Family 44 xyloglucanase variants

Abstract

The present disclosure relates to xyloglucanase variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

Description

[0001] This application is a divisional application of Chinese patent application No. 2021800504887, filed on August 24, 2021, entitled "Family 44 Xyloglucanase Variants".

[0002] References to sequence lists

[0003] This application contains a sequence list in a computer-readable form, which is incorporated herein by reference. Technical Field

[0004] The present invention relates to xyloglucanase variants belonging to the glycosyl hydrolase family 44, polynucleotides encoding these variants, and methods for producing these variants. Background Technology

[0005] Xyloglucan is the main structural polysaccharide in the primary (growing) cell walls of plants. Structurally, xyloglucan consists of a cellulose-like β-1,4-linked glucose backbone, which is frequently replaced by various side chains. Xyloglucan is believed to function in the primary cell wall of plants by cross-linking cellulose microfibrils to form a cellulose-xyloglucan network.

[0006] Xyloglucanases catalyze the dissolution of xyloglucan into xyloglucan oligosaccharides. Some xyloglucanases exhibit only xyloglucanase activity, while others exhibit both xyloglucanase and cellulase activity. Xyloglucanases can be classified as EC 3.2.1.4 or EC 3.2.1.151. Enzymes with xyloglucanase activity are described, for example, in Vincken et al. (1997) Carbohydrate Research 298(4):299-310, which characterized three different endoglucanases, EndoI, EndoV, and EndoVI, from *Trichoderma viride* (similar to *T. reesei*). EndoI, EndoV, and EndoVI belong to families 5, 7, and 12, respectively; see Henrissat, B. (1991) Biochem. J. [Journal of Biochemistry] 280: 309-316 and Henrissat, B. and Bairoch, A. (1993) Biochem. J. [Journal of Biochemistry] 293: 781-788. WO 94 / 14953 discloses family 12 xyloglucanase (EG II) cloned from the fungus *Aspergillus aculeatus*. WO 99 / 02663 discloses family 12 and family 5 xyloglucanases cloned from *Bacillus licheniformis* and *Bacillus agaradhaerens*, respectively. WO 01 / 062903 discloses family 44 xyloglucanase.

[0007] Specifically, WO 99 / 02663 and WO 01 / 062903 indicate that xyloglucanase can be used in detergents. WO 2009 / 147210 provides xyloglucanase variants.

[0008] The purpose of this invention is to provide a xyloglucanase variant belonging to the glycosyl hydrolase family 44. Summary of the Invention

[0009] This invention relates to isolated xyloglucanase variants that contain alterations at one or more positions corresponding to positions selected from the group consisting of: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238 of the polypeptide of SEQ ID NO: 1. 240, 243, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, of which this variant has xyloglucanase activity. Preferably, the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3, and wherein the variant has xyloglucanase activity.

[0010] This invention relates to isolated xyloglucanase variants that contain a substitution at position 129T corresponding to the polypeptide of SEQ ID NO: 2, wherein the variant possesses xyloglucanase activity. Preferably, the variant has at least 99% but less than 100% sequence identity with the polypeptide of SEQ ID NO: 2. In particular, this invention relates to isolated xyloglucanase variants that comprise or consist of the polypeptide of SEQ ID NO: 3.

[0011] The present invention also relates to isolated polynucleotides encoding these variants; nucleic acid constructs, vectors, and host cells containing these polynucleotides; and methods for generating these variants.

[0012] The present invention also relates to cleaning methods and compositions that include variations of the present invention.

[0013] sequence

[0014] SEQ ID NO: 1 is a mature polypeptide obtained from Paenibacillus polymyxa.

[0015] SEQ ID NO: 2 variant peptide.

[0016] SEQ ID NO: 3 variant peptide.

[0017] SEQ ID NO: 4 is a protease protein sequence from Bacillus lentus.

[0018] definition

[0019] Based on this detailed description, the following definitions apply. Note that the singular forms “a / an” and “the” include plural indicators unless the context explicitly indicates otherwise.

[0020] This article refers to the value or parameter “about” as including aspects of that value or parameter itself. For example, a description of “about X” includes aspect “X”.

[0021] Unless otherwise defined or explicitly indicated by the context, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains.

[0022] Allele variants: The term "allelic variant" refers to any of two or more alternative forms of a gene occupying the same chromosomal locus. Allelic variations arise naturally through mutation and can lead to polymorphism within a population. Gene mutations can be silent (encoding a polypeptide with no change) or can encode a polypeptide with a modified amino acid sequence. Allelic variants of a polypeptide are polypeptides encoded by allelic variants of a gene.

[0023] Amino acids:As used herein, the term "amino acid" refers to the standard twenty genetically encoded amino acids and their corresponding stereoisomers in the "d" form (as opposed to the natural "l" form), ω-amino acids, other naturally occurring amino acids, unconventional amino acids (e.g., α,α-disubstituted amino acids, N-alkyl amino acids, etc.), and chemically derivatized amino acids. Chemical derivatives of one or more amino acids can be achieved by reacting with functional side groups. Such derived molecules include, for example, those in which the free amino group has been derivatized to form amine hydrochloride, p-toluenesulfonyl group, carboxyphenoxy group, tert-butoxycarbonyl group, chloroacetyl group, or formyl group. The free carboxyl group can be derivatized to form salts, methyl esters and ethyl esters, or other types of esters and hydrazides. The free hydroxyl group can be derivatized to form O-acyl or O-alkyl derivatives. Also included as chemical derivatives are peptides containing derivatives of the twenty standard amino acids. For example, 4-hydroxyproline can replace proline; 5-hydroxylysine can replace lysine; 3-methylhistidine can replace histidine; homoserine can replace serine and ornithine can replace lysine. Derivatives may also include peptides containing one or more additions or deletions, provided the necessary activity is maintained. Other modifications include amidation, amino-terminal acylation (e.g., acetylation or thioacetate amidation), terminal carboxyl amidation (e.g., with ammonia or methylamine), and similar terminal modifications.

[0024] When an amino acid is explicitly listed as "alanine," "Ala," or "A," the term refers to both l-alanine and d-alanine unless otherwise explicitly stated. Other unconventional amino acids may also be suitable components of the polypeptides of the present invention, provided that the desired functional properties are retained by the polypeptide. For the peptides shown, where appropriate, each encoded amino acid residue is represented by a single-letter symbol corresponding to the common name of a conventional amino acid. In one embodiment, the polypeptide of the present invention comprises or is composed of l-amino acids.

[0025] Cellulase or cellulaseThe term “cellulase” or “cellulase” refers to one or more (e.g., several) enzymes that hydrolyze cellulose materials. Such enzymes include one or more endoglucanases (e.g., EC3.2.1.4), one or more cellobiases, one or more β-glucosidases, or combinations thereof. Two basic methods for measuring cellulase activity include (1) measuring total cellulase activity and (2) measuring the activity of individual cellulases (endoglucanases, cellobiases, and β-glucosidases), as reviewed in Zhang et al., 2006, Biotechnology Advances 24: 452-481. Total cellulase activity can be measured using insoluble substrates, including Whatman No. 1 filter paper, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, pretreated lignocellulose, etc. The most common assay for total cellulose activity is the filter paper assay using Whatman No. 1 filter paper as the substrate. This assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, 1987, Pure Appl. Chem. 59: 257-68).

[0026] Cellulose materials The term "cellulose material" refers to any material containing cellulose. The primary polysaccharide in the primary cell walls of biomass is cellulose, followed by hemicellulose, and then pectin. Secondary cell walls, formed after cell cessation of growth, also contain polysaccharides and are reinforced by polymeric lignin covalently cross-linked with hemicellulose. Cellulose is a homopolymer of dehydrated cellobiose and is therefore a linear β-(1-4)-D-glucan, while hemicellulose comprises a variety of compounds with a complex branched structure containing a series of substituents, such as xylan, xyloglucan, arabinoylxylan, and mannan. Although cellulose is generally polymorphic, it is found primarily in plant tissues as an insoluble crystalline matrix of parallel glucan chains. Hemicellulose is typically hydrogen-bonded to cellulose and other hemicelluloses, which helps stabilize the cell wall matrix.

[0027] cDNA The term "cDNA" refers to a DNA molecule that can be prepared by reverse transcription from mature, spliced ​​mRNA molecules obtained from eukaryotic or prokaryotic cells. cDNA lacks intron sequences that can be present in the corresponding genomic DNA. The initial primary RNA transcript is the precursor of mRNA, which is processed through a series of steps (including splicing) to become mature, spliced ​​mRNA.

[0028] Encoded sequenceThe term "coding sequence" refers to a polynucleotide that directly defines the amino acid sequence of a variant. The boundaries of a coding sequence are typically defined by a read frame, which begins with a start codon (e.g., ATG, GTG, or TTG) and ends with a stop codon (e.g., TAA, TAG, or TGA). Coding sequences can be genomic DNA, cDNA, synthetic DNA, or a combination thereof.

[0029] control sequence The term "control sequence" refers to the nucleic acid sequence necessary for the expression of a polynucleotide encoding a variant of the present invention. Each control sequence may be native (i.e., from the same gene) or exogenous (i.e., from a different gene) for the polynucleotide encoding that variant, or native or exogenous relative to each other. Such control sequences include, but are not limited to, leader sequences, polyadenylated sequences, propeptide sequences, promoters, signal peptide sequences, and transcription terminators. At a minimum, these control sequences include promoters and transcription and translation termination signals. Control sequences may be provided with adapters for the purpose of introducing specific restriction sites that facilitate the connection of control sequences to the coding regions of polynucleotides encoding variants.

[0030] Dishwashing composition: As used herein, the term "dishwashing composition" refers to all forms of compositions for cleaning hard surfaces. This invention is not limited to any particular type of dishwashing composition or any particular detergent. Thus, in one embodiment, the dishwashing composition is a liquid dishwashing composition or a powdered dishwashing composition, wherein the composition may optionally be in unit dosage form.

[0031] Detergent components The term "detergent component" is defined herein as referring to a type of chemical that may be used in a detergent composition. Examples of detergent components include surfactants, water-soluble auxiliaries, builders, co-builders, chelators or chelating agents, bleaching systems or bleaching components, polymers, fabric toners, fabric conditioning agents, foam boosters, defoamers, dispersants, dye transfer inhibitors, optical brighteners, fragrances, optical brighteners, bactericides, fungicides, dirt suspending agents, dirt-releasing polymers, anti-redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants, and solubilizers. A detergent composition may contain one or more detergent components of any type.

[0032] Detergent compositionThe term "detergent composition" refers to a composition for removing unwanted compounds from items to be cleaned, such as textiles, tableware, and hard surfaces. This detergent composition can be used, for example, to clean textiles, tableware, and hard surfaces, for both household and industrial cleaning and / or for fabric care. These terms encompass any material / compound chosen for the form (e.g., liquid, gel, powder, granules, paste, or spray compositions) of the desired specific type of cleaning composition and product, and include, but are not limited to, detergent compositions (e.g., liquid and / or solid laundry detergents and delicate fabric detergents; hard surface cleaning formulations, such as those for glass, wood, plastic, ceramic, and metal countertops and windows; carpet cleaners; oven cleaners; fabric fresheners; fabric softeners; and textile and garment pre-stain removers, along with dishwashing detergents). In addition to the enzymes of this invention, the detergent formulation may also contain one or more other enzymes (e.g., amylase, protease, peroxidase, cellulase, β-glucanase, xyloglucanase, hemicellulase, xanthan gumase, xanthan gum lyase, lipase, acyltransferase, phospholipase, esterase, laccase, catalase, aryl esterase, amylase, α-amylase, glucosylamylase, keratinase, pectinase, pectin lyase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, carrageenanase, pullulanase, tanninase, arabinosidase, hyaluronidase, chondroitinase, xyloglucanase, xylanase, pectin acetylesterase, polygalacturonase, rhamnogalacturonase, endopeptidase). -β-mannanase, exo-β-mannanase (GH5 and / or GH26), licheninase, phosphodiesterase, pectin methyl esterase, cellobiase, transglutaminase, nuclease, and combinations thereof, or any mixture thereof), and / or components such as surfactants, detergents, chelating agents or chelating reagents, bleaching systems or bleaching components, polymers, fabric conditioners, foaming agents, defoaming agents, dyes, fragrances, darkening inhibitors, optical brighteners, bactericides, fungicides, dirt suspending agents, corrosion inhibitors, enzyme inhibitors or stabilizers, enzyme activators, one or more transferases, hydrolases, oxidoreductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.

[0033] Dishwashing The term "dishwashing" refers to all forms of dishwashing, such as manual dishwashing (HDW) or automatic dishwashing (ADW). Dishwashing includes, but is not limited to, cleaning all forms of tableware, such as plates, cups, glasses, bowls, all forms of cutlery (such as spoons, knives, and forks), and serving utensils made of ceramic, plastic, metal, porcelain, glass, and acrylic.

[0034] Benefits of enzyme washingThe term "enzyme washing benefit" is defined herein as the advantageous effect of adding an enzyme to a detergent compared to the same detergent without that enzyme. Important washing benefits that enzymes can provide include stain removal with little or no visible dirt after washing and / or cleaning; prevention or reduction of redeposition of dirt released during washing (also known as anti-redeposition effect); and complete or partial restoration of the whiteness of textiles that were originally white but have acquired a pale gray or yellowish appearance after repeated use and washing. Textile care benefits not directly related to catalyzing stain removal or preventing redeposition are also important to the enzyme washing benefit. Examples of such textile care benefits include preventing or reducing dye transfer from one fabric to another or another part of the same fabric (also known as dye transfer inhibition or anti-reversion effect); removing protruding or broken fibers from the fabric surface to reduce pilling tendency or remove existing pills or fuzz (also known as anti-pilling effect); improving fabric softness; clarifying fabric colors; and removing particulate dirt trapped in the fibers of fabrics or garments. Enzymatic bleaching is another benefit of enzyme washing, where catalytic activity is typically used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides.

