at least 75% sequence identity to SEQ ID NO: 13, optionally, wherein the polypeptide comprises a modification in one or more of positions: 48, 49, 107, 156, 181 , 190, 197, 201 , 209, and/or 264;

(i) a polypeptide having at least 75% sequence identity to SEQ ID NO: 14 or SEQ ID NO: 19, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 54, 56, 72, 109, 1 13, 1 16, 134, 140, 159, 167, 169, 172, 173, 174, 181 , 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391 , 395, 439, 469, 444, 473, 476, and/or 477;

(j) a polypeptide having at least 75% sequence identity to SEQ ID NO: 15 or SEQ ID NO: 16;

(k) a polypeptide having at least 75% sequence identity to SEQ ID NO: 17, optionally, wherein the polypeptide comprises a modification in one or more of positions: 59, 89, 129, 177, 179, 181 , 182, 183, 184, 193, 208, 220, 224, 254, and/or 284; and

(I) a polypeptide having at least 75% sequence identity to SEQ ID NO: 18.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 6, optionally, wherein the polypeptide comprises a modification in one or more of positions: 9, 15, 23, 105, 106, 1 18, 124, 128, 133, 149, 154, 156, 178, 179, 181 , 182, 183, 184, 186, 188, 190, 195, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 246, 257, 264, 295, 299, 304, 305, 320, 323, 339, 391 , 408, 444, 445, and/or 458.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 7, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 7, 109, 140, 181 , 182, 183, 184, 195, 206, 243, 260, 280, 304, 391 and/or 476.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 8, optionally, wherein the polypeptide comprises a modification in one or more of positions: 180, 181 , 182, 183, 243, and/or 475.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 9, optionally, wherein the polypeptide comprises a modification in one or more of positions: 126, 153, 178, 179, 180, 181 , 187, 203, 458, 459, 460, and/or 476. In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 10, optionally, wherein the polypeptide comprises a modification in position 202.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 1 1 , optionally, wherein the polypeptide comprises a modification in one or more of positions: 181 , 182, 183, 184, 405, 421 , 422, and/or 428.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 12.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 13, optionally, wherein the polypeptide comprises a modification in one or more of positions: 48, 49, 107, 156, 181 , 190, 197, 201 , 209, and/or 264.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 14 or SEQ ID NO: 19, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 54, 56, 72, 109, 1 13, 1 16, 134, 140, 159, 167, 169, 172, 173, 174, 181 , 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391 , 395, 439, 469, 444, 473, 476, and/or 477.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 15 or SEQ ID NO: 16.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 17, optionally, wherein the polypeptide comprises a modification in one or more of positions: 59, 89, 129, 177, 179, 181 , 182, 183, 184, 193, 208, 220, 224, 254, and/or 284.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 1 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 18.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 6, optionally, wherein the polypeptide comprises a modification in one or more of positions: 9, 15, 23, 105, 106, 1 18, 124, 128, 133, 149, 154, 156, 178, 179, 181 , 182, 183, 184, 186, 188, 190, 195, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 246, 257, 264, 295, 299, 304, 305, 320, 323, 339, 391 , 408, 444, 445, and/or 458.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 7, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 7, 109, 140, 181 , 182, 183, 184, 195, 206, 243, 260, 280, 304, 391 and/or 476.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 8, optionally, wherein the polypeptide comprises a modification in one or more of positions: 180, 181 , 182, 183, 243, and/or 475.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 9, optionally, wherein the polypeptide comprises a modification in one or more of positions: 126, 153, 178, 179,

180, 181 , 187, 203, 458, 459, 460, and/or 476.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 10, optionally, wherein the polypeptide comprises a modification in position 202.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 1 1 , optionally, wherein the polypeptide comprises a modification in one or more of positions: 181 , 182, 183, 184, 405, 421 , 422, and/or 428.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 12.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 13, optionally, wherein the polypeptide comprises a modification in one or more of positions: 48, 49, 107, 156,

181 , 190, 197, 201 , 209, and/or 264.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 14 or SEQ ID NO: 19, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 54, 56, 72, 109, 1 13, 1 16, 134, 140, 159, 167, 169, 172, 173, 174, 181 , 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391 , 395, 439, 469, 444, 473, 476, and/or 477.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 15 or SEQ ID NO: 16.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 17, optionally, wherein the polypeptide comprises a modification in one or more of positions: 59, 89, 129, 177, 179, 181 , 182, 183, 184, 193, 208, 220, 224, 254, and/or 284.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 2 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 18. In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 6, optionally, wherein the polypeptide comprises a modification in one or more of positions: 9, 15, 23, 105, 106, 1 18, 124, 128, 133, 149, 154, 156, 178, 179, 181 , 182, 183, 184, 186, 188, 190, 195, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 246, 257, 264, 295, 299, 304, 305, 320, 323, 339, 391 , 408, 444, 445, and/or 458.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 7, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 7, 109, 140, 181 , 182, 183, 184, 195, 206, 243, 260, 280, 304, 391 and/or 476.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 8, optionally, wherein the polypeptide comprises a modification in one or more of positions: 180, 181 , 182, 183, 243, and/or 475.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 9, optionally, wherein the polypeptide comprises a modification in one or more of positions: 126, 153, 178, 179,

180, 181 , 187, 203, 458, 459, 460, and/or 476.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 10, optionally, wherein the polypeptide comprises a modification in position 202.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 1 1 , optionally, wherein the polypeptide comprises a modification in one or more of positions: 181 , 182, 183, 184, 405, 421 , 422, and/or 428.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 12.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 13, optionally, wherein the polypeptide comprises a modification in one or more of positions: 48, 49, 107, 156,

181 , 190, 197, 201 , 209, and/or 264.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 14 or SEQ ID NO: 19, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 54, 56, 72, 109, 1 13, 1 16, 134, 140, 159, 167, 169, 172, 173, 174, 181 , 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391 , 395, 439, 469, 444, 473, 476, and/or 477. In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 15 or SEQ ID NO: 16.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 17, optionally, wherein the polypeptide comprises a modification in one or more of positions: 59, 89, 129, 177,

179, 181 , 182, 183, 184, 193, 208, 220, 224, 254, and/or 284.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 3 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 18.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 6, optionally, wherein the polypeptide comprises a modification in one or more of positions: 9, 15, 23, 105, 106, 1 18, 124, 128, 133, 149, 154, 156, 178, 179, 181 , 182, 183, 184, 186, 188, 190, 195, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 246, 257, 264, 295, 299, 304, 305, 320, 323, 339, 391 , 408, 444, 445, and/or 458.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 7, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 7, 109, 140, 181 , 182, 183, 184, 195, 206, 243, 260, 280, 304, 391 and/or 476.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 8, optionally, wherein the polypeptide comprises a modification in one or more of positions: 180, 181 , 182, 183, 243, and/or 475.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 9, optionally, wherein the polypeptide comprises a modification in one or more of positions: 126, 153, 178, 179,

180, 181 , 187, 203, 458, 459, 460, and/or 476.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 10, optionally, wherein the polypeptide comprises a modification in position 202.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 1 1 , optionally, wherein the polypeptide comprises a modification in one or more of positions: 181 , 182, 183, 184, 405, 421 , 422, and/or 428.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 12.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 13, optionally, wherein the polypeptide comprises a modification in one or more of positions: 48, 49, 107, 156,

181 , 190, 197, 201 , 209, and/or 264.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 14 or SEQ ID NO: 19, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 54, 56, 72, 109, 1 13, 1 16, 134, 140, 159, 167, 169, 172, 173, 174, 181 , 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391 , 395, 439, 469, 444, 473, 476, and/or 477.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 15 or SEQ ID NO: 16.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 17, optionally, wherein the polypeptide comprises a modification in one or more of positions: 59, 89, 129, 177,

179, 181 , 182, 183, 184, 193, 208, 220, 224, 254, and/or 284.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 4 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 18.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 6, optionally, wherein the polypeptide comprises a modification in one or more of positions: 9, 15, 23, 105, 106, 1 18, 124, 128, 133, 149, 154, 156, 178, 179, 181 , 182, 183, 184, 186, 188, 190, 195, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 246, 257, 264, 295, 299, 304, 305, 320, 323, 339, 391 , 408, 444, 445, and/or 458.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 7, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 7, 109, 140, 181 ,

182, 183, 184, 195, 206, 243, 260, 280, 304, 391 and/or 476.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 8, optionally, wherein the polypeptide comprises a modification in one or more of positions: 180, 181 , 182, 183, 243, and/or 475.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 9, optionally, wherein the polypeptide comprises a modification in one or more of positions: 126, 153, 178, 179,

180, 181 , 187, 203, 458, 459, 460, and/or 476.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 10, optionally, wherein the polypeptide comprises a modification in position 202.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 1 1 , optionally, wherein the polypeptide comprises a modification in one or more of positions: 181 , 182, 183, 184, 405, 421 , 422, and/or 428.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 12.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 13, optionally, wherein the polypeptide comprises a modification in one or more of positions: 48, 49, 107, 156, 181 , 190, 197, 201 , 209, and/or 264.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 14 or SEQ ID NO: 19, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 54, 56, 72, 109, 1 13, 1 16, 134, 140, 159, 167, 169, 172, 173, 174, 181 , 182, 183, 184, 189, 194, 195, 206, 255, 260, 262, 265, 284, 289, 304, 305, 347, 391 , 395, 439, 469, 444, 473, 476, and/or 477.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 15 or SEQ ID NO: 16.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 17, optionally, wherein the polypeptide comprises a modification in one or more of positions: 59, 89, 129, 177, 179, 181 , 182, 183, 184, 193, 208, 220, 224, 254, and/or 284.

In one embodiment, the composition comprises a cellulase polypeptide of SEQ ID NO: 5 and an amylase polypeptide having at least 75% sequence identity to SEQ ID NO: 18.

In one embodiment, the composition further comprises a protease, preferably, wherein the protease is a polypeptide having at least 60% sequence identity to SEQ ID NO: 20.

In another embodiment, the present invention relates to alpha-amylase variants of the polypeptide of sequence selected from the group consisting of: SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 1 1 , SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 17, and SEQ ID NO: 19 comprising a substitution, deletion, and/or insertion at one or more (e.g., several) positions. In an embodiment, the number of amino acid substitutions, deletions and/or insertions introduced into the mature polypeptide of sequence selected from the group consisting of: SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 1 1 , SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 17, and SEQ I D NO: 19 is up to 10, e.g., 1 , 2, 3, 4, 5, 6, 7, 8, 9, or 10. The amino acid changes may be of a minor nature, that is conservative amino acid substitutions or insertions that do not significantly affect the folding and/or activity of the protein; small deletions, typically of 1 - 30 amino acids; small amino- or carboxyl-terminal extensions, such as an amino-terminal methionine residue; a small linker peptide of up to 20-25 residues; or a small extension that facilitates purification by changing net charge or another function, such as a poly-histidine tract, an antigenic epitope or a binding domain.

Examples of conservative substitutions are within the groups of basic amino acids (arginine, lysine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine), and small amino acids (glycine, alanine, serine, threonine and methionine). Amino acid substitutions that do not generally alter specific activity are known in the art and are described, for example, by H. Neurath and R.L. Hill, 1979, In, The Proteins, Academic Press, New York. Common substitutions are Ala/Ser, Val/lle, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/lle, LeuA al, Ala/Glu, and Asp/Gly.

Alternatively, the amino acid changes are of such a nature that the physico-chemical properties of the polypeptides are altered. For example, amino acid changes may improve the thermal stability of the polypeptide, alter the substrate specificity, change the pH optimum, and the like.

Essential amino acids in a polypeptide can be identified accordingly to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham and Wells, 1989, Science 244: 1081 -1085). In the latter technique, single alanine mutations are introduced at every residue in the molecule, and the resultant molecules are tested for beta- glucanase activity to identify amino acid residues that are critical to the activity of the molecule. See also, Hilton et al., 1996, J. Biol. Chem. 271 : 4699-4708. The active site of the enzyme or other biological interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, in conjunction with mutation of putative contact site amino acids. See, for example, de Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224: 899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. The identity of essential amino acids can also be inferred from an alignment with a related polypeptide.

Single or multiple amino acid substitutions, deletions, and/or insertions can be made and tested using known methods of mutagenesis, recombination, and/or shuffling, followed by a relevant screening procedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241 : 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95/17413; or WO 95/22625. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991 , Biochemistry 30: 10832-10837; U.S. Patent No. 5,223,409; WO 92/06204), and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Ner ei a/., 1988, DNA 7: 127).

Mutagenesis/shuffling methods can be combined with high-throughput, automated screening methods to detect activity of cloned, mutagenized polypeptides expressed by host cells (Ness et al., 1999, Nature Biotechnology 17: 893-896). Mutagenized DNA molecules that encode active polypeptides can be recovered from the host cells and rapidly sequenced using standard methods in the art. These methods allow the rapid determination of the importance of individual amino acid residues in a polypeptide.

The polypeptide may be a hybrid polypeptide in which a region of one polypeptide is fused at the N-terminus or the C-terminus of a region of another polypeptide.

The polypeptide may be a fusion polypeptide or cleavable fusion polypeptide in which another polypeptide is fused at the N-terminus or the C-terminus of the polypeptide of the present invention. A fusion polypeptide is produced by fusing a polynucleotide encoding another polypeptide to a polynucleotide of the present invention. Techniques for producing fusion polypeptides are known in the art, and include ligating the coding sequences encoding the polypeptides so that they are in frame and that expression of the fusion polypeptide is under control of the same promoter(s) and terminator. Fusion polypeptides may also be constructed using intein technology in which fusion polypeptides are created post-translationally (Cooper et al., 1993, EMBO J. 12: 2575-2583; Dawson et al., 1994, Science 266: 776-779).

A fusion polypeptide can further comprise a cleavage site between the two polypeptides.

Upon secretion of the fusion protein, the site is cleaved releasing the two polypeptides. Examples of cleavage sites include, but are not limited to, the sites disclosed in Martin et al., 2003, J. Ind. Microbiol. Biotechnol. 3: 568-576; Svetina et al., 2000, J. Biotechnol. 76: 245-251 ; Rasmussen- Wilson et al., 1997, Appl. Environ. Microbiol. 63: 3488-3493; Ward et al., 1995, Biotechnology 13: 498-503; and Contreras et al., 1991 , Biotechnology 9: 378-381 ; Eaton et al., 1986, Biochemistry 25: 505-512; Collins-Racie et al., 1995, Biotechnology 13: 982-987; Carter et al., 1989, Proteins: Structure, Function, and Genetics 6: 240-248; and Stevens, 2003, Drug Discovery World 4: 35- 48.

Preferably, the compositions of the present invention are enriched in such a polypeptide. The term "enriched" indicates that the cellulase activity of the composition has been increased, e.g., with an enrichment factor of at least 1 .1 .

In one embodiment, the polypeptides comprised in the composition of the present invention, has improved stability and/or wash performance under alkaline conditions, preferably the alkaline conditions have pH 7.5 or above.

The compositions may comprise a polypeptide of the present invention as the major enzymatic component, e.g., a mono-component composition. Alternatively, the compositions may comprise multiple enzymatic activities, such as one or more (e.g., several) enzymes selected from the group consisting of hydrolase, isomerase, ligase, lyase, oxidoreductase, or transferase, e.g., an alpha-galactosidase, alpha-glucosidase, aminopeptidase, amylase, beta-galactosidase, beta- glucosidase, beta-xylosidase, carbohydrase, carboxypeptidase, catalase, cellobiohydrolase, cellulase, chitinase, cutinase, cyclodextrin glycosyltransferase, deoxyribonuclease, endoglucanase, esterase, glucoamylase, invertase, laccase, lipase, mannosidase, mutanase, oxidase, pectinolytic enzyme, peroxidase, phytase, polyphenoloxidase, proteolytic enzyme, ribonuclease, transglutaminase, or xylanase. An embodiment is a cleaning or detergent composition comprising a beta-glucanase polypeptide of the invention and one or more amylases.

The compositions 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 compositions may be stabilized in accordanwith methods known in the art. An embodiment is a cleaning or detergent composition comprising a beta-glucanase polypeptide of the invention and one or more amylases.

Examples are given below of preferred uses of the compositions of the present invention. The dosage of the composition and other conditions under which the composition is used may be determined on the basis of methods known in the art.

Uses

The compositions of the invention may be used in applications where cellulose containing material needs to be degraded (e.g. under alkaline conditions). An embodiment is a cleaning or detergent composition comprising a cellulase polypeptide and one or more amylases. Examples of where cellulases could be used include detergent applications, paper and pulp productions. In one aspect, compositions of the invention may be used for washing or cleaning a textile and/or a hard surface such as dish wash including Automatic Dish Wash (ADW), Hand Dish Wash (HDW), and/or in a cleaning process such as laundry or hard surface cleaning including dish wash including Automatic Dish Wash (ADW) and industrial cleaning, and/or for laundering and/or hard surface cleaning including dish wash including Automatic Dish Wash (ADW), and/or for at least one of the following: and/or for anti-redeposition.

In one embodiment, the present invention relates to compositions in particular to cleaning compositions and/or detergent compositions comprising a polypeptide having cellulase activity, at least one polypeptide having alpha-amylase activity, and a suitable surfactant.

In one embodiment, the detergent composition may be adapted for specific uses such as laundry, in particular household laundry, dish washing or hard surface cleaning.

In another embodiment a composition of the present invention is a cleaning or a detergent composition.

Alkaline Liquid detergents having high pH are widely used in cleaning, such as laundry and dish wash cleaning. Liquid detergents with elevated pH are especially commonly used by consumers in North America. The high pH cleaning compositions are also used in industrial cleaning processes. Alkaline detergents include liquids having detergent properties. The pH of such detergents usually ranges in pH from 9 to 12.5. The high pH detergents typically comprise components such as surfactants, builders and bleach components and additionally they may also contain a significant amount of water and alkalis such as NaOH, TSP (Trisodium phosphate), ammonia, Sodium carbonate, Potassium hydroxide (KOH) these alkalis are usually added in amount corresponding to 0.1 to 30 percent weight (wt). Adding enzymes to detergents is highly advantageous as the specific activities of these enzymes effectively removes specific stains from surfaces such as textile and cutlery. However, the difficulty of maintaining acceptable enzyme stability in the high pH liquid detergents has for many years prohibited inclusion of enzymes into these detergents. In another embodiment the present invention relates high pH liquid cleaning compositions comprising an alkaline stable beta-glucanase of the present invention suitable for use in such compositions.

In another embodiment a composition of the present invention preferably contains alkaline buffer system to provide a pH of at least about 7.5, at least about 8, at least about 9, preferably pH 10 or above. Preferably the pH is from about 9 to about 13. In order to achieve the high pH it is necessary to have present an alkali metal hydroxide especially sodium or potassium hydroxide, normally in an amount of 0.1 to about 30% by weight (percentage by weight, abbreviated wt%) of the composition, and preferably 1 .0 to 2.5%, or higher amounts of a suitable alkali metal silicate such as metal silicate, according to the desired pH for the product.

In another embodiment a composition of the present invention has pH of 7.5 or above and optionally comprises a bleaching agent; preferably said pH is selected in the range from about 7.5 to about 13.5, further preferably said pH is selected in the range from about 7.5 to about 12.5, most preferably said pH is selected in the range from about 8.5 to about 1 1.5, further most preferably said pH is selected in the range from about 9.5 to about 10.5.

In another embodiment the present invention relates to a liquid cleaning composition having pH 7.5 or above, comprising at least 0.01 wt % cellulase, wherein said cellulase has an amino acid sequence which has at least 75% sequence identity to the polypeptide of the sequence selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5. In further related embodiments cellulases has an amino acid sequence which has at least 80% (or at least 81 %, 82%, 83%, or 84%, or 85%, or 86%, or 87%, or 88%, or 89%, or 90%, or 91 %, or 92%, or 93%, or 94%, or 95%, or 96%, or 97%, or 98% or 99% or 100%) sequence identity to the polypeptide of the sequence selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5.