[0035] Express The term "expression" includes any step involved in variant generation, including but not limited to transcription, post-transcriptional modification, translation, post-translational modification, and secretion.

[0036] expression carrier The term "expression vector" refers to a straight or circular DNA molecule that contains a polynucleotide encoding a variant and is operatively linked to a control sequence that provides for its expression.

[0037] Excerpt The term "fragment" refers to a polypeptide in which one or more (e.g., several) amino acids are missing from the amino and / or carboxyl ends of a mature polypeptide; wherein the fragment has xyloglucanase activity. In one aspect, the fragment contains at least 445 amino acid residues, at least 471 amino acid residues, or at least 497 amino acid residues.

[0038] Fusion PeptidesThe term "fusion polypeptide" refers to a polypeptide in which one polypeptide is fused at the N-terminus or C-terminus of a variant of the invention. Fusion polypeptides are produced by fusing a polynucleotide encoding another polypeptide with a polynucleotide of the invention. Techniques for producing fusion polypeptides are known in the art and include linking the coding sequences of the polypeptides such that they conform to reading frames, and that the expression of the fusion polypeptide is controlled by one or more identical promoters and terminators. Fusion polypeptides can also be constructed using intron technology, where the fusion polypeptide is produced post-translational (Cooper et al., 1993, EMBO J. [Journal of the European Society for Molecular Biology] 12: 2575-2583; Dawson et al., 1994, Science [Science] 266:776-779). Fusion polypeptides may further include a cleavage site between the two polypeptides. Upon secretion of the fusion protein, the site is cleaved, thereby releasing both polypeptides. Examples of cleavage sites include, but are not limited to, those disclosed in the following literature: Martin et al., 2003, J. Ind. Microbiol. Biotechnol. [Journal of Industrial Microbiology and Biotechnology] 3: 568-576; Svetina et al., 2000, J. Biotechnol. [Journal of Biotechnology] 76: 245-251; Rasmussen-Wilson et al., 1997, Appl. Environ. Microbiol. [Applied and Environmental Microbiology] 63: 3488-3493; Ward et al., 1995, Biotechnology [Biotechnology] 13: 498-503; and Contreras et al., 1991, Biotechnology [Biotechnology] 9: 378-381; Eaton et al., 1986, Biochemistry [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.

[0039] Hard surface cleaningThe term "hard surface cleaning" is defined in this document as cleaning hard surfaces, which can include floors, tables, walls, roofs, etc., along with surfaces of hard objects such as cars (car washing) and tableware (dishwashing). Dishwashing includes, but is not limited to, cleaning plates, cups, glasses, bowls, cutlery (such as spoons, knives, and forks), serving utensils, ceramics, plastics, metals, porcelain, glass, and acrylics.

[0040] host cells The term "host cell" refers to any cell type that is readily transformed, transfected, transduced, etc., using nucleic acid constructs or expression vectors containing the polynucleotides of the present invention. The term "host cell" also encompasses any parental cell progeny that differs from the parent cell due to mutations occurring during replication.

[0041] Hybrid polypeptides: The term "hybrid polypeptide" refers to a polypeptide comprising domains from two or more polypeptides of different origins (e.g., a binding module from one polypeptide and a catalytic domain from another). These domains may be fused at the N-terminus or C-terminus. Of particular interest in this paper are polypeptides comprising: a binding module from one polypeptide (which may be naturally occurring or further modified), an engineered linker region (e.g., a proline-rich linker region (which is a synthetic construct)), and a catalytic domain from another polypeptide (which may be naturally occurring or further modified).

[0042] Hybridization:The term "hybridization" refers to the pairing of substantially complementary strands of nucleic acids using a standard DNA blotting procedure. Hybridization can be performed under medium, medium-high, high, or very high stringency conditions. Medium stringency conditions refer to pre-hybridization and hybridization at 42°C in 5X SSPE, 0.3% SDS, 200 μg / ml of sheared and denatured salmon sperm DNA, and 35% formamide for 12 to 24 hours, followed by washing three times at 55°C with 0.2X SSC and 0.2% SDS for 15 minutes each. Medium-high stringency conditions refer to pre-hybridization and hybridization at 42°C in 5X SSPE, 0.3% SDS, 200 μg / ml of sheared and denatured salmon sperm DNA, and 35% formamide for 12 to 24 hours, followed by washing three times at 60°C with 0.2X SSC and 0.2% SDS for 15 minutes each. Highly stringent conditions refer to pre-hybridization and hybridization at 42°C in 5X SSPE, 0.3% SDS, 200 μg / ml of sheared and denatured salmon sperm DNA, and 50% formamide for 12 to 24 hours, followed by washing three times at 65°C with 0.2X SSC and 0.2% SDS for 15 minutes each time. Very high stringent conditions refer to pre-hybridization and hybridization at 42°C in 5X SSPE, 0.3% SDS, 200 μg / ml of sheared and denatured salmon sperm DNA, and 50% formamide for 12 to 24 hours, followed by washing three times at 70°C with 0.2X SSC and 0.2% SDS for 15 minutes each time.

[0043] Improved features The term "improved properties" refers to characteristics associated with a variant that is improved compared to the reference enzyme / parental enzyme. Such improved properties include, but are not limited to, improved washing performance, improved enzyme washing benefits, improved stability, and / or improved whiteness.

[0044] Improved stability The term "improved stability" refers to the variant enzyme retaining its enzyme activity after incubation for a period of time in the presence of one or more naturally occurring or synthetic chemicals that reduce the activity of the parent enzyme. Improved stability means that the variant enzyme exhibits better stability in the presence of a protease relative to the stability of a reference / parent enzyme, and includes, for example, protein hydrolysis stability, detergent storage stability, detergent storage stability in the presence of a chelating agent or chelating reagent, improved stability during the production of the detergent composition, and stability during washing. Specifically, improved detergent stability refers to the improved stability of xyloglucanase activity when the xyloglucanase variant of the present invention is mixed into a liquid detergent formulation or a unit dose detergent formulation and then stored at a temperature of 15°C–50°C.

[0045] In this invention, liquid detergent is particularly useful as a liquid laundry detergent and / or a unit dose laundry detergent.

[0046] Improvements in stability can be quantified, for example, by detergent stability testing as described in Example 3.

[0047] Improved washing performance The term "improved washing performance" is defined herein as the improved washing performance of an enzyme in a detergent composition relative to a reference / parent enzyme, for example, through increased color clarification and / or anti-pilling effect, when evaluated on a new sample and / or after the sample has been stored under the same conditions. The term "improved washing performance" includes washing performance in laundry and also in hard surface cleaning such as automated dishwashing (ADW).

[0048] Separate The term "isolated" means a polypeptide, nucleic acid, cell, or other specific material or component that is separate from at least one other material or component (including, but not limited to, other proteins, nucleic acids, cells, etc.) found in nature and naturally associated with it. Isolated polypeptides include, but are not limited to, culture media containing secreted polypeptides.

[0049] washing: The term "washing" encompasses both household and industrial washing and refers to the process of treating textiles with a solution containing the cleaning or detergent composition of the present invention. The washing process can be performed, for example, using a household or industrial washing machine or manually.

[0050] Mature polypeptides The term "mature polypeptide" refers to a polypeptide in its mature form after N-terminal processing (e.g., removal of the signal peptide).

[0051] Mature polypeptide coding sequence The term "mature polypeptide coding sequence" refers to a polynucleotide that encodes a mature polypeptide with xyloglucanase activity.

[0052] mutant The term "mutant" refers to a polynucleotide that encodes a variant.

[0053] Modification: In the context of the polypeptides of this invention, the term "modification" means altering one or more amino acids in the reference amino acid sequence (i.e., SEQ ID NO: 1, 2, or 3) by substitution with different amino acids, by insertion of amino acids, or by deletion (preferably by at least one deletion). The terms "modification," "alteration," and "mutation" are used interchangeably and have the same meaning and purpose.

[0054] Nucleic acid constructsThe term "nucleic acid construct" refers to a single-stranded or double-stranded nucleic acid molecule that is isolated from a naturally occurring gene, modified in a way that does not normally exist in nature to contain segments of nucleic acid, or is synthesized and contains one or more control sequences.

[0055] Operable connection: The term "operably linked" refers to 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 the expression of the coding sequence.

[0056] Parental lineage or parental xyloglucanase The term "parent" or "parent xyloglucanase" refers to any polypeptide having xyloglucanase activity, modified (e.g., one or more substitutions, one or more insertions, one or more deletions, and / or one or more truncations) to produce the xyloglucanase variant of the present invention. The parent can be a naturally occurring (wild-type) polypeptide or a variant or fragment thereof. The parent can be a naturally occurring (wild-type) polypeptide, such as the enzyme of SEQ ID NO: 1, or a polypeptide having at least 60%, more preferably at least 65%, more preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, even more preferably at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity with it. The parent polypeptide can also be a variant of a naturally occurring polypeptide whose amino acid sequence has been modified or altered, such as the polypeptides of SEQ ID NO: 2 or SEQ ID NO: 3 herein. Parents can also be allele variants, which are polypeptides encoded by any of two or more alternative forms of a gene occupying the same chromosomal locus.

[0057] PurifiedThe term "purified" means nucleic acids or peptides that are substantially free of other components, as determined by analytical techniques well known in the art (e.g., in electrophoresis gels, chromatographic eluates, and / or media subjected to density gradient centrifugation, where purified peptides or nucleic acids form discrete bands). Purified nucleic acids or peptides are at least about 50% pure, and typically at least about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, about 99.5%, about 99.6%, about 99.7%, about 99.8%, or more pure (e.g., molar weight percentage). In a relevant sense, a composition is enriched when there is a significant increase in the concentration of molecules after the application of purification or enrichment techniques. The term "enrichment" means that a compound, peptide, cell, nucleic acid, amino acid, or other specified material or component is present in the composition at a relative or absolute concentration higher than that of the starting composition.

[0058] Reorganization When used to refer to cells, nucleic acids, proteins, or vectors, the term "recombinant" means that the protein has been modified from its natural state. Thus, for example, recombinant cells express genes not found in the natural (non-recombinant) form of the cell, or express natural genes at different levels or under different conditions compared to those found in nature. The difference between recombinant nucleic acids and their natural sequences lies in the operative linking of one or more nucleotides and / or a foreign sequence (e.g., a foreign promoter in an expression vector). The difference between recombinant proteins and their natural sequences may lie in the fusion of one or more amino acids and / or a foreign sequence. A vector containing nucleic acids encoding a polypeptide is a recombinant vector. The term "recombinant" is synonymous with "genetically modified" and "transgenic."

[0059] Sequence identity The degree of association between two amino acid sequences or two nucleotide sequences is described by the parameter "sequence identity".

[0060] For the purposes of this invention, the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. [Journal of Molecular Biology] 48: 443-453) is used to determine sequence identity between two amino acid sequences. This algorithm is implemented in the Niedle procedure using the EMBOSS software package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. [Trends in Genetics] 16: 276-277) (preferably version 5.0.0 or later). The parameters used are a vacancy opening penalty of 10, a vacancy extension penalty of 0.5, and an EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of the "longest identity" marked by Niedle (obtained using the non-simplified (-nobrief) option) is used as the identity percentage and calculated as follows:

[0061] (Identical residues x 100) / (Alignment length - Total number of vacancies in the alignment)

[0062] For the purposes of this invention, the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, ibid.) is used to determine sequence identity between two deoxyribonucleotide sequences. This algorithm is implemented in the Niedle procedure of the EMBOSS software package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, ibid.) (preferably version 5.0.0 or later). The parameters used are a vacancy opening penalty of 10, a vacancy extension penalty of 0.5, and an EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. The output of the "longest identity" marked by Niedle (obtained using the non-simplified (-nobrief) option) is used as the identity percentage and calculated as follows:

[0063] (Identical deoxyribonucleotides x 100) / (Alignment length – total number of vacancies in the alignment)

[0064] subsequence The term "subsequence" refers to a polynucleotide in which one or more nucleotides are deleted from the 5' and / or 3' end of the coding sequence of a mature polypeptide; wherein the subsequence encodes a fragment having xyloglucanase activity.

[0065] textile The term "textiles" means any textile material, including yarns, yarn intermediates, fibers, nonwoven materials, natural materials, synthetic materials, and any other textile material, fabrics made from these materials, and products made from these fabrics (e.g., clothing and other articles). The textile or fabric can be in the form of knitted fabrics, woven fabrics, denim, nonwoven fabrics, felt, yarns, and terry cloth. The textile can be cellulose-based, such as natural cellulose products including cotton, flax / linen, jute, ramie, sisal, or coconut fiber, or man-made cellulose products (e.g., derived from wood pulp), including viscose / rayon, cellulose acetate fiber (tricell), lyocell, or blends thereof. Textiles or fabrics may also be non-cellulose-based, such as natural polyamides including wool, camel hair, cashmere, mohair, rabbit hair, and silk, or synthetic polymers such as nylon, aramid, polyester, acrylate, polypropylene, and spandex / elastane, or blends thereof, as well as blends of cellulose-based and non-cellulose-based fibers. Examples of blends are blends of cotton and / or rayon / viscose fibers with one or more accompanying materials such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers) and / or cellulose-containing fibers (e.g., rayon / viscose fibers, ramie, flax / linen, jute, cellulose acetate fibers, lyocell fibers). Fabrics can be conventional washable garments, such as stained home clothes. When the term fabric or garment is used, the broad term textiles is intended to also be included.