The detergent compositions of the invention may be formulated, for example, as a hand or machine laundry detergent composition including a laundry additive composition suitable for pre-treatment of stained fabrics and a rinse added fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing operations. The detergent compositions of the invention may find use in hard surface cleaning, automatic dishwashing applications, as well as cosmetic applications such as dentures, teeth, hair and skin.

The detergent composition of the invention may be in any convenient form, e.g., a bar, a tablet, a powder, a granule, a paste or a liquid. A liquid detergent may be aqueous, typically containing up to 70% water and 0-30% organic solvent, or non-aqueous.

Unless otherwise noted, all component or composition levels provided herein are made in reference to the active level of that component or composition, and are exclusive of impurities, for example, residual solvents or by-products, which may be present in commercially available sources.

The enzymes (e.g. cellulases and alpha-amylases) is normally incorporated in the detergent composition at a level of from 0.000001 % to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.00001 % to 1 % of enzyme protein by weight of the composition, more preferably at a level of from 0.0001 % to 0.75% of enzyme protein by weight of the composition, even more preferably at a level of from 0.001 % to 0.5% of enzyme protein by weight of the composition.

Furthermore, the enzymes are normally incorporated in the detergent composition in such amounts that their concentration in the wash water is at a level of from 0.0000001 % to 1 % enzyme protein, preferably at a level of from 0.000005% to 0.01 % of enzyme protein, more preferably at a level of from 0.000001 % to 0.005% of enzyme protein, even more preferably at a level of from 0.00001 % to 0.001 % of enzyme protein in wash water.

As is well known, the amount of enzyme will also vary according to the particular application and/or as a result of the other components included in the compositions.

A composition for use in automatic dishwash (ADW), for example, may include 0.001 %- 50%, such as 0.01 %-25%, such as 0.02%-20%, such as 0.1 -15% of enzyme protein by weight of the composition.

A composition for use in laundry granulation, for example, may include 0.0001 %-50%, such as 0.001 %-20%, such as 0.01 %-15%, such as 0.05%-10% of enzyme protein by weight of the composition.

A composition for use in laundry liquid, for example, may include 0.0001 %-10%, such as

0.001 -7%, such as 0.1 %-5% of enzyme protein by weight of the composition.

In some preferred embodiments, the detergent compositions provided herein are typically formulated such that, during use in aqueous cleaning operations, the wash water has a pH of from about 5.0 to about 13.5, or in alternative embodiments, even from about 6.0 to about 10.5, such as from about 5 to about 1 1 , from about 5 to about 10, from about 5 to about 9, from about 5 to about 8, from about 5 to about 7, from about 6 to about 1 1 , from about 6 to about 10, from about 6 to about 9, from about 6 to about 8, from about 6 to about 7, from about 7 to about 1 1 , from about 7 to about 10, from about 7 to about 9, or from about 7 to about 8. Preferably, the detergent compositions provided herein are typically formulated such that, during use in aqueous cleaning operations, the wash water has a pH selected in the range from about 7.5 to about 13.5, further preferably said pH is selected in the range from about 8.5 to about 1 1.5, most preferably said pH is selected in the range from about 9.5 to about 10.5; further most preferably pH 7.5 or above.

In some preferred embodiments, granular or liquid laundry products are formulated such that the wash water has a pH from about 5.5 to about 8. In other preferred embodiments, granular or liquid laundry products are formulated such that the wash water has a pH selected in the range from about 7.5 to about 13.5, further preferably said pH is selected in the range from about 8.5 to about 1 1 .5, most preferably said pH is selected in the range from about 9.5 to about 10.5; further most preferably pH 7.5 or above. Techniques for controlling pH at recommended usage levels include the use of buffers, alkalis, acids, etc., and are well known to those skilled in the art. An embodiment is a cleaning or detergent composition comprising a beta-glucanase polypeptide of the invention and one or more amylases.

Enzyme components weights are based on total protein. All percentages and ratios are calculated by weight unless otherwise indicated. All percentages and ratios are calculated based on the total composition unless otherwise indicated. In the exemplified detergent composition, the enzymes levels are expressed by pure enzyme by weight of the total composition and unless otherwise specified, the detergent ingredients are expressed by weight of the total composition.

The enzymes of the present invention also find use in detergent additive products. A detergent additive product comprising a cellulase and alpha-amylase is suited for inclusion in a wash process when, e.g., temperature is low, such as at temperatures about 40°C or below, the pH is between 6 and 8 and the washing time short, e.g., below 30 min. A detergent additive product comprising a beta-glucanase of the invention is further ideally suited for inclusion in an alkaline wash process when, e.g., a pH selected in the range from about 7.5 to about 13.5, a temperature selected in the range from about 20°C to about 75°C, and the washing time short, e.g., below 30 min, e.g. at least 15 minutes. An embodiment is a cleaning or detergent composition comprising a beta-glucanase polypeptide of the invention and one or more amylases.

The single dosage may comprise a pill, tablet, gelcap or other single dosage unit including powders and/or liquids. In some embodiments, filler and/or carrier material(s) are included, suitable filler or carrier materials include, but are not limited to, various salts of sulfate, carbonate and silicate as well as talc, clay and the like. In some embodiments filler and/or carrier materials for liquid compositions include water and/or low molecular weight primary and secondary alcohols including polyols and diols. Examples of such alcohols include, but are not limited to, methanol, ethanol, propanol and isopropanol.

In one particularly preferred embodiment the composition according to the invention is employed in a granular composition or liquid, the enzymes may be in form of an encapsulated particle. In one embodiment, the encapsulating material is selected from the group consisting of carbohydrates, natural or synthetic gums, chitin and chitosan, cellulose and cellulose derivatives, silicates, phosphates, borates, polyvinyl alcohol, polyethylene glycol, paraffin waxes and combinations thereof.

The compositions according to the invention typically comprise one or more detergent ingredients. The term detergent compositions include articles and cleaning and treatment compositions. The term cleaning composition includes, unless otherwise indicated, tablet, granular or powder- form all-purpose or "heavy-duty" washing agents, especially laundry detergents; liquid, gel or paste-form all-purpose washing agents, especially the so-called heavy- duty liquid types; liquid fine-fabric detergents; hand dishwashing agents or light duty dishwashing agents, especially those of the high-foaming type; machine dishwashing agents, including the various tablet, granular, liquid and rinse-aid types for household and institutional use. The composition can also be in unit dose packages, including those known in the art and those that are water soluble, water insoluble and/or water permeable.

In embodiments in which cleaning and/or detergent components may not be compatible with the cellulases and/or alpha-amylases, suitable methods may be used for keeping the cleaning and/or detergent components and the enzymes separated (i.e., not in contact with each other) until combination of the two components is appropriate. Such separation methods include any suitable method known in the art (e.g., gelcaps, encapsulation, tablets, and physical separation e.g., by use of a water dissolvable pouch having one or more compartments).

The composition of the present invention may employed as a component of a detergent composition (e.g., a laundry washing detergent composition, or a dishwashing detergent composition), it may, for example, be included in the detergent composition in the form of a non- dusting granulate, a stabilized liquid, or a protected enzyme. Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 and 4,661 ,452 (both to Novo Industri A S) and may optionally be coated by methods known in the art. Examples of waxy coating materials are polyethyleneglycol (PEG) products with mean molecular weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids. Examples of film- forming coating materials suitable for application by fluid bed techniques are given in GB 1483591 .

In some embodiments, the enzymes employed herein are stabilized by the presence of water-soluble sources of zinc (II), calcium (II) and/or magnesium (II) ions in the finished compositions that provide such ions to the enzymes, as well as other metal ions (e.g., barium (II), scandium (II), iron (II), manganese (II), aluminum (III), tin (II), cobalt (II), copper (II), nickel (II), and oxovanadium (IV)). The enzymes of the detergent compositions of the invention may also be stabilized using conventional stabilizing agents such as polyol, e.g., propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, and the composition may be formulated as described in, e.g., WO 92/19709 and WO 92/19708. The enzymes of the invention may also be stabilized by adding reversible enzyme inhibitors, e.g., of the protein type (as described in EP 544 777) or the boronic acid type. Other enzyme stabilizers are well known in the art, such as peptide aldehydes and protein hydrolysate, e.g. the beta-glucanase according to the invention may be stabilized using peptide aldehydes or ketones such as described in WO2005/105826 and WO2009/1 18375.

Protected enzymes for inclusion in a detergent composition of the invention may be prepared, as mentioned above, according to the method disclosed in EP 238 216.

These agents may include, but are not limited to, dispersants, surfactants, detergents, other enzymes, anti-microbials, and biocides.

The compositions of the invention may be applied in dosing elements to be used in an auto-dosing device. The dosing elements comprising the composition of the present invention can be placed into a delivery cartridge as that described in WO 2007/052004 and WO 2007/0833141 . The dosing elements can have an elongated shape and set into an array forming a delivery cartridge which is the refill for an auto-dosing dispensing device as described in case WO 2007/051989. The delivery cartridge is to be placed in an auto-dosing delivery device, such as that described in WO 2008/053191.

Suitable disclosure of auto-dosing devices can be found in WO 2007/083139, WO

2007/051989, WO 2007/083141 , WO 2007/083142 and EP2361964,

Other enzymes

In one embodiment, the composition according to the invention comprises more than the cellulase and alpha-amylase, and thus, may be combined with one or more additional enzymes, such as at least two enzymes, more preferred at least three, four or five enzymes. Preferably, the enzymes have different substrate specificity, e.g., proteolytic activity, amylolytic activity, lipolytic activity, hemicellulytic activity or pectolytic activity. An embodiment is a cleaning or detergent composition comprising a beta-glucanase polypeptide of the invention and one or more amylases.

The detergent additive as well as the detergent composition may comprise one or more enzymes such as a protease, lipase, cutinase, an amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase and/or peroxidase.

In general, the properties of the selected enzyme(s) should be compatible with the selected detergent, (i.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.

Proteases: Suitable proteases include those of bacterial, fungal, plant, viral or animal origin e.g. microbial or vegetable origin. Microbial origin is preferred. Chemically modified or protein engineered variants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as subtilisin. A metalloproteases protease may for example be a thermolysin from e.g. family M4 or other metalloprotease such as those from M5, M7 or M8 families.

The term "subtilases" refers to a sub-group of serine protease according to Siezen et al.,

Protein Engng. 4 (1991 ) 719-737 and Siezen et al. Protein Science 6 (1997) 501 -523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate. The subtilases may be divided into 6 sub-divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.

Examples of subtilases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and WO09/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO89/06279 and protease PD138 described in (WO93/18140). Other useful proteases may be those described in W092/175177, WO01/016285, WO02/026024 and WO02/016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO89/06270, W094/25583 and WO05/040372, and the chymotrypsin proteases derived from Cellulomonas described in WO05/052161 and WO05/052146.

A further preferred protease is the alkaline protease from Bacillus lentus DSM 5483, as described for example in W095/23221 , and variants thereof which are described in W092/21760, W095/23221 , EP1921 147 and EP1921 148.

Examples of metalloproteases are the neutral metalloprotease as described in WO07/044993 (Genencor Int.) such as those derived from Bacillus amyloliquefaciens.

Examples of useful proteases are the variants described in: W092/19729, WO96/034946,

WO98/201 15, WO98/201 16, WO99/01 1768, WO01/44452, WO03/006602, WO04/03186, WO04/041979, WO07/006305, W01 1/036263, W01 1/036264, especially the variants with substitutions in one or more of the following positions: 3, 4, 9, 15, 27, 36, 57, 68, 76, 87, 95, 96, 97, 98, 99, 100, 101 , 102, 103, 104, 106, 1 18, 120, 123, 128, 129, 130, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and 274 using the BPN' numbering. More preferred the protease variants may comprise the mutations: S3T, V4I, S9R, A15T, K27R, ^*36D, V68A, N76D, N87S,R, ^*97E, A98S, S99G,D,A, S99AD, S101 G,M,R S103A, V104I,Y,N, S106A, G1 18V,R, H120D,N, N123S, S128L, P129Q, S130A, G160D, Y167A, R170S, A194P, G195E, V199M, V205I, L217D, N218D, M222S, A232V, K235L, Q236H, Q245R, N252K, T274A (using BPN' numbering).

Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, DuralaseTM, DurazymTM, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Neutrase®, Everlase® and Esperase® (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect Prime®, PreferenzTM, Purafect MA®, Purafect Ox®, Purafect OxP®, Puramax®, Properase®, EffectenzTM, FN2®, FN3® , FN4®, Excellase®, Opticlean® and Optimase® (Danisco/DuPont), AxapemTM (Gist-Brocases N.V.), BLAP (sequence shown in Figure 29 of US5352604) and variants hereof (Henkel AG) and KAP (Bacillus alkalophilus subtilisin) from Kao.

Lipases: Suitable lipases include those of animal, vegetable or microbial origin. Particularly suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered variants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces), e.g., from H. lanuginosa (T. lanuginosus) as described in EP 258 068 and EP 305 216 or from H. insolens as described in WO 96/13580, a Pseudomonas lipase, e.g., from P. alcaligenes or P. pseudoalcaligenes (EP 218 272), P. cepacia (EP 331 376), P. stutzeri (GB 1 ,372,034), P. fluorescens, Pseudomonas sp. strain SD 705 (WO 95/06720 and WO 96/27002), P. wisconsinensis (WO 96/12012), a Bacillus lipase, e.g., from B. subtilis (Dartois et al., 1993, Biochemica et Biophysica Acta, 1 131 : 253-360), B. stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422).

Other examples are lipase variants such as those described in WO 92/05249, WO 94/01541 , EP 407 225, EP 260 105, WO 95/35381 , WO 96/00292, WO 95/30744, WO 94/25578, WO 95/14783, WO 95/22615, WO 97/04079 and WO 97/07202.

Preferred commercially available lipase enzymes include LipolaseTM, Lipolase UltraTM, and Lipex™ (Novozymes A/S).

Amylases: Suitable amylases may be an alpha-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein engineered variants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1 ,296,839. Suitable amylases include amylases having SEQ ID NO: 3 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 264, 304, 305, 391 , 408, and 444. Different 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 having a deletion in positions 181 and 182 and a substitution in position 193. Other amylases which are suitable are hybrid alpha-amylase comprising residues 1 -33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90% sequence identity thereof. Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181 , N190, M197, 1201 , A209 and Q264. Most preferred variants of the hybrid alpha- amylase comprising residues 1 -33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of SEQ ID NO: 4 are those having the substitutions:

M197T;

H156Y+A181T+N190F+A209V+Q264S; or

G48A+T49I+G107A+H156Y+A181T+N190F+I201 F+A209V+Q264S.

Further amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99/019467 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181 , G182, H183, G184, N195, I206, E212, E216 and K269. Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184. Additional amylases which can be used are those having SEQ ID NO: 1 , SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96/023873 or variants thereof having 90% sequence identity to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7. Preferred variants of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181 , 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476. More preferred variants are those having a deletion in positions 181 and 182 or positions 183 and 184. Most preferred amylase variants of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476. Other amylases which can be used are amylases having SEQ ID NO: 2 of WO 08/153815, SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01/66712. Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201 , 207, 21 1 and 264. Further suitable amylases are amylases having SEQ ID NO: 2 of WO 09/061380 or variants having 90% sequence identity to SEQ ID NO: 2 thereof. Preferred variants of SEQ ID NO: 2 are those having a truncation of the C-terminus and/or a substitution, a deletion or an insertion in one of more of the following positions: Q87, Q98, S125, N128, T131 , T165, K178, R180, S181 , T182, G183, M201 , F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475. More preferred variants of SEQ ID NO: 2 are those having the substitution in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131 I, T165I, K178L, T182G, M201 L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/or deletion in position R180 and/or S181 or of T182 and/or G183. Most preferred amylase variants of SEQ ID NO: 2 are those having the substitutions:

N128C+K178L+T182G+Y305R+G475K;

N 128C+K178L+T182G+F202Y+Y305R+D319T+G475K;

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

S125A+N 128C+T131 I+T165I+K178L+T182G+Y305R+G475K wherein the variants are

C-terminally truncated and optionally further comprises a substitution at position 243 and/or a deletion at position 180 and/or position 181. Other suitable amylases are the alpha-amylase having SEQ ID NO: 12 in WO01/66712 or a variant having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO: 12 in WO01/66712: R28, R1 18, 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. Particular preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R1 18K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions. Other examples are amylase variants such as those described in WO201 1/098531 , WO2013/001078 and WO2013/001087. Commercially available amylases are DuramylTM, TermamylTM, FungamylTM, Stainzyme TM, Stainzyme PlusTM, NatalaseTM, Liquozyme X and BANTM (from Novozymes A/S), and RapidaseTM , PurastarTM/EffectenzTM, Powerase and Preferenz S100, Preferenz S1 10, and Preferenz S1000 (from Genencor International Inc./DuPont).

Peroxidases/Oxidases: Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered variants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.

Commercially available peroxidases include Guardzyme® (Novozymes A/S).

The detergent enzyme(s) may be included in a detergent composition by adding separate additives containing one or more enzymes, or by adding a combined additive comprising all of these enzymes. A detergent additive of the invention, i.e., a separate additive or a combined additive, can be formulated, for example, as a granulate, liquid, slurry, etc. Preferred detergent additive formulations are granulates, in particular non-dusting granulates as described above, liquids, in particular stabilized liquids, or slurries.

Surfactants

Typically, the detergent composition comprises (by weight of the composition) one or more surfactants in the range of 0% to 50%, preferably from 2% to 40%, more preferably from 5% to 35%, more preferably from 7% to 30%, most preferably from 10% to 25%, even most preferably from 15% to 20%. In a preferred embodiment the detergent is a liquid or powder detergent comprising less than 40%, preferably less than 30%, more preferably less than 25%, even more preferably less than 20% by weight of surfactant. The composition may comprise from 1 % to 15%, preferably from 2% to 12%, 3% to 10%, most preferably from 4% to 8%, even most preferably from 4% to 6% of one or more surfactants. Preferred surfactants are anionic surfactants, non- ionic surfactants, cationic surfactants, zwitterionic surfactants, amphoteric surfactants, and mixtures thereof. Preferably, the major part of the surfactant is anionic. Suitable anionic surfactants are well known in the art and may comprise fatty acid carboxylates (soap), branched- chain, linear-chain and random chain alkyl sulfates or fatty alcohol sulfates or primary alcohol sulfates or alkyl benzenesulfonates such as LAS and LAB or phenylalknesulfonates or alkenyl sulfonates or alkenyl benzenesulfonates or alkyl ethoxysulfates or fatty alcohol ether sulfates or alpha-olefin sulfonate or dodecenyl/tetradecnylsuccinic acid. The anionic surfactants may be alkoxylated. The detergent composition may also comprise from 1 wt% to 10 wt% of non-ionic surfactant, preferably from 2 wt% to 8 wt%, more preferably from 3 wt% to 7 wt%, even more preferably less than 5 wt% of non-ionic surfactant. Suitable non-ionic surfactants are well known in the art and may comprise alcohol ethoxylates, and/or alkyl ethoxylates, and/or alkylphenol ethoxylates, and/or glucamides such as fatty acid N-glucosyl N-methyl amides, and/or alkyl polyglucosides and/or mono- or diethanolamides or fatty acid amides. The detergent composition may also comprise from 0 wt% to 10 wt% of cationic surfactant, preferably from 0.1 wt% to 8 wt%, more preferably from 0.5 wt% to 7 wt%, even more preferably less than 5 wt% of cationic surfactant. Suitable cationic surfactants are well known in the art and may comprise alkyl quaternary ammonium compounds, and/or alkyl pyridinium compounds and/or alkyl quaternary phosphonium compounds and/or alkyl ternary sulphonium compounds. The composition preferably comprises surfactant in an amount to provide from 100 ppm to 5,000 ppm surfactant in the wash liquor during the laundering process. The composition upon contact with water typically forms a wash liquor comprising from 0.5 g/l to 10 g/l detergent composition. Many suitable surface active compounds are available and fully described in the literature, for example, in "Surface- Active Agents and Detergents", Volumes I and 1 1 , by Schwartz, Perry and Berch.