[0066] variants The term "variant" refers to a polypeptide having xyloglucanase activity that contains altered activity at one or more (e.g., several) positions while retaining the parental activity. Substitution means replacing an amino acid occupying a position with a different amino acid. The variants of the present invention have at least 20%, for example, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, 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 at least 100% of the xyloglucanase activity of the polypeptide of SEQ ID NO: 1.

[0067] detergent The term "washing liquid" refers to an aqueous solution containing a detergent composition in a diluted form, such as, but not limited to, a detergent solution containing a laundry detergent composition in a diluted form, for example, a washing liquid in the process of washing clothes.

[0068] Whiteness The term "whiteness" is defined in this document as a broad term with different meanings in different fields and for different customers. Loss of whiteness can be attributed, for example, to ashing, yellowing, or removal of optical brighteners / toners. Ashing and yellowing can be attributed to dirt redeposition, body dirt, coloring from, for example, iron and copper ions, or dye transfer. Whiteness can include one or more issues from the following list: the effect of colorants or dyes; incomplete stain removal (e.g., body dirt, sebum, etc.); redeposition (ashing, yellowing, or other discoloration of an object) (re-associating removed dirt with other parts of the textile (soiled or unsoiled)); chemical changes in the textile during application; and clarification or brightening of color.

[0069] wild type When referring to amino acid or nucleic acid sequences, the term "wild-type" means that the amino acid or nucleic acid sequence is a naturally occurring or naturally occurring sequence. As used herein, the term "naturally occurring" refers to any substance found in nature (e.g., protein, amino acid, or nucleic acid sequences). Conversely, the term "non-naturally occurring" refers to any substance not found in nature (e.g., recombinant nucleic acid and protein sequences produced in a laboratory, or modifications of wild-type sequences).

[0070] xylo-glucanase activity The term "xyglucanase activity" is defined herein as the enzyme-catalyzed hydrolysis of xyglucan. This reaction involves the endo-hydrolysis of the 1,4-β-D-glucosidic bond in the xyglucanase. For the purposes of this invention, xyglucanase activity is determined using AZCL-xyglucan (from Megazyme) as the reaction substrate. This assay can be performed in several ways, for example, as described in Example 2 of this application, or as described in WO 01 / 62903. One unit of xyglucanase activity (XyloU) is defined with reference to the assay method described in WO 01 / 62903, page 60, lines 3-17.

[0071] Variant Naming Conventions

[0072] For the purposes of this invention, the amino acid sequence of the xyloglucanase disclosed in SEQ ID NO: 1 is used to determine the corresponding amino acid residues in another xyloglucanase. The amino acid sequence of the other xyloglucanase is compared with the amino acid sequence of the xyloglucanase disclosed in SEQ ID NO: 1, and based on this comparison, the amino acid position number corresponding to any amino acid residue in the amino acid sequence of the xyloglucanase disclosed in SEQ ID NO: 1 can be determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. [Journal of Molecular Biology] 48: 443-453), which is implemented in the Needleman program of the EMBOSS software package (EMBOSS: The European Molecular Biology OpenSoftware Suite, Rice et al., 2000, Trends Genet. [Trends in Genetics] 16: 276-277) (preferably version 5.0.0 or later). The parameters used are an open space penalty of 10, an open space extension penalty of 0.5, and an EBLOSUM62 (the EMBOSS version of BLOSUM62) replacement matrix.

[0073] In describing variations of the invention, the nomenclature described below has been adjusted for ease of reference. Accepted IUPAC single-letter or three-letter amino acid abbreviations are used.

[0074] replace For amino acid substitutions, the following nomenclature is used: original amino acid, position, substituted amino acid. Accordingly, the substitution of threonine at position 226 with alanine is represented as "Thr226Ala" or "T226A". Multiple mutations are separated by a plus sign ("+"), for example, "Gly205Arg + Ser411Phe" or "G205R + S411F" represent the substitution of glycine (G) and serine (S) at positions 205 and 411 with arginine I and phenylalanine (F), respectively.

[0075] Missing For amino acid deletions, use the following nomenclature: original amino acid, position, Accordingly, the deletion of glycine at position 195 will be represented as "Gly195". "or "G195 Multiple missing items are separated by a plus sign ("+"), for example, "Gly195". + Ser411 "or "G195 + S411 ".

[0076] insert. For amino acid insertions, the following nomenclature is used: original amino acid, position, original amino acid, inserted amino acid. Accordingly, inserting lysine after glycine at position 195 is represented as "Gly195GlyLys" or "G195GK". Insertions of multiple amino acids are represented as [original amino acid, position, original amino acid, inserted amino acid #1, inserted amino acid #2; etc.]. For example, inserting lysine and alanine after glycine at position 195 is represented as "Gly195GlyLysAla" or "G195GKA".

[0077] In such cases, the inserted amino acid residues are numbered by adding lowercase letters to the position numbers of the amino acid residues preceding them. In the example above, the sequence would therefore be:

[0078]

[0079] Multiple changes Variants containing multiple changes are separated by a plus sign ("+"), for example, "Arg170Tyr +Gly195Glu" or "R170Y + G195E" means that arginine and glycine at positions 170 and 195 are replaced by tyrosine and glutamic acid, respectively.

[0080] Different changes Where different changes can be introduced at a single position, these changes are separated by commas. For example, "Arg170Tyr,Glu" represents the substitution of arginine at position 170 with either tyrosine or glutamic acid. Therefore, "Tyr167Gly,Ala + Arg170Gly,Ala" indicates the following variant:

[0081] “Tyr167Gly + Arg170Gly”, “Tyr167Gly + Arg170Ala”, “Tyr167Ala + Arg170Gly”, and “Tyr167Ala + Arg170Ala”. Detailed Implementation

[0082] Xyloglucanase variants

[0083] This invention relates to isolated xyloglucanase variants that contain alterations at one or more positions corresponding to positions selected from the group consisting of: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238 of the polypeptide of SEQ ID NO: 1. 240, 243, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, of which this variant has xyloglucanase activity. Preferably, the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3, and wherein the variant has xyloglucanase activity.

[0084] This invention relates to isolated xyloglucanase variants that contain a substitution at position 129T corresponding to the polypeptide of SEQ ID NO: 2, wherein the variant possesses xyloglucanase activity. Preferably, the variant has at least 99% but less than 100% sequence identity with the polypeptide of SEQ ID NO: 2. In particular, this invention relates to isolated xyloglucanase variants that comprise or consist of the polypeptide of SEQ ID NO: 3.

[0085] In the embodiments, the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% but less than 100% sequence identity with the parent xylo-glucanase.

[0086] In another embodiment, the variant has at least 60% but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99% but less than 100%.

[0087] In another embodiment, the variant has at least 60% but less than 100% sequence identity with the polypeptide of SEQ ID NO: 2, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99% but less than 100%.

[0088] In another embodiment, the variant has at least 60% but less than 100% sequence identity with the polypeptide of SEQ ID NO: 3, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99% but less than 100%.

[0089] In one aspect, the number of changes is 1-50, such as 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10, or 1-5, such as 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, or 50 changes.

[0090] In one respect, the number of substitutions is 1-50, for example 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5, such as 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 substitutions.

[0091] In one aspect, the number of missing items is 1-50, such as 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10, or 1-5, such as 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, or 50 missing items.

[0092] In one aspect, the substituted amino acid residue differs from the naturally occurring amino acid residue at that position. In one embodiment, the substitution is selected from the group consisting of A, C, D, E, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W, and Y, provided that the substituted amino acid residue differs from the naturally occurring amino acid residue at that position.

[0093] In one embodiment, the xyloglucanase variant of the present invention is an isolated variant.

[0094] On the other hand, the variant contains changes at two or more positions corresponding to the positions selected from the group consisting of: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0095] On the other hand, the variant contains changes at three or more positions corresponding to the group selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0096] On the other hand, the variant contains changes at four or more positions corresponding to the group selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0097] On the other hand, the variant contains changes at five or more positions corresponding to the group selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0098] On the other hand, the variant contains changes at six or more positions corresponding to the group selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0099] On the other hand, the variant contains changes at seven or more positions corresponding to the group selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0100] On the other hand, the variant contains changes at eight or more positions corresponding to the group selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0101] On the other hand, the variant contains changes at nine or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0102] On the other hand, the variant contains changes at ten or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0103] On the other hand, the variant contains changes at eleven or more positions corresponding to the group selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0104] On the other hand, the variant contains changes at twelve or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0105] On the other hand, the variant contains changes at thirteen or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0106] On the other hand, the variant contains changes at fourteen or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0107] On the other hand, the variant contains changes at fifteen or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0108] On the other hand, the variant contains changes at sixteen or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0109] On the other hand, the variant contains changes at seventeen or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0110] On the other hand, the variant contains changes at eighteen or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0111] On the other hand, the variant contains changes at nineteen or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0112] On the other hand, the variant contains changes at twenty or more positions corresponding to the groups selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0113] On the other hand, the variant contains changes at each position corresponding to the group selected from the following components: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240, 24 of the polypeptide of SEQ ID NO: 1. 3, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0114] On the other hand, the variant contains changes at each position corresponding to the group selected from the following: 111, 123, 129, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240 of the polypeptide of SEQ ID NO: 1. 243, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0115] On the other hand, the variant contains changes at each position corresponding to the group selected from the following: 111, 123, 129, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240 of the polypeptide of SEQ ID NO: 2. 243, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0116] In one respect, the variant includes one or more of the following changes at the location corresponding to the following positions: SEQ ID NO: The polypeptide of 1 contains P111, S123, V159, S256, I294, K8, K18, R20, A41, A42, S76, Q82, A83, K87, S94, G103, T104, Y105, A118, N121, Q125, E126, S127, N136, Q137, F146, Q147, L148, L152, N153, N155, F165, N168, K169, A177, L184, A189, V203, K206, D210, R211, S214, K217, V219, K220, A226, G237, A238, K240, Q 243, T244, W248, V251, K252, R267, Q271, R276, A289, R295, N298, V300, N302, K322, Q329, P339, K347, R347, K353, R353, N383, D384, K392, K394, D395, P395, S402, K414, T427, V431, K445, L447, A459, I473, S474, K476, K482, K488, E489, A491, P492, Y503, and V505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0117] In one respect, the variant includes one or more of the following changes at the location corresponding to the following positions: SEQ ID NO: The polypeptide of type 1 contains P111, S123, V159, S256, I294, K8, K18, R20, A41, A42, S76, Q82, A83, K87, S94, G103, T104, Y105, A118, N121, Q125, E126, S127, K129, N136, Q137, F146, Q147, L148, L152, N153, N155, F165, N168, K169, A177, L184, A189, V203, K206, D210, R211, S214, K217, V219, K220, A226, G237, A238, and K24. 0, Q243, T244, W248, V251, K252, R267, Q271, R276, A289, R295, N298, V300, N302, K322, Q329, P339, K347, R347, K353, R353, N383, D384, K392, K394, D395, P395, S402, K414, T427, V431, K445, L447, A459, I473, S474, K476, K482, K488, E489, A491, P492, Y503, and V505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO:1, SEQ ID NO:2, or SEQ ID NO:3 have at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100% sequence identity.

[0118] In one respect, the variant includes one or more of the following changes at the location corresponding to the following positions: SEQ ID NO: The polypeptide of type 2 contains P111, S123, V159, S256, I294, K8, K18, R20, A41, A42, S76, Q82, A83, K87, S94, G103, T104, Y105, A118, N121, Q125, E126, S127, A129, N136, Q137, F146, Q147, L148, L152, N153, N155, F165, N168, K169, A177, L184, A189, V203, K206, D210, R211, S214, K217, V219, K220, A226, G237, A238, and K24. 0, Q243, T244, W248, V251, K252, R267, Q271, R276, A289, R295, N298, V300, N302, K322, Q329, P339, K347, R347, K353, R353, N383, D384, K392, K394, D395, P395, S402, K414, T427, V431, K445, L447, A459, I473, S474, K476, K482, K488, E489, A491, P492, Y503, and V505, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ The polypeptides of SEQ ID NO:1, SEQ ID NO:2, or SEQ ID NO:3 have at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100% sequence identity.