Builders

The main role of builder is to sequester divalent metal ions (such as calcium and magnesium ions) from the wash solution that would otherwise interact negatively with the surfactant system. Builders are also effective at removing metal ions and inorganic soils from the fabric surface, leading to improved removal of particulate and beverage stains. Builders are also a source of alkalinity and buffer the pH of the wash water to a level of 9.5 to 1 1 . The buffering capacity is also termed reserve alkalinity, and should preferably be greater than 4.

The detergent compositions of the present invention may comprise one or more detergent builders or builder systems. Many suitable builder systems are described in the literature, for example in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc. Builder may comprise from 0% to 60%, preferably from 5% to 45%, more preferably from 10% to 40%, most preferably from 15% to 35%, even more preferably from 20% to 30% builder by weight of the subject composition. The composition may comprise from 0% to 15%, preferably from 1 % to 12%, 2% to 10%, most preferably from 3% to 8%, even most preferably from 4% to 6% of builder by weight of the subject composition.

Builders include, but are not limited to, the alkali metal, ammonium and alkanolammonium salts of polyphosphates (e.g., tripolyphosphate STPP), alkali metal silicates, alkaline earth and alkali metal carbonates, aluminosilicate builders (e.g., zeolite) and polycarboxylate compounds, ether hydroxypolycarboxylat.es, copolymers of maleic anhydride with ethylene or vinyl methyl ether, 1 , 3, 5-trihydroxy benzene-2, 4, 6-trisulphonic acid, and carboxymethyloxysuccinic acid, the various alkali metal, ammonium and substituted ammonium salts of polyacetic acids such as ethylenediamine tetraacetic acid and nitrilotriacetic acid, as well as polycarboxylates such as mellitic acid, succinic acid, citric acid, oxydisuccinic acid, polymaleic acid, benzene 1 ,3,5- tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble salts thereof. Ethanole amines (MEA, DEA, and TEA) may also contribute to the buffering capacity in liquid detergents.

Bleaches

The detergent compositions of the present invention may comprise one or more bleaching agents. In particular powdered detergents may comprise one or more bleaching agents. Suitable bleaching agents include other photobleaches, pre-formed peracids, sources of hydrogen peroxide, bleach activators, hydrogen peroxide, bleach catalysts and mixtures thereof. In general, when a bleaching agent is used, the compositions of the present invention may comprise from about 0.1 % to about 50% or even from about 0.1 % to about 25% bleaching agent by weight of the subject cleaning composition. Examples of suitable bleaching agents include:

(1 ) other photobleaches for example Vitamin K3;

(2) preformed peracids: Suitable preformed peracids include, but are not limited to, compounds selected from the group consisting of percarboxylic acids and salts, percarbonic acids and salts, perimidic acids and salts, peroxymonosulfuric acids and salts, for example, Oxone , and mixtures thereof. Suitable percarboxylic acids include hydrophobic and hydrophilic peracids having the formula R-(C=0)0-0-M wherein R is an alkyl group, optionally branched, having, when the peracid is hydrophobic, from 6 to 14 carbon atoms, or from 8 to 12 carbon atoms and, when the peracid is hydrophilic, less than 6 carbon atoms or even less than 4 carbon atoms; and M is a counterion, for example, sodium, potassium or hydrogen;

(3) sources of hydrogen peroxide, for example, inorganic perhydrate salts, including alkali metal salts such as sodium salts of perborate (usually mono- or tetra-hydrate), percarbonate, persulphate, perphosphate, persilicate salts and mixtures thereof. In one aspect of the invention the inorganic perhydrate salts are selected from the group consisting of sodium salts of perborate, percarbonate and mixtures thereof. When employed, inorganic perhydrate salts are typically present in amounts of from 0.05 to 40 wt%, or 1 to 30 wt% of the overall composition and are typically incorporated into such compositions as a crystalline solid that may be coated. Suitable coatings include inorganic salts such as alkali metal silicate, carbonate or borate salts or mixtures thereof, or organic materials such as water-soluble or dispersible polymers, waxes, oils or fatty soaps. Useful bleaching compositions are described in U.S. Patent Nos. 5,576,282, and 6,306,812;

(4) bleach activators having R-(C=0)-L wherein R is an alkyl group, optionally branched, having, when the bleach activator is hydrophobic, from 6 to 14 carbon atoms, or from 8 to 12 carbon atoms and, when the bleach activator is hydrophilic, less than 6 carbon atoms or even less than 4 carbon atoms; and L is leaving group. Examples of suitable leaving groups are benzoic acid and derivatives thereof - especially benzene sulphonate. Suitable bleach activators include dodecanoyl oxybenzene sulphonate, decanoyl oxybenzene sulphonate, decanoyl oxybenzoic acid or salts thereof, 3,5,5-trimethyl hexanoyloxybenzene sulphonate, tetraacetyl ethylene diamine (TAED) and nonanoyloxybenzene sulphonate (NOBS). Suitable bleach activators are also disclosed in WO 98/17767. While any suitable bleach activator may be employed, in one aspect of the invention the subject cleaning composition may comprise NOBS, TAED or mixtures thereof; and

(5) bleach catalysts that are capable of accepting an oxygen atom from peroxyacid and transferring the oxygen atom to an oxidizable substrate are described in WO 2008/007319.

Suitable bleach catalysts include, but are not limited to: iminium cations and polyions; iminium zwitterions; modified amines; modified amine oxides; N-sulphonyl imines; N-phosphonyl imines; N-acyl imines; thiadiazole dioxides; perfluoroimines; cyclic sugar ketones and mixtures thereof. The bleach catalyst will typically be comprised in the detergent composition at a level of from 0.0005% to 0.2%, from 0.001 % to 0.1 %, or even from 0.005% to 0.05% by weight.

When present, the peracid and/or bleach activator is generally present in the composition in an amount of from about 0.1 to about 60 wt%, from about 0.5 to about 40 wt% or even from about 0.6 to about 10 wt% based on the composition. One or more hydrophobic peracids or precursors thereof may be used in combination with one or more hydrophilic peracid or precursor thereof.

The amounts of hydrogen peroxide source and peracid or bleach activator may be selected such that the molar ratio of available oxygen (from the peroxide source) to peracid is from 1 :1 to 35:1 , or even 2:1 to 10:1 .

Adjunct materials

Dispersants - The detergent compositions of the present invention can also contain dispersants. In particular powdered detergents may comprise dispersants. Suitable water-soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.

Dye Transfer Inhibiting Agents - The detergent compositions of the present invention may also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about 0.0001 % to about 10%, from about 0.01 % to about 5% or even from about 0.1 % to about 3% by weight of the composition.

Fluorescent whitening agent - The detergent compositions of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent or optical brighteners. Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention. The most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulphonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives.

Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of 4, 4'-bis-(2-morpholino- 4 anilino-s-triazin-6-ylamino) stilbene disulphonate. Tinopal CBS is the disodium salt of 2,2'-bis- (phenyl-styryl) disulphonate.

Also preferred are fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India.

Other fluorescers suitable for use in the invention include the 1 -3-diaryl pyrazolines and the 7-alkylaminocoumarins.

Suitable fluorescent brightener levels include lower levels of from about 0.01 , from 0.05, from about 0.1 or even from about 0.2 wt% to upper levels of 0.5 or even 0.75 wt%.

Fabric hueing agents - The detergent compositions of the present invention may also include fabric hueing agents such as dyes or pigments which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liquor comprising said detergent compositions thus altering the tint of said fabric through absorption of visible light. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum. Suitable fabric hueing agents include dyes and dye-clay conjugates, and may also include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.I.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in WO 2005/03274, WO 2005/03275, WO 2005/03276 and EP 1 876 226. The detergent composition preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.0001 wt% to about 0.04 wt% fabric hueing agent. The composition may comprise from 0.0001 wt% to 0.2 wt% fabric hueing agent, this may be especially preferred when the composition is in the form of a unit dose pouch.

Soil release polymers - The detergent compositions of the present invention may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular, the removal of hydrophobic soils from polyester based fabrics. The soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series, volume 71 , Marcel Dekker, Inc. Another type of soil release polymers are amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure. The core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523. Furthermore, random graft co-polymers are suitable soil release polymers Suitable graft co-polymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/1 13314. Other soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose deriviatives such as those described in EP 1 867 808 or WO 2003/040279. Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cationically modified cellulose, zwitterionically modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methyl cellulose, carboxy methyl cellulose, ethyl cellulose, hydroxyl ethyl cellulose, hydroxyl propyl methyl cellulose, ester carboxy methyl cellulose, and mixtures thereof.

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

Other suitable adjunct materials include, but are not limited to, anti-shrink agents, anti- wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, structurants for liquid detergents and/or structure elasticizing agents.

In one aspect the detergent is a compact fluid laundry detergent composition comprising: a) at least about 10%, preferably from 20 to 80% by weight of the composition, of surfactant selected from anionic surfactants, non ionic surfactants, soap and mixtures thereof; b) from about 1 % to about 30%, preferably from 5 to 30%, by weight of the composition, of water; c) from about 1 % to about 15%, preferably from 3 to 10% by weight of the composition, of non-aminofunctional solvent; and d) from about 5% to about 20%, by weight of the composition, of a performance additive selected from chelants, soil release polymers, enzymes and mixtures thereof; wherein the compact fluid laundry detergent composition comprises at least one of:

(i) the surfactant has a weight ratio of the anionic surfactant to the nonionic surfactant from about 1.5:1 to about 5:1 , the surfactant comprises from about 15% to about 40%, by weight of the composition, of anionic surfactant and comprises from about 5% to about 40%, by weight of the composition, of the soap; (ii) from about 0.1 % to about 10%, by weight of the composition, of a suds boosting agent selected from suds boosting polymers, cationic surfactants, zwitterionic surfactants, amine oxide surfactants, amphoteric surfactants, and mixtures thereof; and (ii) both (i) and (ii). All the ingredients are described in WO 2007/130562. Further polymers useful in detergent formulations are described in WO 2007/149806.

In another aspect the detergent is a compact granular (powdered) detergent comprising a) at least about 10%, preferably from 15 to 60% by weight of the composition, of surfactant selected from anionic surfactants, non-ionic surfactants, soap and mixtures thereof; b) from about 10 to 80% by weight of the composition, of a builder, preferably from 20% to 60% where the builder may be a mixture of builders selected from i) phosphate builder, preferably less than 20%, more preferably less than 10% even more preferably less than 5% of the total builder is a phosphate builder; ii) a zeolite builder, preferably less than 20%, more preferably less than 10% even more preferably less than 5% of the total builder is a zeolite builder; iii) citrate, preferably 0 to 5% of the total builder is a citrate builder; iv) polycarboxylate, preferably 0 to 5% of the total builder is a polycarboxylate builder v) carbonate, preferably 0 to 30% of the total builder is a carbonate builder and vi) sodium silicates, preferably 0 to 20% of the total builder is a sodium silicate builder; c) from about 0% to 25% by weight of the composition, of fillers such as sulphate salts, preferably from 1 % to 15%, more preferably from 2% to 10%, more preferably from 3% to 5% by weight of the composition, of fillers; and d) from about 0.1 % to 20% by weight of the composition, of enzymes, preferably from 1 % to 15%, more preferably from 2% to 10% by weight of the composition, of enzymes.

The soils and stains that are important for detergent formulators are composed of many different substances, and a range of different enzymes, all with different substrate specificities have been developed for use in detergents both in relation to laundry and hard surface cleaning, such as dishwashing. These enzymes are considered to provide an enzyme detergency benefit, since they specifically improve stain removal in the cleaning process they are applied in as compared to the same process without enzymes. Stain removing enzymes that are known in the art include enzymes such as carbohydrases, amylases, proteases, lipases, cellulases, hemicellulases, xylanases, cutinases, and pectinase.

In a preferred aspect of the present invention the beta-glucanase of the invention may be combined with at least two enzymes. These additional enzymes are described in details in the section "other enzymes", more preferred at least three, four or five enzymes. Preferably, the enzymes have different substrate specificity, e.g., carbolytic activity, proteolytic activity, amylolytic activity, lipolytic activity, hemicellulytic activity or pectolytic activity. The enzyme combination may for example be a beta-glucanase of the invention with another stain removing enzyme, e.g., a beta-glucanase of the invention and a protease, a beta-glucanase of the invention and a serine protease, a beta-glucanase of the invention and an amylase, a beta-glucanase of the invention and a licheninase , beta-glucanase of the invention and a lipase, a beta-glucanase of the invention and a cutinase, a beta-glucanase of the invention and a pectinase or a beta-glucanase of the invention and an anti-redeposition enzyme. More preferably, the beta-glucanase of the invention is combined with at least two other stain removing enzymes, e.g., a beta-glucanase of the invention, a lipase and an amylase; or a beta-glucanase of the invention, a protease and an amylase; or a beta-glucanase of the invention, a protease and a lipase; or a beta-glucanase of the invention, a protease and a pectinase; or a beta-glucanase of the invention, a protease and a cellulase; or a beta-glucanase of the invention, a protease and a hemicellulase; or a beta- glucanase of the invention, a protease and a cutinase; or a beta-glucanase of the invention, an amylase and a pectinase; or a beta-glucanase of the invention, an amylase and a cutinase; or a beta-glucanase of the invention, an amylase and a cellulase; or a beta-glucanase of the invention, an amylase and a hemicellulase; or a beta-glucanase of the invention, a lipase and a pectinase; or a beta-glucanase of the invention, a lipase and a cutinase; or a beta-glucanase of the invention, a lipase and a cellulase; or a beta-glucanase of the invention, a lipase and a hemicellulase. Even more preferably, a beta-glucanase of the invention may be combined with at least three other stain removing enzymes, e.g., a beta-glucanase of the invention, a protease, a lipase and an amylase; or a beta-glucanase of the invention, a protease, an amylase and a pectinase; or a beta- glucanase of the invention, a protease, an amylase and a cutinase; or a beta-glucanase of the invention, a protease, an amylase and a cellulase; or a beta-glucanase of the invention, a protease, an amylase and a hemicellulase; or a beta-glucanase of the invention, an amylase, a lipase and a pectinase; or a beta-glucanase of the invention, an amylase, a lipase and a cutinase; or a beta-glucanase of the invention, an amylase, a lipase and a cellulase; or a beta-glucanase of the invention, an amylase, a lipase and a hemicellulase; or a beta-glucanase of the invention, a protease, a lipase and a pectinase; or a beta-glucanase of the invention, a protease, a lipase and a cutinase; or a beta-glucanase of the invention, a protease, a lipase and a cellulase; or a beta-glucanase of the invention, a protease, a lipase and a hemicellulase. A beta-glucanase according to the present invention may be combined with any of the enzymes selected from the non-exhaustive list comprising: carbohydrases, such as an amylase, a hemicellulase, a pectinase, a cellulase, a xanthanase or a pullulanase, a peptidase, a protease or a lipase.

In a preferred embodiment, a beta-glucanase of the invention is combined with a serine protease, e.g., an S8 family protease such as Savinase®.

In another embodiment of the present invention, a beta-glucanase of the invention may be combined with one or more metalloproteases, such as an M4 metalloprotease, including Neutrase® or Thermolysin. Such combinations may further comprise combinations of the other detergent enzymes as outlined above.

The cleaning process or the textile care process may for example be a laundry process, a dishwashing process or cleaning of hard surfaces such as bathroom tiles, floors, table tops, drains, sinks and washbasins. Laundry processes can for example be household laundering, but it may also be industrial laundering. Furthermore, the invention relates to a process for laundering of fabrics and/or garments where the process comprises treating fabrics with a washing solution containing a detergent composition, and at least one beta-glucanase of the invention. The cleaning process or a textile care process can for example be carried out in a machine washing process or in a manual washing process. The washing solution can for example be an aqueous washing solution containing a detergent composition.

The fabrics and/or garments subjected to a washing, cleaning or textile care process of the present invention may be conventional washable laundry, for example household laundry. Preferably, the major part of the laundry is garments and fabrics, including knits, woven, denims, non-woven, felts, yarns, and towelling. The fabrics may be cellulose based such as natural cellulosics, including cotton, flax, linen, jute, ramie, sisal or coir or manmade cellulosics (e.g., originating from wood pulp) including viscose/rayon, ramie, cellulose acetate fibers (tricell), lyocell or blends thereof. The fabrics may also be non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabit and silk or synthetic polymer such as nylon, aramid, polyester, acrylic, polypropylen and spandex/elastane, or blends thereof as well as blend of cellulose based and non-cellulose based fibers. Examples of blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl alcohol fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and cellulose-containing fibers (e.g., rayon/viscose, ramie, flax, linen, jute, cellulose acetate fibers, lyocell).

The last few years there has been an increasing interest in replacing components in detergents, which is derived from petrochemicals with renewable biological components such as enzymes and polypeptides without compromising the wash performance. When the components of detergent compositions change new enzyme activities or new enzymes having alternative and/or improved properties compared to the common used detergent enzymes such as proteases, lipases and amylases is needed to achieve a similar or improved wash performance when compared to the traditional detergent compositions. Typical detergent compositions includes various components in addition to the enzymes, these components have different effects, some components like the surfactants lower the surface tension in the detergent, which allows the stain being cleaned to be lifted and dispersed and then washed away, other components like bleach systems removes discolor often by oxidation and many bleaches also have strong bactericidal properties, and are used for disinfecting and sterilizing. Yet other components like builder and chelator softens, e.g., the wash water by removing the metal ions from the liquid.

In a particular embodiment, the invention concerns the use of a composition comprising a beta-glucanase of the invention, wherein said enzyme composition further comprises at least one or more of the following a surfactant, a builder, a chelator or chelating agent, bleach system or bleach component in laundry or dish wash.

In a preferred embodiment of the invention the amount of a surfactant, a builder, a chelator or chelating agent, bleach system and/or bleach component are reduced compared to amount of surfactant, builder, chelator or chelating agent, bleach system and/or bleach component used without the added beta-glucanase of the invention. Preferably the at least one component which is a surfactant, a builder, a chelator or chelating agent, bleach system and/or bleach component is present in an amount that is 1 % less, such as 2% less, such as 3% less, such as 4% less, such as 5% less, such as 6% less, such as 7% less, such as 8% less, such as 9% less, such as 10% less, such as 15% less, such as 20% less, such as 25% less, such as 30% less, such as 35% less, such as 40% less, such as 45% less, such as 50% less than the amount of the component in the system without the addition of beta-glucanase of the invention, such as a conventional amount of such component. In one aspect, the beta-glucanase of the invention is used in detergent compositions wherein said composition is free of at least one component which is a surfactant, a builder, a chelator or chelating agent, bleach system or bleach component and/or polymer.

Washing method

The detergent compositions of the present invention are ideally suited for use in laundry applications. Accordingly, the present invention includes a method for laundering a fabric. The method comprises the steps of contacting a fabric to be laundered with a cleaning laundry solution comprising the detergent composition according to the invention. The fabric may comprise any fabric capable of being laundered in normal consumer use conditions. The solution preferably has a pH of from about 5.5 to about 8, further preferably pH selected in the range from about 7.5 to about 13.5, or in the range from about 7.5 to about 12.5, or in the range from about 8.5 to about 1 1.5, or in the range from about 9.5 to about 10.5, or pH 7.5 or above.

A preferred embodiment concerns a method of cleaning, the method comprising the steps of: contacting an object with a high pH cleaning composition (e.g. pH 7.5 or above) comprising a beta-glucanase of the invention under conditions suitable for cleaning the object. In a preferred embodiment the cleaning composition is used in a laundry or a dish wash process.

Still another embodiment relates to a method for removing stains from fabric or dishware which comprises contacting the fabric or dishware with a high pH cleaning composition (e.g. pH 7.5 or above) comprising a beta-glucanase of the invention under conditions suitable for cleaning the object.

Also contemplated are compositions and methods of treating fabrics (e.g., to desize a textile) using the cleaning composition of the invention. The high pH cleaning composition can be used in any fabric-treating method which is well known in the art.