[0119] In one aspect, the variant contains one or more of the following changes at positions corresponding to the following locations: P111Q, S123P, V159M, S256E, S256Q, I294E, I294Q, K8E, K8R, K18E, R20K, A41L, A41E, A41R, A42V, S76E, Q82E, A83E, K87E, S94R, G103V, T104G, T104 of the polypeptide of SEQ ID NO: 1. R, Y105E, A118K, N121E, Q125F, Q125K, Q125L, Q125P, Q125S, E126P, S127H, S 127L, S127W, S127D, N136D, Q137E, Q137K, F146D, Q147G, Q147K, L148P, L152 , L152D, L152E, L152P, N153E, N155D, N155E, F165H, N168R, K169E, K169R, A17 7G, L184M, A189G, V203T, K206E, K206R, D210H, D210R, R211K, S214Q, K217R, K 217T, V219A, V219T, K220R, A226D, A226K, G237M, A238S, A238T, K240F, K240L , Q243E, T244E, T244R, W248V, V251E, K252E, R267C, R267H, R267K, Q271D, Q27 1E, R276K, A289T, R295K, N298D, V300L, N302H, K322E, Q329E, P339S, K347E, K 347R, K353R, N383E, N383Q, D384G, K392E, K394R, D395P, S402Q, K414E, T427V V431E, K445E, L447M, A459P, I473T, S474E, K476R, K482R, K488T, E489K, E489R, A491E, A491V, P492D, Y503L, Y503V, and V505L, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0120] In one aspect, the variant contains one or more of the following changes at positions corresponding to the following locations: P111Q, S123P, V159M, S256E, S256Q, I294E, I294Q, K8E, K8R, K18E, R20K, A41L, A41E, A41R, A42V, S76E, Q82E, A83E, K87E, S94R, G103V, T104G, T104R, Y105 of the polypeptide of SEQ ID NO: 1. E, A118K, N121E, Q125F, Q125K, Q125L, Q125P, Q125S, E126P, S127H, S127L, S127 W, S127D, K129A, K129T, N136D, Q137E, Q137K, F146D, Q147G, Q147K, L148P, L152 , L152D, L152E, L152P, N153E, N155D, N155E, F165H, N168R, K169E, K169R, A17 7G, L184M, A189G, V203T, K206E, K206R, D210H, D210R, R211K, S214Q, K217R, K 217T, V219A, V219T, K220R, A226D, A226K, G237M, A238S, A238T, K240F, K240L , Q243E, T244E, T244R, W248V, V251E, K252E, R267C, R267H, R267K, Q271D, Q27 1E, R276K, A289T, R295K, N298D, V300L, N302H, K322E, Q329E, P339S, K347E, K 347R, K353R, N383E, N383Q, D384G, K392E, K394R, D395P, S402Q, K414E, T427V V431E, K445E, L447M, A459P, I473T, S474E, K476R, K482R, K488T, E489K, E489R, A491E, A491V, P492D, Y503L, Y503V, and V505L, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0121] In one aspect, the variant contains one or more of the following changes at positions corresponding to the following locations: P111Q, S123P, V159M, S256E, S256Q, I294E, I294Q, K8E, K8R, K18E, R20K, A41L, A41E, A41R, A42V, S76E, Q82E, A83E, K87E, S94R, G103V, T104G, T104R, Y of the polypeptide of SEQ ID NO: 2. 105E, A118K, N121E, Q125F, Q125K, Q125L, Q125P, Q125S, E126P, S127H, S127L , S127W, S127D, A129T, N136D, Q137E, Q137K, F146D, Q147G, Q147K, L148P, L152 , L152D, L152E, L152P, N153E, N155D, N155E, F165H, N168R, K169E, K169R, A17 7G, L184M, A189G, V203T, K206E, K206R, D210H, D210R, R211K, S214Q, K217R, K 217T, V219A, V219T, K220R, A226D, A226K, G237M, A238S, A238T, K240F, K240L , Q243E, T244E, T244R, W248V, V251E, K252E, R267C, R267H, R267K, Q271D, Q27 1E, R276K, A289T, R295K, N298D, V300L, N302H, K322E, Q329E, P339S, K347E, K 347R, K353R, N383E, N383Q, D384G, K392E, K394R, D395P, S402Q, K414E, T427V V431E, K445E, L447M, A459P, I473T, S474E, K476R, K482R, K488T, E489K, E489R, A491E, A491V, P492D, Y503L, Y503V, and V505L, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0122] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 8. In another aspect, the amino acid at the position corresponding to position 8 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substituted K8R or K8E of the polypeptide of SEQ ID NO:1.

[0123] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 18. In another aspect, the amino acid at the position corresponding to position 18 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K18E of the polypeptide of SEQ ID NO: 1.

[0124] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 20. In another aspect, the amino acid at the position corresponding to position 20 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substituted R20K of the polypeptide of SEQ ID NO: 1.

[0125] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 41. In another aspect, the amino acid at the position corresponding to position 41 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substitution A41E, A41L, or A41R of the polypeptide of SEQ ID NO: 1.

[0126] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 42. In another aspect, the amino acid at the position corresponding to position 42 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted A42V of the polypeptide of SEQ IDNO: 1.

[0127] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 76. In another aspect, the amino acid at the position corresponding to position 76 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution S76E of the polypeptide of SEQ ID NO: 1.

[0128] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 82. In another aspect, the amino acid at the position corresponding to position 82 is substituted with Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution Q82E of the polypeptide of SEQ ID NO: 1.

[0129] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 83. In another aspect, the amino acid at the position corresponding to position 83 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the A83E substitution of the polypeptide of SEQ IDNO: 1.

[0130] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 87. In another aspect, the amino acid at the position corresponding to position 87 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K87E of the polypeptide of SEQ ID NO: 1.

[0131] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 94. In another aspect, the amino acid at the position corresponding to position 94 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution S94R of the polypeptide of SEQ ID NO: 1.

[0132] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 103. In another aspect, the amino acid at the position corresponding to position 103 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably Val. In another aspect, the variant contains or is composed of the substituted G103V of the polypeptide of SEQ ID NO: 1.

[0133] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 104. In another aspect, the amino acid at the position corresponding to position 104 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Gly or Arg. In another aspect, the variant contains or is composed of the substitution T104G or T104R of the polypeptide of SEQ ID NO: 1.

[0134] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 105. In another aspect, the amino acid at the position corresponding to position 105 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted Y105E of the polypeptide of SEQ ID NO: 1.

[0135] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 111. In another aspect, the amino acid at the position corresponding to position 111 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted P111Q of the polypeptide of SEQ ID NO: 1.

[0136] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 118. In another aspect, the amino acid at the position corresponding to position 118 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted A118K of the polypeptide of SEQ ID NO: 1.

[0137] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 121. In another aspect, the amino acid at the position corresponding to position 121 is substituted with Ala, Arg, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted N121E of the polypeptide of SEQ ID NO: 1.

[0138] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 123. In another aspect, the amino acid at the position corresponding to position 123 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution S123P of the polypeptide of SEQ ID NO: 1.

[0139] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 125. In another aspect, the amino acid at the position corresponding to position 125 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably Phe, Leu, or Ser, and most preferably Ser. In another aspect, the variant contains or is composed of the substitution of the polypeptide of SEQ ID NO: 1 with Q125F, Q125K, Q125L, Q125P, Q125S, most preferably Q125S.

[0140] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 126. In another aspect, the amino acid at the position corresponding to position 126 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted E126P of the polypeptide of SEQ ID NO: 1.

[0141] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 127. In another aspect, the amino acid at the position corresponding to position 127 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substitution S127H, S127L, S127W, or S127D of the polypeptide of SEQ ID NO: 1.

[0142] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 136. In another aspect, the amino acid at the position corresponding to position 136 is substituted with Ala, Arg, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted N136D of the polypeptide of SEQ ID NO: 1.

[0143] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 137. In another aspect, the amino acid at the position corresponding to position 137 is substituted with Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substitution Q137E or Q137K of the polypeptide of SEQ ID NO: 1.

[0144] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 146. In another aspect, the amino acid at the position corresponding to position 146 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution F146D of the polypeptide of SEQ ID NO: 1.

[0145] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 147. In another aspect, the amino acid at the position corresponding to position 147 is substituted with Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted Q147G or Q147K of the polypeptide of SEQ ID NO: 1.

[0146] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 148. In another aspect, the amino acid at the position corresponding to position 148 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted L148P of the polypeptide of SEQ ID NO: 1.

[0147] On the other hand, the variant contains a substitution or deletion or is composed of at the position corresponding to position 152. On the other hand, the amino acid at the position corresponding to position 152 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. On the other hand, the variant contains a substitution or deletion of the polypeptide of SEQ ID NO: 1, either L152D, L152E, L152P, or L152. Or composed of.

[0148] In another aspect, the variant contains or is composed of a substitution at position 153. In another aspect, the amino acid at position 153 is substituted with Ala, Arg, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted N153E of the polypeptide of SEQ ID NO: 1.

[0149] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 155. In another aspect, the amino acid at the position corresponding to position 155 is substituted with Ala, Arg, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substitution N155D or N155E of the polypeptide of SEQ ID NO: 1.

[0150] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 159. In another aspect, the amino acid at the position corresponding to position 159 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted V159M of the polypeptide of SEQ ID NO: 1.

[0151] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 165. In another aspect, the amino acid at the position corresponding to position 165 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution F165H of the polypeptide of SEQ IDNO: 1.

[0152] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 168. In another aspect, the amino acid at the position corresponding to position 168 is substituted with Ala, Arg, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted N168R of the polypeptide of SEQ ID NO: 1.

[0153] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 169. In another aspect, the amino acid at the position corresponding to position 169 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substituted K169E or K169R of the polypeptide of SEQ ID NO: 1.

[0154] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 177. In another aspect, the amino acid at the position corresponding to position 177 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted A177G of the polypeptide of SEQ ID NO: 1.

[0155] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 184. In another aspect, the amino acid at the position corresponding to position 184 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted L184M of the polypeptide of SEQ ID NO: 1.

[0156] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 189. In another aspect, the amino acid at the position corresponding to position 189 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted A189G of the polypeptide of SEQ ID NO: 1.

[0157] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 203. In another aspect, the amino acid at the position corresponding to position 203 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted V203T of the polypeptide of SEQ ID NO: 1.

[0158] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 206. In another aspect, the amino acid at the position corresponding to position 206 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substituted K206E or K206R of the polypeptide of SEQ IDNO: 1.

[0159] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 210. In another aspect, the amino acid at the position corresponding to position 210 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution D210H or D210R of the polypeptide of SEQ ID NO: 1.

[0160] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 211. In another aspect, the amino acid at the position corresponding to position 211 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted R211K of the polypeptide of SEQ ID NO: 1.

[0161] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 214. In another aspect, the amino acid at the position corresponding to position 214 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution S214Q of the polypeptide of SEQ ID NO: 1.

[0162] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 217. In another aspect, the amino acid at the position corresponding to position 217 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substituted K217R or K217T of the polypeptide of SEQ ID NO: 1.

[0163] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 219. In another aspect, the amino acid at the position corresponding to position 219 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substitution V219A or V219T of the polypeptide of SEQ ID NO: 1.

[0164] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 220. In another aspect, the amino acid at the position corresponding to position 220 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K220R of the polypeptide of SEQ ID NO: 1.

[0165] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 226. In another aspect, the amino acid at the position corresponding to position 226 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution A226D or A226K of the polypeptide of SEQ ID NO: 1.

[0166] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 237. In another aspect, the amino acid at the position corresponding to position 237 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted G237M of the polypeptide of SEQ ID NO: 1.

[0167] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 238. In another aspect, the amino acid at the position corresponding to position 238 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted A238S or A238T of the polypeptide of SEQ ID NO: 1.

[0168] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 240. In another aspect, the amino acid at the position corresponding to position 240 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substituted K240L or K240F polypeptide of SEQ ID NO: 1.

[0169] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 243. In another aspect, the amino acid at the position corresponding to position 243 is substituted with Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution Q243E of the polypeptide of SEQ ID NO: 1.

[0170] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 244. In another aspect, the amino acid at the position corresponding to position 244 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution T244E or T244R of the polypeptide of SEQ ID NO: 1.

[0171] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 248. In another aspect, the amino acid at the position corresponding to position 248 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution W248V of the polypeptide of SEQ ID NO: 1.

[0172] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 251. In another aspect, the amino acid at the position corresponding to position 251 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution V251E of the polypeptide of SEQ ID NO: 1.

[0173] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 252. In another aspect, the amino acid at the position corresponding to position 252 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K252E of the polypeptide of SEQ IDNO: 1.

[0174] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 256. In another aspect, the amino acid at the position corresponding to position 256 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution S256E or S256Q of the polypeptide of SEQ ID NO: 1.

[0175] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 267. In another aspect, the amino acid at the position corresponding to position 267 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substitution R267C, R267H, or R267K of the polypeptide of SEQ ID NO: 1.

[0176] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 271. In another aspect, the amino acid at the position corresponding to position 271 is substituted with Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substitution Q271D or Q271E of the polypeptide of SEQ ID NO: 1.

[0177] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 276. In another aspect, the amino acid at the position corresponding to position 276 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted R276K of the polypeptide of SEQ ID NO: 1.

[0178] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 289. In another aspect, the amino acid at the position corresponding to position 289 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted A289T of the polypeptide of SEQ ID NO: 1.

[0179] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 294. In another aspect, the amino acid at the position corresponding to position 294 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution I294E or I294Q of the polypeptide of SEQ ID NO: 1.

[0180] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 295. In another aspect, the amino acid at the position corresponding to position 295 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted R295K of the polypeptide of SEQ ID NO: 1.

[0181] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 298. In another aspect, the amino acid at the position corresponding to position 298 is substituted with Ala, Arg, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted N298D of the polypeptide of SEQ ID NO: 1.

[0182] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 300. In another aspect, the amino acid at the position corresponding to position 300 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted V300L of the polypeptide of SEQ ID NO: 1.

[0183] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 302. In another aspect, the amino acid at the position corresponding to position 302 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted N302H of the polypeptide of SEQ ID NO: 1.

[0184] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 322. In another aspect, the amino acid at the position corresponding to position 322 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K322E of the polypeptide of SEQ ID NO: 1.

[0185] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 329. In another aspect, the amino acid at the position corresponding to position 329 is substituted with Ala, Arg, Asn, Asp, Cys, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution Q329E of the polypeptide of SEQ ID NO: 1.

[0186] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 339. In another aspect, the amino acid at the position corresponding to position 339 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted P339S of the polypeptide of SEQ ID NO: 1.

[0187] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 347. In another aspect, the amino acid at the position corresponding to position 347 is substituted with Ala, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substituted K347E or K347R of the polypeptide of SEQ ID NO: 1.