In another embodiment the high pH cleaning composition of the present invention is suited for use in liquid laundry and liquid hard surface applications, including dish wash and car wash. Accordingly, the present invention includes a method for laundering a fabric or washing a hard surface. The method comprises the steps of contacting the fabric/dishware to be cleaned with a solution comprising the high pH cleaning composition according to the invention. The fabric may comprise any fabric capable of being laundered in normal consumer use conditions. The hard surface may comprise any dishware such as crockery, cutlery, ceramics, plastics such as melamine, metals, china, glass, acrylics or other hard surfaces such as cars, floors etc. The solution preferably has a pH, e.g. 7.5 or above, e.g. from about 9 to about 13.5.

The compositions may be employed at concentrations of from about 100 ppm, preferably 500 ppm to about 15,000 ppm in solution. The water temperatures typically range from about 5°C to about 90°C, including about 10°C, about 15°C, about 20°C, about 25°C, about 30°C, about 35°C, about 40°C, about 45°C, about 50°C, about 55°C, about 60°C, about 65°C, about 70°C, about 75°C, about 80°C, about 85°C and about 90°C. The water to fabric ratio is typically from about 1 :1 to about 30:1.

In particular embodiments, the washing method is conducted at a pH of from about 5.0 to about 1 1.5, or in alternative embodiments, even from about 6 to about 10.5, such as about 5 to about 1 1 , about 5 to about 10, about 5 to about 9, about 5 to about 8, about 5 to about 7, about 5.5 to about 1 1 , about 5.5 to about 10, about 5.5 to about 9, about 5.5 to about 8, about 5.5. to about 7, about 6 to about 1 1 , about 6 to about 10, about 6 to about 9, about 6 to about 8, about 6 to about 7, about 6.5 to about 1 1 , about 6.5 to about 10, about 6.5 to about 9, about 6.5 to about 8, about 6.5 to about 7, about 7 to about 1 1 , about 7 to about 10, about 7 to about 9, or about 7 to about 8, preferably about 5.5 to about 9, and more preferably about 6 to about 8. In preferred embodiments the washing method is conducted at a pH selected in the range from about 7.5 to about 13.5, or in the range from about 7.5 to about 12.5, or in the range from about 8.5 to about 1 1.5, or in the range from about 9.5 to about 10.5, or pH 7.5 or above.

In some preferred embodiments, the high pH cleaning compositions provided herein are typically formulated such that, during use in aqueous cleaning operations, the wash water has a pH of from about 9 to about 13.5, or in alternative embodiments, or from about 10 to about 13.5 even from about 1 1 to about 13.5. In some preferred embodiments the liquid laundry products are formulated to have a pH from about 12 to about 13.5. Techniques for controlling pH at recommended usage levels include the use of buffers, acids, alkalis, etc., and are well known to those skilled in the art. In the context of the present invention alkalis are used to adjust pH to about 9 to 13.5 preferably about 10 to 13.5.

In particular embodiments, the washing method is conducted at a degree of hardness of from about 0°dH to about 30°dH, such as about 1 °dH, about 2°dH, about 3°dH, about 4°dH, about 5°dH, about 6°dH, about 7°dH, about 8°dH, about 9°dH, about 10°dH, about 1 1 °dH, about 12°dH, about 13°dH, about 14°dH, about 15°dH, about 16°dH, about 17°dH, about 18°dH, about 19°dH, about 20°dH, about 21 °dH, about 22°dH, about 23°dH, about 24°dH, about 25°dH, about 26°dH, about 27°dH, about 28°dH, about 29°dH, about 30°dH. Under typical European wash conditions, the degree of hardness is about 15°dH, under typical US wash conditions about 6°dH, and under typical Asian wash conditions, about 3°dH.

The present invention relates to a method of cleaning a fabric, a dishware or hard surface with a detergent composition comprising a beta-glucanase of the invention.

A preferred embodiment concerns a method of cleaning, said method comprising the steps of: contacting an object with a cleaning composition comprising a beta-glucanase of the invention under conditions suitable for cleaning said object. In a preferred embodiment the cleaning composition is a detergent composition and the process is a laundry or a dish wash process.

Still another embodiment relates to a method for removing stains from fabric which comprises contacting said a fabric with a composition comprising a beta-glucanase of the invention under conditions suitable for cleaning said object.

Low temperature uses

One embodiment of the invention concerns a method of doing laundry, dish wash or industrial cleaning comprising contacting a surface to be cleaned with a beta-glucanase of the invention, and wherein said laundry, dish wash, industrial or institutional cleaning is performed at a temperature of about 40°C or below. One embodiment of the invention relates to the use of a beta-glucanase in laundry, dish wash or a cleaning process wherein the temperature in laundry, dish wash, industrial cleaning is about 40°C or below

In another embodiment, the invention concerns the use of a beta-glucanase according to the invention in a beta-glucan removing process, wherein the temperature in the beta-glucan removing process is about 40°C or below.

In each of the above-identified methods and uses, the wash temperature is about 40°C or below, such as about 39°C or below, such as about 38°C or below, such as about 37°C or below, such as about 36°C or below, such as about 35°C or below, such as about 34°C or below, such as about 33°C or below, such as about 32°C or below, such as about 31°C or below, such as about 30°C or below, such as about 29°C or below, such as about 28°C or below, such as about 27°C or below, such as about 26°C or below, such as about 25°C or below, such as about 24°C or below, such as about 23°C or below, such as about 22°C or below, such as about 21°C or below, such as about 20°C or below, such as about 19°C or below, such as about 18°C or below, such as about 17°C or below, such as about 16°C or below, such as about 15°C or below, such as about 14°C or below, such as about 13°C or below, such as about 12°C or below, such as about 1 1 °C or below, such as about 10°C or below, such as about 9°C or below, such as about 8°C or below, such as about 7°C or below, such as about 6°C or below, such as about 5°C or below, such as about 4°C or below, such as about 3°C or below, such as about 2°C or below, such as about 1 °C or below.

In another preferred embodiment, the wash temperature is in the range of about 5-40°C, such as about 5-30°C, about 5-20°C, about 5-10°C, about 10-40°C, about 10-30°C, about 10- 20°C, about 15-40°C, about 15-30°C, about 15-20°C, about 20-40°C, about 20-30°C, about 25- 40°C, about 25-30°C, or about 30-40°C. In particular, preferred embodiments the wash temperature is about 20°C, about 30°C, or about 40°C.

High temperature uses

One embodiment of the invention concerns a method of doing laundry, dish wash or industrial cleaning comprising contacting a surface to be cleaned with composition of the invention, and wherein said laundry, dish wash, industrial or institutional cleaning is performed at a temperature of about 75°C or below. One embodiment of the invention relates to the use of a beta-glucanase in laundry, dish wash or a cleaning process wherein the temperature in laundry, dish wash, industrial cleaning is about 70°C or below.

In another embodiment, the invention concerns the use of a composition according to the invention in a beta-glucan removing process, wherein the temperature in the beta-glucan removing process is about 65°C or below.

In each of the above-identified methods and uses, the wash temperature is about 60°C or below, such as about 59°C or below, such as about 58°C or below, such as about 57°C or below, such as about 56°C or below, such as about 55°C or below, such as about 54°C or below, such as about 53°C or below, such as about 52°C or below, such as about 51 °C or below, such as about 50°C or below, such as about 49°C or below, such as about 48°C or below, such as about 47°C or below, such as about 46°C or below, such as about 45°C or below, such as about 44°C or below, such as about 43°C or below, such as about 42°C or below, such as about 41°C or below.

In another preferred embodiment, the wash temperature is in the range of about 41 -90°C, such as about 41 -80°C, about 41 -85°C, about 41 -80°C, about 41 -75°C, about 41 -70°C, about 41 - 65°C, about 41 -60°C. The present invention is further described by the following examples that should not be construed as limiting the scope of the invention.

EXAMPLES

Example 1 - Activity determination assays

pNP-G7 assay for determination of alpha-amylase activity

The alpha-amylase activity may be determined by a method employing the G7-pNP substrate. G7-pNP which is an abbreviation for 4,6-ethylidene(G/>-p-nitrophenyl(G!)-a,D- maltoheptaoside, a blocked oligosaccharide which can be cleaved by an endo-amylase, such as an alpha-amylase. Following the cleavage, the alpha-Glucosidase included in the kit digest the hydrolysed substrate further to liberate a free PNP molecule which has a yellow color and thus can be measured by visible spectophometry at λ=405ηηΊ (400-420 nm.). Kits containing G7-pNP substrate and alpha-Glucosidase is manufactured by Roche/Hitachi (cat. No.1 1876473).

The G7-pNP substrate from this kit contains 22 mM 4,6-ethylidene- G7-pNP and 52.4 mM

HEPES (2-[4-(2-hydroxyethyl)-1 -piperazinyl]-ethanesulfonic acid), pH 7.0).

The alpha-Glucosidase reagent contains 52.4 mM HEPES, 87 mM NaCI, 12.6 mM MgCI₂, 0.075 mM CaC , > 4 kU/L alpha-glucosidase).

The substrate working solution is made by mixing 1 mL of the alpha-Glucosidase reagent with 0.2 mL of the G7-pNP substrate. This substrate working solution is made immediately before use.

Dilution buffer: 50 mM MOPS, 0.05% (w/v) Triton X100 (polyethylene glycol p-(1 , 1 ,3,3- tetramethylbutyl)-phenyl ether (Ci4H₂20(C2H₄0)_/1 (n = 9-10))), 1 mM CaCI2, pH8.0.

The amylase sample to be analyzed was diluted in dilution buffer to ensure the pH in the diluted sample is 7. The assay was performed by transferring 20μΙ diluted enzyme samples to 96 well microtiter plate and adding 80μΙ substrate working solution. The solution was mixed and pre- incubated 1 minute at room temperature and absorption is measured every 20 sec. over 5 minutes at OD 405 nm.

The slope (absorbance per minute) of the time dependent absorption-curve is directly proportional to the specific activity (activity per mg enzyme) of the alpha-amylase in question under the given set of conditions. The amylase sample should be diluted to a level where the slope is below 0.4 absorbance units per minute.