[0188] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 353. In another aspect, the amino acid at the position corresponding to position 353 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K353R of the polypeptide of SEQ ID NO: 1.

[0189] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 383. In another aspect, the amino acid at the position corresponding to position 383 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution N383E or N383Q of the polypeptide of SEQ ID NO: 1.

[0190] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 384. In another aspect, the amino acid at the position corresponding to position 384 is substituted with Ala, Arg, Asn, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution D384G of the polypeptide of SEQ ID NO: 1.

[0191] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 392. In another aspect, the amino acid at the position corresponding to position 392 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K392E of the polypeptide of SEQ ID NO: 1.

[0192] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 394. In another aspect, the amino acid at the position corresponding to position 394 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K394R of the polypeptide of SEQ ID NO: 1.

[0193] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 395. In another aspect, the amino acid at the position corresponding to position 395 is substituted with Ala, Arg, Asn, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted D395P of the polypeptide of SEQ ID NO: 1.

[0194] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 402. In another aspect, the amino acid at the position corresponding to position 402 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution S402Q of the polypeptide of SEQ ID NO: 1.

[0195] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 414. In another aspect, the amino acid at the position corresponding to position 414 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K414E of the polypeptide of SEQ ID NO: 1.

[0196] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 427. In another aspect, the amino acid at the position corresponding to position 427 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted T427V of the polypeptide of SEQ ID NO: 1.

[0197] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 431. In another aspect, the amino acid at the position corresponding to position 431 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, or Tyr, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution V431E of the polypeptide of SEQ ID NO: 1.

[0198] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 445. In another aspect, the amino acid at the position corresponding to position 445 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K445E of the polypeptide of SEQ ID NO: 1.

[0199] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 447. In another aspect, the amino acid at the position corresponding to position 447 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted L447M of the polypeptide of SEQ ID NO: 1.

[0200] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 459. In another aspect, the amino acid at the position corresponding to position 459 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted A459P of the polypeptide of SEQ ID NO: 1.

[0201] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 473. In another aspect, the amino acid at the position corresponding to position 473 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted I473T of the polypeptide of SEQ ID NO: 1.

[0202] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 474. In another aspect, the amino acid at the position corresponding to position 474 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution S474E of the polypeptide of SEQ ID NO: 1.

[0203] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 476. In another aspect, the amino acid at the position corresponding to position 476 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K476R of the polypeptide of SEQ ID NO: 1.

[0204] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 482. In another aspect, the amino acid at the position corresponding to position 482 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K482R of the polypeptide of SEQ ID NO: 1.

[0205] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 488. In another aspect, the amino acid at the position corresponding to position 488 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted K488T of the polypeptide of SEQ ID NO: 1.

[0206] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 489. In another aspect, the amino acid at the position corresponding to position 489 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution E489K or E489R of the polypeptide of SEQ ID NO: 1.

[0207] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 491. In another aspect, the amino acid at the position corresponding to position 491 is substituted with Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substitution A491E or A491V of the polypeptide of SEQ ID NO: 1.

[0208] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 492. In another aspect, the amino acid at the position corresponding to position 492 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Ser, Thr, Trp, Tyr, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of the substituted P492D of the polypeptide of SEQ ID NO: 1.

[0209] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 503. In another aspect, the amino acid at the position corresponding to position 503 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, or Val, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substituted Y503L or Y503V polypeptide of SEQ ID NO: 1.

[0210] In another aspect, the variant contains or is composed of a substitution at the position corresponding to position 505. In another aspect, the amino acid at the position corresponding to position 505 is substituted with Ala, Arg, Asn, Asp, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Phe, Pro, Ser, Thr, Trp, or Tyr, preferably substituted with Pro. In another aspect, the variant contains or is composed of a substituted V505L of the polypeptide of SEQ ID NO: 1.