AZCL-He-cellulose assay for determination of cellulase activity

An AZCL-He-cellulose (azurine dye covalently cross-linked cellulose) assay was used for detection of cellulase (endo-glucanase) activity. AZCL-He-cellulose (75 mg) was suspended in 15 mL detergent (Model detergent A, Model detergent X or ADW Model detergent A). To 1 mL of this solution in Eppendorf tubes was added 100 L enzyme (0.09 mg enzyme protein/mL), incubated for 15 min at 40°C while shaking at 1250 rpm in a pre-heated thermo mixer and spun down for 2 min at 13200 rpm. 250 μί of the solution was transferred to a micro-titer plate and the sample absorbance was measured at 590 nm.

Example 2 - detergent compositions

Detergent compositions used in the following example were made according to the definitions below.

Model detergent A

Compound Content of compound (% w/w) Active component (% w/w)

LAS 12.0 97

AEOS, SLES 17.6 28

Soy fatty acid 2.8 90

Coco fatty acid 2.8 99

AEO 1 1.0 100

Sodium hydroxide 1 .8 99

Ethanol / Propan-2-ol 3.0 90/10

MPG 6.0 98

Glycerol 1 .7 99.5

TEA 3.3 100

Sodium formate 1 .0 95

Sodium citrate 2.0 100

DTMPA (as Na7-salt) 0.5 42

PCA (as Na-salt) 0.5 40

Phenoxy ethanol 0.5 99

Ion exchanged water 33.6 —

The water hardness was adjusted to 15°dH by addition of CaCI2, MgCI2, and NaHC03 (Ca2+:Mg2+:HC03- = 4:1 :7.5) to the test system.

Model detergent X

Compound Content of compound (% w/w) Active component (% w/w)

LAS 16.5 91

AEO^* 2 99.5

Sodium carbonate 20 100 Sodium (di)silicate 12 82.5

Zeolite A 15 80

Sodium sulfate 33.5 100

PCA 1 100

^* Model detergent X was mixed without AEO. AEO was added separately before wash. The water hardness was adjusted to 12°dH by addition of CaCI2, MgCI2, and NaHC03 (Ca2+:Mg2+:HC03- = 2:1 :4.5) to the test system.

ADW model detergent A

Compound Content of compound (% w/w) Active component w/w)

MGDA (Trilon M Granules SG) 20 59

Sodium citrate 20 100

Sodium carbonate 20 100

Sodium percarbonate 10 88

Sodium Silicate 5 80

Sodium sulfate 12 100

Acusol 588G 5 92

TAED 3 92

Surfac 23-6.5 (liq) 5 100

The water hardness was adjusted to 21 °dH by addition of CaCI2, MgCI2, and NaHC03 (Ca2+:Mg2+:HC03- = 2:1 :7) to the test system.

Example 3 - Synergistic effect of cellulase combined with an alpha-amylase

Wascator bottle wash method

A Wascator bottle wash method was used to detect the performance of the enzymes. In a Wascator washing machine (FOM 71 Lab) bottles (60 mL, DSE PP 70X35 Aseptisk, material No.: 216-2620, from VWR) with 25 mL detergent solution including enzyme(s) and four stains (035KC Chocolate porridge oat from Equest, UK, 2 cm in diameter) were added. Two kg ballast (tea towels, cotton) was included in the washing machine. Washed in 25 L water for 30 min at 40°C in liquid and powder model detergents for laundry (model detergent A and model detergent X, respectively) and in ADW model detergent (ADW model detergent A). After wash the stains were rinsed with tap water twice (3 L) and dried ON at room temperature in drying cabinet (Electrolux, Intuition, EDD2400). The remission was measured on a spectrophotometer (Macbeth Color-Eye 7000 Remissions) at 460 nm. In this experiment the results of combining the individual cellulases with an alpha-amylase (a variant of AA560 (SEQ ID NO: 6), the variant contains the following modifications: R1 18K+D183^*+G184^*+N195F+R320K+R458K) were studied in order to investigate a potential synergistic effect between the two enzymes in various detergents with various pHs using the Wascator bottle wash method with 0.01 mg enzyme protein per liter of cellulase and 0.05 mg enzyme protein per liter of alpha-amylase variants at 40°C. The detailed conditions used in this experiment are described in Tables 1 , 2, and 3 the results are shown in Tables 4-6 below.

Table 1 : Experimental conditions for Wascator bottle wash performance

Table 3: Experimental conditions for Wascator bottle wash performance

Test solution volume 25 ml_

pH As is

Wash time 30 minutes

Temperature 40°C

Water hardness 21 °dH

Amylase concentration in test 0.05 mg/L

Cellulase concentration in test 0.01 mg/L

Test material 035 KC Chocolate porridge oats

Abbreviations as used herein: REM = Measured value; AREM = REM - Blank; REM combined = Measured value; AREM combined = REM combined - Blank; AREM theoretic = AREM (Amylase) + AREM (Cellulase); REM Synergistic effect = AREM combined - AREM theoretic

Table 4: Wascator bottle wash in Model detergent A at 40°C, 30 min (pH 7.7):

Table 5: Wascator bottle wash in Model detergent X at 40°C, 30 min (pH 10.1 ):

Cellulase 3 (SEQ ID NO 3) 57,4 -0,2 70,0 12,4 7,1 5,3

Cellulase 4 (SEQ ID NO 4) 58,8 1 ,2 67,0 9,4 8,5 0,9

Cellulase 5 (SEQ ID NO 5) 57,7 0,1 65,7 8,1 7,4 0.7

SEQ ID NO: 6 +

R1 18K+D183^*+G184^*+N195F

+R320K+R458K 64,9 7,3

Blank 57,6 0,0 — — — —

Table 6: Wascator bottle wash in ADW Model detergent A at 40°C, 30 min (pH 10.1 ):

Claims

1 . A composition comprising (i) a polypeptide having cellulase activity, selected from the group consisting of:

(b) a fragment of the polypeptide of (a) that has cellulase activity;

and (ii) at least one polypeptide having alpha-amylase activity.

2. The composition according to claim 1 , wherein said polypeptide having cellulase activity has at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to any one of the mature polypeptide sequences selected from the group consisting of: SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5.

3. The composition according to any one of the preceding claims, wherein said polypeptide having alpha-amylase activity is selected from the group consisting of a polypeptide sequence having at least 75% sequence identity any one of the polypeptide sequences selected from the group consisting of: SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 1 1 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, and SEQ ID NO: 19.

4. The composition according to any one of the preceding claims, wherein said polypeptide having cellulose activity is beta-1 ,4-glucanase EC 3.2.1 .4 activity.

5. The composition according to any one of the preceding claims, wherein said polypeptide having alpha-amylase activity is alpha-1 ,4-glucan-4-glucanohydrolase E.C. 3.2.1.1 activity.

6. The composition according to any one of the preceding claims, further comprising:

i) one or more detergent components; and/or

ii) one or more additional enzymes.

7. The composition according to any one of the preceding claims, wherein said composition has a pH of 7.5 or above and optionally comprises a bleaching agent; preferably said pH is in the range from about 7.5 to about 13.5, further preferably said pH is in the range from about 7.5 to about 12.5, most preferably said pH is in the range from about 8.5 to about 1 1.5, further most preferably said pH is in the range from about 9.5 to about 10.5.

8. The composition according to any one of the preceding claims, wherein said composition is a cleaning or a detergent composition, wherein said cleaning or a detergent composition is a dish wash composition or a laundry composition.

9. The composition according to any one of the preceding claims, wherein said alpha- amylase is selected from the group consisting of:

(a) a polypeptide having at least 75% sequence identity to SEQ ID NO: 6, optionally, wherein the polypeptide comprises a modification in one or more of positions: 9, 15,

23, 105, 106, 1 18, 124, 128, 133, 149, 154, 156, 178, 179, 181 , 182, 183, 184, 186, 188, 190, 195, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 246, 257, 264, 295, 299, 304, 305, 320, 323, 339, 391 , 408, 444, 445, and/or 458;

(b) a polypeptide having at least 75% sequence identity to SEQ ID NO: 7, optionally, wherein the polypeptide comprises a modification in one or more of positions: 1 , 7,

109, 140, 181 , 182, 183, 184, 195, 206, 243, 260, 280, 304, 391 and/or 476,

(c) a polypeptide having at least 75% sequence identity to SEQ ID NO: 8, optionally, wherein the polypeptide comprises a modification in one or more of positions: 180,

181 , 182, 183, 243, and/or 475;

153, 178, 179, 180, 181 , 187, 203, 458, 459, 460, and/or 476;

(f) a polypeptide having at least 75% sequence identity to SEQ ID NO: 1 1 , optionally, wherein the polypeptide comprises a modification in one or more of positions: 181 ,

182, 183, 184, 405, 421 , 422, and/or 428;

(g) a polypeptide having at least 75% sequence identity to SEQ ID NO: 12;

(h) a polypeptide having at least 75% sequence identity to SEQ ID NO: 13, optionally, wherein the polypeptide comprises a modification in one or more of positions: 48, 49,

107, 156, 181 , 190, 197, 201 , 209, and/or 264;

(I) a polypeptide having at least 75% sequence identity to SEQ ID NO: 18.

10. The composition according to any one of the preceding claims, wherein said composition further comprises a protease, preferably, wherein said protease is a polypeptide having at least 60% sequence identity to SEQ ID NO: 20.

1 1 . The composition according to any one of the preceding claims, wherein said polypeptides in said composition has improved stability and/or wash performance under alkaline conditions, preferably said alkaline conditions have pH 7.5 or above.

12. Use of the composition according to any one of the preceding claims in a cleaning process such as laundry, optionally said use is carried out under alkaline conditions having pH 7.5 or above.

13. A process of degrading a cellulose-containing material comprising applying the composition according to any one of claims 1 to 1 1 to said cellulose-containing material; optionally, said process is carried out under alkaline conditions having pH 7.5 or above.

14. A method for reducing or preventing soil re-deposition using a composition according to any one of claims 1 to 1 1 .

15. A method of laundering fabrics or textiles or hard surface cleaning including automated dish wash (ADW) and hand dish wash (HDW) using a composition according to any one of claims 1 to 1 1 .