[0211] In one aspect, the variant contains changes at positions corresponding to the group selected from the following components: E126P, S127H, T104G, Q125K, Q125P, Q125S, D395P, G103V, T104R, Q125L, A41E, A41R, Q125F, S127L, A226K, A41L, A226D, K394R, S127D, R211K, S123P, K488T, S256Q, K476R, K217R, Q271D, S214Q, L447M, K482R, K169R, L152D, R267K, L152E, D210R, L152 The following variants are listed: R295K, N155D, Q137K, N155E, Q147K, R276K, V203T, S94R, K18E, K252E, V219T, Q243E, K414E, K445E, V159M, K392E, Q82E, S76E, A83E, Q271E, S256E, I294E, Q329E, V431E, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0212] In one aspect, the variant contains changes at positions corresponding to the group selected from the following components: E126P, S127H, T104G, Q125K, Q125P, Q125S, K129T, K129A, D395P, G103V, T104R, Q125L, A41E, A41R, Q125F, S127L, A226K, A41L, A226D, K394R, S127D, R211K, S123P, K488T, S256Q, K476R, K217R, Q271D, S214Q, L447M, K482R, K169R, L152D, R267K, L152E, D210R, L152 The following variants are listed: R295K, N155D, Q137K, N155E, Q147K, R276K, V203T, S94R, K18E, K252E, V219T, Q243E, K414E, K445E, V159M, K392E, Q82E, S76E, A83E, Q271E, S256E, I294E, Q329E, and V431E, wherein the variant possesses xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0213] In one aspect, the variant contains changes at positions corresponding to the group selected from the following components: E126P, S127H, T104G, Q125K, Q125P, Q125S, A129T, D395P, G103V, T104R, Q125L, A41E, A41R, Q125F, S127L, A226K, A41L, A226D, K394R, S127D, R211K, S123P, K488T, S256Q, K476R, K217R, Q271D, S214Q, L447M, K482R, K169R, L152D, R267K, L152E, D210R, L152 The following variants are listed: R295K, N155D, Q137K, N155E, Q147K, R276K, V203T, S94R, K18E, K252E, V219T, Q243E, K414E, K445E, V159M, K392E, Q82E, S76E, A83E, Q271E, S256E, I294E, Q329E, V431E, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0214] In one aspect, the variant contains a change at a position corresponding to the group selected from the following: A118K + S123P, R267C + T427V, R20K + S123P, S123P + K206R, S123P + K347R, S123P + D395P, S123P + S127D, E489R + P492D, Y503L + V505L, Y503V + V505L, L184M + V219A of the polypeptide of SEQ ID NO: 1, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 1. The polypeptide of 3 has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0215] In one aspect, the variant contains a change at a position corresponding to the group selected from the following: A118K + S123P + K129T, R267C + T427V + K129T, R20K + S123P + K129T, S123P + K206R + K129T, S123P + K347R + K129T, S123P + D395P + K129T, S123P + S127D + K129T, E489R + P492D + K129T, Y503L + V505L + K129T, Y503V + V505L + K129T, L184M + V219A + K129T of the polypeptide of SEQ ID NO: 1, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 1 ... The polypeptide NO: 2 or SEQ ID NO: 3 has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0216] In one aspect, the variant contains a change at a position corresponding to the group selected from the following: A118K + S123P + A129T, R267C + T427V + A129T, R20K + S123P + A129T, S123P + K206R + A129T, S123P + K347R + A129T, S123P + D395P + A129T, S123P + S127D + A129T, E489R + P492D + A129T, Y503L + V505L + A129T, Y503V + V505L + A129T, L184M + V219A + A129T of the polypeptide of SEQ ID NO: 2, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2. The polypeptide NO: 2 or SEQ ID NO: 3 has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0217] In one aspect, the variant contains a change at a position corresponding to the group selected from the following: R20K + S123P + R211K, R20K + S123P + K220R, P111Q + S123P + V159M, K8E + P111Q + V159M, S94R + P111Q + V159M, P111Q + Q137K + V159M, P111Q + Q147K + V159M of the polypeptide of SEQ ID NO: 1, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 1. The polypeptide of 3 has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0218] In one aspect, the variant contains a change at a position corresponding to the group selected from the following: R20K+S123P+R211K+K129T, R20K+S123P+K220R+K129T, P111Q+S123P+V159M+K129T, K8E+P111Q+V159M+K129T, S94R+P111Q+V159M+K129T, P111Q+Q137K+V159M+K129T, P111Q+Q147K+V159M+K129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 1. The polypeptide of 3 has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0219] In one aspect, the variant contains a change at a position corresponding to the group selected from the following: R20K+S123P+R211K+A129T, R20K+S123P+K220R+A129T, P111Q+S123P+V159M+A129T, K8E+P111Q+V159M+A129T, S94R+P111Q+V159M+A129T, P111Q+Q137K+V159M+A129T, P111Q+Q147K+V159M+A129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0220] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following compositions: S123P + K347R + K353R + D395P, R20K + Y105E + S123P + R267K, R20K + Y105E + S123P + N136D, R20K + S123P + Q137K + Q147K, S94R + P111Q + S123P + V159M, K87E + P111Q + S123P + V159M, P111Q + S123P + V159M + S402Q, P111Q + Q147K + V159M + K220R, P111Q + V159M + K206E + I294Q, K8E + P111Q of the polypeptide of SEQ ID NO: 1. +N155D + V159M, P111Q + Q137K + Q147K + V159M, R20K + S123P + K220R + I294E, R20K + S123P + N155D + K220R, R20K + S123P + V203T + V219T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0221] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following compositions: S123P + K347R + K353R + D395P + K129T, R20K + Y105E + S123P + R267K + K129T, R20K + Y105E + S123P + N136D + K129T, R20K + S123P + Q137K + Q147K + K129T, S94R + P111Q + S123P + V159M + K129T, K87E + P111Q + S123P + V159M + K129T, P111Q + S123P + V159M + S402Q + K129T, P111Q + Q147K + V159M +K220R + K129T, P111Q + V159M + K206E + I294Q + K129T, K8E + P111Q + N155D +V159M + K129T, P111Q + Q137K + Q147K + V159M + K129T, R20K + S123P + K220R + I294E + K129T, R20K + S123P + N155D + K220R + K129T, R20K + S123P + V203T + V219T + K129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0222] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S123P + K347R + K353R + D395P + A129T, R20K + Y105E + S123P + R267K + A129T, R20K + Y105E + S123P + N136D + A129T, R20K + S123P + Q137K + Q147K + A129T, S94R + P111Q + S123P + V159M + A129T, K87E + P111Q + S123P + V159M + A129T, P111Q + S123P + V159M + S402Q + A129T, P111Q + Q147K + V159M +K220R + A129T, P111Q + V159M + K206E + I294Q + A129T, K8E + P111Q + N155D +V159M + A129T, P111Q + Q137K + Q147K + V159M + A129T, R20K + S123P + K220R + I294E + A129T, R20K + S123P + N155D + K220R + A129T, R20K + S123P + V203T + V219T + A129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0223] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S123P + R211K + K217R + S256Q + K488T, R20K + Y105E + S123P + Q147K + R267K, K87E + P111Q + S123P + V159M + S402Q, K87E + P111Q + V159M + I294Q + I473T, K8E + K18E + P111Q + V159M + K206E, R20K + P111Q + S123P + S127D + V159M, P111Q + V159M + K206E + I294Q + K347E, P111Q + Q137K + Q147K of the polypeptide of SEQ ID NO: 1. + V159M +K252E, P111Q + Q137K + Q147K + N155D + K252E, P111Q + Q137K + L152D + V203T +K217R, P111Q + S123P + Q137K + V159M + K488T, P111Q + S123P + Q137K + V159M +S256Q, K87E + P111Q + Q147K + L152D + V159M, R20K + A83E + S123P + K220R +S256E, R20K + A83E + S123P + K220R + K252E, R20K + Q82E + S123P + Q147K +K220R, R20K + A83E + S123P + K220R + S256Q, R20K + Q82E + S123P + N155D +K220R, R20K + S123P + V203T + K220R + K252E, R20K + A41L + Q82E + S123P +K220R, R20K + A42V + S76E + S123P + K220R, R20K + A42V + A83E + S123P + K220R, A83E + P111Q + S123P + V159M + K252E, wherein the variant has xyloglucanase activity and wherein the variant has at least 60% of the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.For example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0224] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S123P + R211K + K217R + S256Q + K488T + K129T, R20K + Y105E + S123P + Q147K + R267K + K129T, K87E + P111Q + S123P + V159M + S402Q + K129T, K87E + P111Q + V159M + I294Q + I473T + K129T, K8E + K18E + P111Q + V159M + K206E + K129T, R20K + P111Q + S123P + S127D + V159M + K129T, P111Q + V159M +K206E + I294Q + K347E + K129T, P111Q + Q137K + Q147K + V159M + K252E + K129T, P111Q + Q137K + Q147K + N155D + K252E + K129T, P111Q + Q137K + L152D + V203T +K217R + K129T, P111Q + S123P + Q137K + V159M + K488T + K129T, P111Q + S123P +Q137K + V159M + S256Q + K129T, K87E + P111Q + Q147K + L152D + V159M + K129T, R20K + A83E + S123P + K220R + S256E + K129T, R20K + A83E + S123P + K220R +K252E + K129T, R20K + Q82E + S123P + Q147K + K220R + K129T, R20K + A83E + S123P+ K220R + S256Q + K129T, R20K + Q82E + S123P + N155D + K220R + K129T, R20K +S123P + V203T + K220R + K252E + K129T, R20K + A41L + Q82E + S123P + K220R +K129T, R20K + A42V + S76E + S123P + K220R + K129T, R20K + A42V + A83E +S123P +K220R + K129T, A83E + P111Q + S123P + V159M + K252E + K129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0225] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S123P + R211K + K217R + S256Q + K488T + A129T, R20K + Y105E + S123P + Q147K + R267K + A129T, K87E + P111Q + S123P + V159M + S402Q + A129T, K87E + P111Q + V159M + I294Q + I473T + A129T, K8E + K18E + P111Q + V159M + K206E + A129T, R20K + P111Q + S123P + S127D + V159M + A129T, P111Q + V159M +K206E + I294Q + K347E + A129T, P111Q + Q137K + Q147K + V159M + K252E + A129T, P111Q + Q137K + Q147K + N155D + K252E + A129T, P111Q + Q137K + L152D + V203T +K217R + A129T, P111Q + S123P + Q137K + V159M + K488T + A129T, P111Q + S123P +Q137K + V159M + S256Q + A129T, K87E + P111Q + Q147K + L152D + V159M + A129T, R20K + A83E + S123P + K220R + S256E + A129T, R20K + A83E + S123P + K220R +K252E + A129T, R20K + Q82E + S123P + Q147K + K220R + A129T, R20K + A83E + S123P+ K220R + S256Q + A129T, R20K + Q82E + S123P + N155D + K220R + A129T, R20K +S123P + V203T + K220R + K252E + A129T, R20K + A41L + Q82E + S123P + K220R +A129T, R20K + A42V + S76E + S123P + K220R + A129T, R20K + A42V + A83E +S123P +K220R + A129T, A83E + P111Q + S123P + V159M + K252E + A129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0226] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: Y105E + A118K + S123P + K206R + K220R + R267K, A41L + P111Q + S123P + Q147K + V159M + V203T, A41L + P111Q + S123P + Q147K + V159M + K217R, P111Q + S123P + Q147K + V159M + I294Q + S402Q, P111Q + Q137K + Q147K + V159M + V203T + K217R, K87E + P111Q + L152D + V159M + V203T + I294Q, R20K + S76E + A83E + S123P + K220R + K252E, R20K + A42V + S123P + K220R + K252E + I294E, R20K +A83E + S123P + V203T + K220R + K252E, R20K + A42V + S76E + S123P + V203T +K220R, A83E + P111Q + S123P + V159M + S256E + I294E, Q82E + P111Q + S123P +V159M + S256E + I294E, Q82E + P111Q + S123P + Q147K + V159M + I294E, K87E +P111Q + S123P + V159M + K217T + I294E, A83E + P111Q + S123P + V159M + K240F + K252E, K87E + P111Q + S123P + V159M + S256Q + I294E, K87E + P111Q + S123P + V159M + K347E + N383E, Q82E + P111Q + S123P + N155D + S256E + I294E, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of type 3 has a content of at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, or at least 95%.For example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0227] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: Y105E + A118K + S123P + K206R + K220R + R267K + K129T, A41L + P111Q + S123P + Q147K + V159M + V203T + K129T, A41L + P111Q + S123P + Q147K + V159M + K217R + K129T, P111Q + S123P + Q147K + V159M + I294Q + S402Q + K129T, P111Q + Q137K + Q147K + V159M + V203T + K217R + K129T, K87E + P111Q + L152D +V159M + V203T + I294Q + K129T, R20K + S76E + A83E + S123P + K220R + K252E +K129T, R20K + A42V + S123P + K220R + K252E + I294E + K129T, R20K + A83E + S123P + V203T + K220R + K252E + K129T, R20K + A42V + S76E + S123P + V203T + K220R +K129T, A83E + P111Q + S123P + V159M + S256E + I294E + K129T, Q82E + P111Q +S123P + V159M + S256E + I294E + K129T, Q82E + P111Q + S123P + Q147K + V159M +I294E + K129T, K87E + P111Q + S123P + V159M + K217T + I294E + K129T, A83E +P111Q + S123P + V159M + K240F + K252E + K129T, K87E + P111Q + S123P + V159M +S256Q + I294E + K129T, K87E + P111Q + S123P + V159M + K347E + N383E + K129T, Q82E + P111Q + S123P + N155D+S256E+I294E+K129T,The variant possesses xyloglucanase activity and wherein the variant has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0228] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: SEQ ID NO: 2 peptides Y105E + A118K + S123P + K206R + K220R + R267K + A129T, A41L + P111Q + S123P + Q147K + V159M + V203T + A129T, A41L + P111Q + S123P + Q147K + V159M + K217R + A129T, P111Q + S123P + Q147K + V159M + I294Q + S402Q + A129T, P111Q + Q137K + Q147K + V159M + V203T + K217R + A129T, K87E + P111Q + L152D +V159M + V203T + I294Q + A129T, R20K + S76E + A83E + S123P + K220R + K252E +A129T, R20K + A42V + S123P + K220R + K252E + I294E + A129T, R20K + A83E + S123P + V203T + K220R + K252E + A129T, R20K + A42V + S76E + S123P + V203T + K220R +A129T, A83E + P111Q + S123P + V159M + S256E + I294E + A129T, Q82E + P111Q +S123P + V159M + S256E + I294E + A129T, Q82E + P111Q + S123P + Q147K + V159M +I294E + A129T, K87E + P111Q + S123P + V159M + K217T + I294E + A129T, A83E +P111Q + S123P + V159M + K240F + K252E + A129T, K87E + P111Q + S123P + V159M +S256Q + I294E + A129T, K87E + P111Q + S123P + V159M + K347E + N383E + A129T, Q82E + P111Q + S123P + N155D+S256E+I294E+A129T,The variant possesses xyloglucanase activity and wherein the variant has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0229] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: P111Q + S123P + Q137K + Q147K + V159M + S256Q + S402Q, A41L + P111Q + Q137K + V159M + N168R + Q271D + K488T, S76E + Q82E + K87E + P111Q + S123P + V159M + V203T, Q82E + P111Q + S123P + Q147K + V159M + S256E + I294E, K8E + Q82E + P111Q + S123P + V159M + S256E + I294E, Q82E + P111Q + S123P +V159M + K240F + S256E + I294E, Q82E + P111Q + S123P + V159M + G237M + V251E + I294E, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0230] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: P111Q + S123P + Q137K + Q147K + V159M + S256Q + S402Q + K129T, A41L + P111Q + Q137K + V159M + N168R + Q271D + K488T + K129T, S76E + Q82E + K87E + P111Q + S123P + V159M + V203T + K129T, Q82E + P111Q + S123P + Q147K + V159M + S256E + I294E + K129T, K8E + Q82E + P111Q + S123P + V159M + S256E + I294E + K129T, Q82E + P111Q + S123P + V159M + K240F + S256E + I294E + K129T, Q82E + P111Q + S123P + V159M + G237M + V251E + I294E + K129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0231] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: peptides of SEQ ID NO: 2, specifically P111Q + S123P + Q137K + Q147K + V159M + S256Q + S402Q + A129T, A41L + P111Q + Q137K + V159M + N168R + Q271D + K488T + A129T, S76E + Q82E + K87E + P111Q + S123P + V159M + V203T + A129T, Q82E + P111Q + S123P + Q147K + V159M + S256E + I294E + A129T, K8E + Q82E + P111Q + S123P + V159M + S256E + I294E + A129T, Q82E + P111Q + S123P + V159M + K240F + S256E + I294E + A129T, Q82E + P111Q + S123P + V159M + G237M + V251E + I294E + A129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0232] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + S256Q + S402Q, P111Q + S123P + Q137K + Q147K + N155D + S256Q + A289T + N302H, P111Q + S123P + Q137K + Q147K + V159M + K252E + S256Q + S402Q, P111Q + S123P + Q137K + Q147K + N155D + S256Q + I294E + S402Q, S76E + P111Q + S123P + Q137K + Q147K + V159M +S256Q + S402Q, K8R + P111Q + S123P + Q137K + Q147K + V159M + S256Q + S402Q, S123P + S127D + N136D + Q137K + Q147K + L152E + N153E + N155E, R20K + S123P +K169R + K217T + K240F + S256Q + R267H + I294E, Q82E + P111Q + S123P + V159M +V203T + G237M + S256E + I294E, Q82E + P111Q + S123P + N155D + K169R + G237M +S256E + I294E, Q82E + P111Q + S123P + Q137K + V159M + G237M + S256E + I294E, Q82E + P111Q + S123P + Q137K + V159M + K240F + S256E + I294E, Q82E + P111Q +S123P + Q147K + N155D + K240F + S256E + I294E, A83E + P111Q + S123P + Q147K +V159M + S256E + I294E + Q329E, Q82E + P111Q + S123P + V159M + K169R + S256E +I294E + V431E, A41L + Q82E + P111Q + S123P + V159M + S256E+ I294E + N383E, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0233] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + S256Q + S402Q + K129T, P111Q + S123P + Q137K + Q147K + N155D + S256Q + A289T + N302H + K129T, P111Q + S123P + Q137K + Q147K + V159M + K252E + S256Q + S402Q + K129T, P111Q + S123P + Q137K + Q147K + N155D + S256Q + I294E + S402Q + K129T, S76E +P111Q + S123P + Q137K + Q147K + V159M + S256Q + S402Q + K129T, K8R + P111Q +S123P + Q137K + Q147K + V159M + S256Q + S402Q + K129T, S123P + S127D + N136D +Q137K + Q147K + L152E + N153E + N155E + K129T, R20K + S123P + K169R + K217T +K240F + S256Q + R267H + I294E + K129T, Q82E + P111Q + S123P + V159M + V203T +G237M + S256E + I294E + K129T, Q82E + P111Q + S123P + N155D + K169R + G237M +S256E + I294E + K129T, Q82E + P111Q + S123P + Q137K + V159M + G237M + S256E +I294E, Q82E + P111Q + S123P + Q137K + V159M + K240F + S256E + I294E + K129T, Q82E + P111Q + S123P + Q147K + N155D + K240F + S256E + I294E + K129T, A83E +P111Q + S123P + Q147K + V159M + S256E + I294E + Q329E +K129T, Q82E + P111Q + S123P + V159M + K169R + S256E + I294E + V431E + K129T, A41L + Q82E + P111Q + S123P + V159M + S256E + I294E + N383E + K129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0234] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + S256Q + S402Q + A129T, P111Q + S123P + Q137K + Q147K + N155D + S256Q + A289T + N302H + A129T, P111Q + S123P + Q137K + Q147K + V159M + K252E + S256Q + S402Q + A129T, P111Q + S123P + Q137K + Q147K + N155D + S256Q + I294E + S402Q + A129T, S76E +P111Q + S123P + Q137K + Q147K + V159M + S256Q + S402Q + A129T, K8R + P111Q +S123P + Q137K + Q147K + V159M + S256Q + S402Q + A129T, S123P + S127D + N136D +Q137K + Q147K + L152E + N153E + N155E + A129T, R20K + S123P + K169R + K217T +K240F + S256Q + R267H + I294E + A129T, Q82E + P111Q + S123P + V159M + V203T +G237M + S256E + I294E + A129T, Q82E + P111Q + S123P + N155D + K169R + G237M +S256E + I294E + A129T, Q82E + P111Q + S123P + Q137K + V159M + G237M + S256E +I294E + A129T, Q82E + P111Q + S123P + Q137K + V159M + K240F + S256E + I294E +A129T, Q82E + P111Q + S123P + Q147K + N155D + K240F + S256E + I294E + A129T, A83E + P111Q + S123P + Q147K + V159M + S256E + I294E + Q329E +A129T, Q82E + P111Q + S123P + V159M + K169R + S256E + I294E + V431E + A129T, A41L + Q82E + P111Q + S123P + V159M + S256E + I294E + N383E + A129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0235] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S76E + P111Q + S123P + Q137E + Q147K + V159M + K252E + S256Q + S402Q, P111Q + N121E + Q137K + Q147K + V159M + K169R + S256Q + I294E + S402Q, P111Q + S123P + Q137K + Q147K + V159M + K169R + S256Q + I294E + S402Q, P111Q + S123P + Q137K + Q147K + V159M + L184M + V219T + S256Q + S402Q, A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + S256Q + S402Q, Q82E + P111Q +S123P + Q137K + Q147K + V159M + K252E + S256Q + S402Q, S123P + S127D + N136D +Q137K + Q147K + L152E + N153E + N155E + A491E, Q82E + P111Q + S123P + V159M +A177G + K240F + S256E + I294E + D384G, K8R + Q82E + P111Q + S123P + V159M +K169R + K240F + S256E + I294E, R20K + S123P + Q137K + K169R + K217T + K240F +S256Q + R267H + I294E, R20K + S123P + N155D + K169R + K217T + K240F + S256Q +R267H + I294E, R20K + S123P + Q147K + K169R + V219T + K240F + S256Q + R267H +I294E, Q82E + P111Q + S123P + V159M + V203T + G237M + K252E + S256E + I294E, S76E + Q82E+P111Q+ S123P + V159M + V203T + G237M + S256E +I294E, Q82E + P111Q + S123P + Q147K + V159M + V203T + G237M + S256E + I294E, Q82E + P111Q + S123P + V159M + V203T + G237M + T244R + S256E + I294E, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0236] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S76E+P111Q+S123P+Q137E+Q147K+V159M+K252E+S256Q+S402Q+K129T, P111Q+N121E+Q137K+Q147K+V159M+K169R+S256Q+I294E+S402Q+K129T, P111Q+S123P+Q137K+Q147K+V159M+K169R+S256Q+I294E+S402Q+K129T, P111Q+S123P+Q137K+Q147K+V159M+L184M+V219T of the polypeptide of SEQ ID NO: 1. + S256Q+ S402Q + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256Q+ S402Q + K129T, Q82E + P111Q + S123P + Q137K + Q147K + V159M + K252E + S256Q + S402Q + K129T, S123P + S127D + N136D + Q137K + Q147K + L152E + N153E + N155E + A491E + K129T, Q82E + P111Q + S123P + V159M + A177G + K240F + S256E + I294E+ D384G + K129T, K8R + Q82E + P111Q + S123P + V159M + K169R + K240F + S256E +I294E + K129T, R20K + S123P + Q137K + K169R + K217T + K240F + S256Q + R267H +I294E + K129T, R20K + S123P + N155D + K169R + K217T + K240F + S256Q + R267H +I294E, R20K + S123P + Q147K + K169R + V219T + K240F + S256Q + R267H + I294E +K129T、Q82E + P111Q + S123P + V159M + V203T + G237M +K252E + S256E + I294E + K129T, S76E + Q82E + P111Q + S123P + V159M + V203T + G237M + S256E + I294E + K129T, Q82E + P111Q + S123P + Q147K + V159M + V203T + G237M + S256E + I294E + K129T, Q82E + P111Q + S123P + V159M + V203T + G237M + T244R + S256E + I294E + K129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0237] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S76E+P111Q+S123P+Q137E+Q147K+V159M+K252E+S256Q+S402Q+A129T, P111Q+N121E+Q137K+Q147K+V159M+K169R+S256Q+I294E+S402Q+A129T, P111Q+S123P+Q137K+Q147K+V159M+K169R+S256Q+I294E+S402Q+A129T, P111Q+S123P+Q137K+Q147K+V159M+L184M+V219T of the polypeptide of SEQ ID NO: 2. + S256Q+ S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256Q+ S402Q + A129T, Q82E + P111Q + S123P + Q137K + Q147K + V159M + K252E + S256Q + S402Q + A129T, S123P + S127D + N136D + Q137K + Q147K + L152E + N153E + N155E + A491E + A129T, Q82E + P111Q + S123P + V159M + A177G + K240F + S256E + I294E+ D384G + A129T, K8R + Q82E + P111Q + S123P + V159M + K169R + K240F + S256E +I294E + A129T, R20K + S123P + Q137K + K169R + K217T + K240F + S256Q + R267H +I294E + A129T, R20K + S123P + N155D + K169R + K217T + K240F + S256Q + R267H +I294E, R20K + S123P + Q147K + K169R + V219T + K240F + S256Q + R267H + I294E +A129T、Q82E + P111Q + S123P + V159M + V203T + G237M +K252E + S256E + I294E + A129T, S76E + Q82E + P111Q + S123P + V159M + V203T + G237M + S256E + I294E + A129T, Q82E + P111Q + S123P + Q147K + V159M + V203T + G237M + S256E + I294E + A129T, Q82E + P111Q + S123P + V159M + V203T + G237M + T244R + S256E + I294E + A129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0238] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256Q + I294E + S402Q, A83E + P111Q + S123P + Q137K + Q147K + N155D + L184M + S256Q + I294E + S402Q, R20K + S123P + Q147K + N155D + K169R + K217T + K240F + S256Q + R267H + I294E, R20K + S123P + N155D + K169R + K217T + K240F + S256Q + R267H+ I294E + S474E, R20K + A41L + S123P + L152P + K169R + K217T + K240F + S256Q + R267H + I294E, K8R + R20K + S123P + K169R + D210H + K217T + K240F + S256Q +R267H + I294E, P111Q + S123P + Q137K + Q147K + V159M + G237M + T244R + S256Q +I294E + S402Q, P111Q + S123P + Q137K + Q147K + V159M + K169R + V203T + S256Q +I294E + S402Q, Q82E + P111Q + S123P + Q137K + V159M + V203T + D210H + G237M + S256E + I294E, Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0239] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256Q + I294E + S402Q + K129T, A83E + P111Q + S123P + Q137K + Q147K + N155D + L184M + S256Q + I294E + S402Q + K129T, R20K + S123P + Q147K + N155D + K169R + K217T + K240F + S256Q + R267H + I294E + K129T, R20K + S123P + N155D + K169R + K217T+ K240F + S256Q + R267H + I294E + S474E + K129T, R20K + A41L + S123P + L152P +K169R + K217T + K240F + S256Q + R267H + I294E + K129T, K8R + R20K + S123P +K169R + D210H + K217T + K240F + S256Q + R267H + I294E + K129T, P111Q + S123P +Q137K + Q147K + V159M + G237M + T244R + S256Q + I294E + S402Q + K129T, P111Q +S123P + Q137K + Q147K + V159M + K169R + V203T + S256Q + I294E + S402Q + K129T, Q82E + P111Q + S123P + Q137K + V159M + V203T + D210H + G237M + S256E + I294E + K129T, Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E + K129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60% of the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.For example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0240] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256Q + I294E + S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + N155D + L184M + S256Q + I294E + S402Q + A129T, R20K + S123P + Q147K + N155D + K169R + K217T + K240F + S256Q + R267H + I294E + A129T, R20K + S123P + N155D + K169R + K217T+ K240F + S256Q + R267H + I294E + S474E + A129T, R20K + A41L + S123P + L152P +K169R + K217T + K240F + S256Q + R267H + I294E + A129T, K8R + R20K + S123P +K169R + D210H + K217T + K240F + S256Q + R267H + I294E + A129T, P111Q + S123P +Q137K + Q147K + V159M + G237M + T244R + S256Q + I294E + S402Q + A129T, P111Q +S123P + Q137K + Q147K + V159M + K169R + V203T + S256Q + I294E + S402Q + A129T, Q82E + P111Q + S123P + Q137K + V159M + V203T + D210H + G237M + S256E + I294E + A129T, Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E + A129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60% of the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.For example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0241] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: Q82E+P111Q+S123P+Q137K+Q147K+V159M+L184M+A238S+S256Q+I294E+S402Q, A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+S256Q+I294E+S402Q, A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+S256E+I294E+S402Q, R20K+S123P+N155D+K169R+ K217T+ K240F + S256Q + R267H + I294E + D384G + E489R, R20K + S123P + K169R + K217T+ K240F + S256Q + R267H + I294E + Q329E + V431E + E489R, P111Q + S123P + Q137K + Q147K + V159M + K169R + K252E + S256Q + I294E + K322E + S402Q、P111Q + S123P+ Q137K + Q147K + V159M + K169R + K240F + S256Q + I294E + K322E + S402Q, S76E+ P111Q + S123P + Q137K + Q147K + V159M + K169R + G237M + S256Q + I294E +S402Q, P111Q + S123P + Q137K + Q147K + V159M + K169R + G237M + T244R + S256Q +I294E + S402Q, P111Q + S123P + Q137K + Q147K + V159M + K169R + V219T + K240F +S256Q + I294E + S402Q, P111Q + S123P + Q137K + Q147K + V159M + V251E + S256E +Q271E + I294E + Q329E + S402Q, Q82E + P111Q + S123P +L152P + V159M + K169R + V203T + G237M + T244R + S256E + I294E, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0242] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: Q82E+P111Q+S123P+Q137K+Q147K+V159M+L184M+A238S+S256Q+I294E+S402Q+K129T, A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+S256Q+I294E+S402Q+K129T, A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+S256E+I294E+S402Q+K129T, R20K+ S123P+ N155D + K169R + K217T + K240F + S256Q + R267H + I294E + D384G + E489R +K129T, R20K + S123P + K169R + K217T + K240F + S256Q + R267H + I294E + Q329E +V431E + E489R + K129T, P111Q + S123P + Q137K + Q147K + V159M + K169R + K252E +S256Q + I294E + K322E + S402Q + K129T, P111Q + S123P + Q137K + Q147K + V159M +K169R + K240F + S256Q + I294E + K322E + S402Q + K129T, S76E + P111Q + S123P + Q137K + Q147K + V159M + K169R + G237M + S256Q + I294E + S402Q + K129T, P111Q +S123P + Q137K + Q147K + V159M + K169R + G237M + T244R + S256Q + I294E + S402Q+ K129T, P111Q + S123P + Q137K + Q147K + V159M + K169R + V219T + K240F + S256Q+ I294E + S402Q + K129T, P111Q + S123P + Q137K + Q147K+ V159M + V251E + S256E+ Q271E + I294E + Q329E + S402Q + K129T, Q82E + P111Q + S123P + L152P + V159M+ K169R + V203T + G237M + T244R + S256E + I294E + K129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0243] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: Q82E+P111Q+S123P+Q137K+Q147K+V159M+L184M+A238S+S256Q+I294E+S402Q+A129T, A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+S256Q+I294E+S402Q+A129T, A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+S256E+I294E+S402Q+A129T, R20K+ S123P+ N155D + K169R + K217T + K240F + S256Q + R267H + I294E + D384G + E489R +A129T, R20K + S123P + K169R + K217T + K240F + S256Q + R267H + I294E + Q329E +V431E + E489R + A129T, P111Q + S123P + Q137K + Q147K + V159M + K169R + K252E +S256Q + I294E + K322E + S402Q + A129T, P111Q + S123P + Q137K + Q147K + V159M +K169R + K240F + S256Q + I294E + K322E + S402Q + A129T, S76E + P111Q + S123P + Q137K + Q147K + V159M + K169R + G237M + S256Q + I294E + S402Q + A129T, P111Q +S123P + Q137K + Q147K + V159M + K169R + G237M + T244R + S256Q + I294E + S402Q+ A129T, P111Q + S123P + Q137K + Q147K + V159M + K169R + V219T + K240F + S256Q+ I294E + S402Q + A129T, P111Q + S123P + Q137K + Q147K+ V159M + V251E + S256E+ Q271E + I294E + Q329E + S402Q + A129T, Q82E + P111Q + S123P + L152P + V159M+ K169R + V203T + G237M + T244R + S256E + I294E + A129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0244] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E+P111Q+S123P+Q137K+F146D+Q147G+L148P+V159M+L184M+S256Q+I294E+S402Q, A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256Q+I294E+N298D+V300L+S402Q, A83E+P111Q+S123P+Q137K+Q147K+V159M+K169R+L184M+K240L+S256Q+I294E+S402Q, A83E+ P111Q+ S123P + Q137K + Q147K + V159M + L184M + G237M + S256Q + I294E + S402Q +K488T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + K240F +S256Q + I294E + S402Q, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M +K240F + S256Q + I294E + S402Q + E489R, A83E + P111Q + S123P + Q137K + Q147K +V159M + F165H + L184M + S256Q + I294E + S402Q + V431E, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + Q271E + I294E + Q329E + S402Q, P111Q +S123P + Q137K + Q147K + V159M + K169R + D210H + K240F + S256E + I294E + S402Q+ K488T, S76E + P111Q + S123P + Q137K + Q147K + V159M + K169R + V203T + G237M+ S256Q + I294E + S402Q, P111Q + S123P + Q137K + Q147K +V159M + K169R + G237M + S256Q + I294E + P339S + S402Q + K488T, S76E + Q82E + P111Q + S123P + V159M +V203T + G237M + S256E + I294E + S474E + E489R + P492D, P111Q + S123P + Q137K +Q147K + V159M + A238T + V251E + S256Q + Q271E + I294E + Q329E + S402Q, A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + S256E + Q271D + I294E + Q329E + S402Q, Q82E + P111Q + S123P + Q137K + V159M + K169R + A189G + V203T + G237M + T244R + S256E + I294E, Q82E + P111Q + S123P + Q137K + V159M + K169R + V203T + G237M + T244R + V251E + S256E + I294E, Q82E + P111Q + S123P + V159M + K169R+ V203T + G237M + T244R + S256E + I294E + N383Q + V431E, S76E + Q82E + S94R +P111Q + S123 + V159M + K169R + V203T + G237M + T244R + S256E + I294E, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0245] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + F146D + Q147G + L148P + V159M + L184M + S256Q + I294E + S402Q + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256Q + I294E + N298D + V300L + S402Q + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + K169R + L184M + K240L + S256Q + I294E of the polypeptide of SEQ ID NO: 1. +S402Q + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + G237M +S256Q + I294E + S402Q + K488T + K129T, A83E + P111Q + S123P + Q137K + Q147K +V159M + L184M + V203T + K240F + S256Q + I294E + S402Q + K129T, A83E + P111Q +S123P + Q137K + Q147K + V159M + L184M + K240F + S256Q + I294E + S402Q + E489R+ K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + F165H + L184M + S256Q+ I294E + S402Q + V431E + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M+ L184M + V251E + Q271E + I294E + Q329E + S402Q, P111Q + S123P + Q137K + Q147K+ V159M + K169R + D210H + K240F + S256E + I294E + S402Q + K488T + K129T, S76E+ P111Q + S123P + Q137K + Q147K + V159M + K169R + V203T +G237M + S256Q +I294E + S402Q + K129T, P111Q + S123P + Q137K + Q147K + V159M + K169R + G237M +S256Q + I294E + P339S + S402Q + K488T + K129T, S76E + Q82E + P111Q + S123P +V159M + V203T + G237M + S256E + I294E + S474E + E489R + P492D + K129T, P111Q +S123P + Q137K + Q147K + V159M + A238T + V251E + S256Q + Q271E+I294E+ Q329E+ S402Q + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256E+ Q271D + I294E + Q329E + S402Q + K129T, Q82E + P111Q + S123P + Q137K + V159M+ K169R + A189G + V203T + G237M + T244R + S256E + I294E + K129T, Q82E + P111Q + S123P + Q137K + V159M + K169R + V203T + G237M + T244R + V251E + S256E +I294E + K129T, Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E + N383Q + V431E + K129T, S76E + Q82E + S94R + P111Q + S123 + V159M + K169R + V203T + G237M + T244R + S256E + I294E + K129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO:The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0246] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + F146D + Q147G + L148P + V159M + L184M + S256Q + I294E + S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256Q + I294E + N298D + V300L + S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + K169R + L184M + K240L + S256Q + I294E of the polypeptide of SEQ ID NO: 2. +S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + G237M +S256Q + I294E + S402Q + K488T + A129T, A83E + P111Q + S123P + Q137K + Q147K +V159M + L184M + V203T + K240F + S256Q + I294E + S402Q + A129T, A83E + P111Q +S123P + Q137K + Q147K + V159M + L184M + K240F + S256Q + I294E + S402Q + E489R+ A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + F165H + L184M + S256Q+ I294E + S402Q + V431E + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M+ L184M + V251E + Q271E + I294E + Q329E + S402Q, P111Q + S123P + Q137K + Q147K+ V159M + K169R + D210H + K240F + S256E + I294E + S402Q + K488T + A129T, S76E+ P111Q + S123P + Q137K + Q147K + V159M + K169R + V203T +G237M + S256Q +I294E + S402Q + A129T, P111Q + S123P + Q137K + Q147K + V159M + K169R + G237M +S256Q + I294E + P339S + S402Q + K488T + A129T, S76E + Q82E + P111Q + S123P +V159M + V203T + G237M + S256E + I294E + S474E + E489R + P492D + A129T, P111Q +S123P + Q137K + Q147K + V159M + A238T + V251E + S256Q + Q271E+I294E+ Q329E+ S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256E+ Q271D + I294E + Q329E + S402Q + A129T, Q82E + P111Q + S123P + Q137K + V159M+ K169R + A189G + V203T + G237M + T244R + S256E + I294E + A129T, Q82E + P111Q + S123P + Q137K + V159M + K169R + V203T + G237M + T244R + V251E + S256E +I294E + A129T, Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E + N383Q + V431E + A129T, S76E + Q82E + S94R + P111Q + S123 + V159M + K169R + V203T + G237M + T244R + S256E + I294E + A129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO:The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0247] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + K252E + S256Q + Q271E + I294E + Q329E + S402Q, Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + Q271E + I294E of the polypeptide of SEQ ID NO: 1. +Q329E + N383E, Q82E + P111Q + S123P + Q137K + N155D + V159M + K169R + V203T + G237M + T244R + S256E + I294E + K445E, K8E + A41L + S76E + Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0248] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + K252E + S256Q + Q271E + I294E + Q329E + S402Q + K129T, Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E of the polypeptide of SEQ ID NO: 1. +Q271E + I294E + Q329E + N383E + K129T, Q82E + P111Q + S123P + Q137K + N155D + V159M + K169R + V203T + G237M + T244R + S256E + I294E + K445E + K129T, K8E + A41L + S76E + Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E + K129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0249] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + K252E + S256Q + Q271E + I294E + Q329E + S402Q + A129T, Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E of the polypeptide of SEQ ID NO: 2. +Q271E + I294E + Q329E + N383E + A129T, Q82E + P111Q + S123P + Q137K + N155D + V159M + K169R + V203T + G237M + T244R + S256E + I294E + K445E + A129T, K8E + A41L + S76E + Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E + A129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0250] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S76E + A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q, A83E + P111Q + S123P + Q137K + Q147K + V159M + K169R + L184M + K252E + S256Q + Q271E + I294E + Q329E + S402Q, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + A238S of the polypeptide of SEQ ID NO: 1. +S256E + Q271E + I294E + Q329E + S402Q, A83E + P111Q + S123P + Q137K + Q147K +V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + V431E, A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E+ Q329E + K347E + S402Q, A83E + P111Q + S123P + Q137K + L152P + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + V431E, K8E + A83E + P111Q +S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E+ S402Q, A83E + P111Q + S123P + Q137K + Q147K + N155D + L184M + G237M + V251E+ S256Q + Q271E + I294E + Q329E + S402Q, A41L + A83E + P111Q + S123P + Q137K +Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E +Q329E + S402Q, A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E+ Q329E + N383Q + S402Q, R20K + S76E + Q82E + P111Q + S123P + V159M + K169R +V203T + G237M + T244R + S256E + I294E + Q329E + P492D, S76E + Q82E + P111Q +S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E+Q329E+ E489R+ P492D, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0251] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S76E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+K129T, A83E+P111Q+S123P+Q137K+Q147K+V159M+K169R+L184M+K252E+S256Q+Q271E+I294E+Q329E+S402Q+K129T, A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+ V203T+ A238S + S256E + Q271E + I294E + Q329E + S402Q + K129T, A83E + P111Q + S123P+ Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E +S402Q + V431E + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M +V251E + S256Q + Q271E + I294E + Q329E + K347E + S402Q + K129T, A83E + P111Q +S123P + Q137K + L152P + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E+ S402Q + V431E + K129T, K8E + A83E + P111Q + S123P + Q137K + Q147K + V159M +L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + K129T, A83E + P111Q +S123P + Q137K + Q147K + N155D + L184M + G237M + V251E + S256Q + Q271E + I294E+ Q329E + S402Q + K129T, A41L + A83E + P111Q + S123P +Q137K + Q147K + V159M +L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + K129T, A83E + P111Q +S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E+ N383Q + S402Q + K129T, R20K + S76E + Q82E + P111Q + S123P + V159M + K169R +V203T + G237M + T244R + S256E + I294E + Q329E + P492D + K129T, S76E + Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E + Q329E + E489R + P492D + K129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0252] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: S76E + A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + K169R + L184M + K252E + S256Q + Q271E + I294E + Q329E + S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T+ A238S + S256E + Q271E + I294E + Q329E + S402Q + A129T, A83E + P111Q + S123P+ Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E +S402Q + V431E + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M +V251E + S256Q + Q271E + I294E + Q329E + K347E + S402Q + A129T, A83E + P111Q +S123P + Q137K + L152P + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E+ S402Q + V431E + A129T, K8E + A83E + P111Q + S123P + Q137K + Q147K + V159M +L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + A129T, A83E + P111Q +S123P + Q137K + Q147K + N155D + L184M + G237M + V251E + S256Q + Q271E + I294E+ Q329E + S402Q + A129T, A41L + A83E + P111Q + S123P +Q137K + Q147K + V159M +L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + A129T, A83E + P111Q +S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E+ N383Q + S402Q + A129T, R20K + S76E + Q82E + P111Q + S123P + V159M + K169R +V203T + G237M + T244R + S256E + I294E + Q329E + P492D + A129T, S76E + Q82E + P111Q + S123P + V159M + K169R + V203T + G237M + T244R + S256E + I294E + Q329E + E489R + P492D + A129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0253] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V219T + G237M + V251E + S256Q + Q271E + I294E + Q329E + S402Q, S76E + A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + A238S + S256E + Q271E + I294E + Q329E + S402Q, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + D210H+ T244R + K252E + S256Q + Q271E + I294E + Q329E + S402Q, A83E + P111Q + S123P+ Q137K + Q147K + V159M + L184M + T244E + V251E + S256Q + Q271E + I294E +Q329E + S402Q + V431E, K8E + A83E + S94R + P111Q + S123P + Q137K + Q147K +V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q, A83E + P111Q +S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E+ S402Q + V431E + K445E, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M+ D210H + K240F + V251E + S256Q + Q271E + I294E + Q329E + S402Q, A41L + A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + K240F + V251E + S256Q + Q271E+ I294E + Q329E+ S402Q, Q82E + P111Q + S123P + Q137K +Q147K + V159M + L184M + V203T + D210H + V251E + S256Q + Q271E + I294E + Q329E + S402Q, A41L + A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E+ Q329E + N383Q + S402Q, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M+ T244R + W248V + V251E + S256Q + Q271E + I294E + Q329E+ S402Q, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + T244R + V251E + S256Q +Q271E + I294E + Q329E + S402Q, A83E + P111Q + S123P + Q137K + Q147K + V159M +L184M + V251E + S256Q + Q271E + R295K + N298D + Q329E + S402Q + L447M, A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + S256E + Q271E+I294E+ Q329E+ P339S + N383E + S402Q + V431E, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0254] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V219T+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+K129T, S76E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+A238S+S256E+Q271E+I294E+Q329E+S402Q+K129T, A83E+P111Q+S123P+Q137K+Q147K+ V159M+ L184M + D210H + T244R + K252E + S256Q + Q271E + I294E + Q329E + S402Q +K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + T244E + V251E +S256Q + Q271E + I294E + Q329E + S402Q + V431E + K129T, K8E + A83E + S94R +P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E+ Q329E + S402Q + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M+ V251E + S256Q + Q271E + I294E + Q329E + S402Q + V431E + K445E + K129T, A83E+ P111Q + S123P + Q137K + Q147K + V159M + L184M + D210H + K240F + V251E +S256Q + Q271E + I294E + Q329E + S402Q + K129T, A41L + A83E + P111Q + S123P +Q137K + Q147K + V159M + L184M + K240F + V251E + S256Q + Q271E +I294E + Q329E + S402Q + K129T, Q82E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + D210H + V251E + S256Q + Q271E + I294E + Q329E + S402Q + K129T, A41L + A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E+ Q329E + N383Q + S402Q + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M+ L184M + T244R + W248V + V251E + S256Q + Q271E + I294E + Q329E + S402Q +K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + T244R +V251E + S256Q + Q271E + I294E + Q329E + S402Q + K129T, A83E + P111Q + S123P +Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + R295K + N298D + Q329E+ S402Q + L447M + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256E + Q271E + I294E + Q329E + P339S + N383E + S402Q + V431E + K129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0255] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V219T + G237M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + A129T, S76E + A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + A238S + S256E + Q271E + I294E + Q329E + S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M+ L184M + D210H + T244R + K252E + S256Q + Q271E + I294E + Q329E + S402Q +A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + T244E + V251E +S256Q + Q271E + I294E + Q329E + S402Q + V431E + A129T, K8E + A83E + S94R +P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E+ Q329E + S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M+ V251E + S256Q + Q271E + I294E + Q329E + S402Q + V431E + K445E + A129T, A83E+ P111Q + S123P + Q137K + Q147K + V159M + L184M + D210H + K240F + V251E +S256Q + Q271E + I294E + Q329E + S402Q + A129T, A41L + A83E + P111Q + S123P +Q137K + Q147K + V159M + L184M + K240F + V251E + S256Q + Q271E +I294E + Q329E + S402Q + A129T, Q82E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + D210H + V251E + S256Q + Q271E + I294E + Q329E + S402Q + A129T, A41L + A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E+ Q329E + N383Q + S402Q + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M+ L184M + T244R + W248V + V251E + S256Q + Q271E + I294E + Q329E + S402Q +A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + T244R +V251E + S256Q + Q271E + I294E + Q329E + S402Q + A129T, A83E + P111Q + S123P +Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + R295K + N298D + Q329E+ S402Q + L447M + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + S256E + Q271E + I294E + Q329E + P339S + N383E + S402Q + V431E + A129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0256] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + G237M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + E489R + V505L, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + K252E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V, A83E + P111Q + S123P + Q137K + Q147K +V159M + L184M + V203T + V251E + S256Q + Q271E + I294E + Q329E + N383Q + S402Q+ V431E, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V219T + G237M+ S256Q + Q271E + I294E + Q329E + S402Q + V431E + S474E, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E +N383E + S402Q + V431E + P492D, A83E + P111Q + S123P + Q137K + Q147K + V159M +L184M + A189G + V251E + S256Q + Q271E + I294E + Q329E + N383Q + S402Q +V431E, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q +Q271D + I294E + Q329E + N383E + S402Q + V431E + A459P, K8R + A83E + P111Q +S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E +I294E + Q329E + S402Q + V431E + E489K, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0257] In one aspect, the variant contains changes at positions corresponding to the group selected from the following components: A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+E489R+V505L+K129T, A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K252E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V+K129T, A83E+P111Q+S123P +Q137K + Q147K + V159M + L184M + V203T + V251E + S256Q + Q271E + I294E + Q329E+ N383Q + S402Q + V431E + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M+ L184M + V219T + G237M + S256Q + Q271E + I294E + Q329E + S402Q + V431E +S474E + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E +S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + P492D + K129T, A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + A189G + V251E + S256Q + Q271E+ I294E + Q329E + N383Q + S402Q + V431E + K129T, A83E + P111Q + S123P + Q137K+ Q147K + V159M + L184M + V251E + S256Q + Q271D + I294E + Q329E + N383E +S402Q + V431E + A459P + K129T, K8R + A83E + P111Q + S123P +Q137K + Q147K +V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + V431E + E489K + K129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V + K129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0258] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+E489R+V505L+A129T, A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K252E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V+A129T, A83E+P111Q+S123P +Q137K + Q147K + V159M + L184M + V203T + V251E + S256Q + Q271E + I294E + Q329E+ N383Q + S402Q + V431E + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M+ L184M + V219T + G237M + S256Q + Q271E + I294E + Q329E + S402Q + V431E +S474E + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E +S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + P492D + A129T, A83E +P111Q + S123P + Q137K + Q147K + V159M + L184M + A189G + V251E + S256Q + Q271E+ I294E + Q329E + N383Q + S402Q + V431E + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271D + I294E + Q329E + N383E +S402Q + V431E + A459P + A129T, K8R + A83E + P111Q + S123P +Q137K + Q147K +V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + V431E + E489K + A129T, A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V + A129T, wherein the variant has xyloglucanase activity and wherein the variant is related to SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: The polypeptide of 3 has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

[0259] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + D210H + G237M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + E489R + P492D, S76E + Q82E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + V251E + S256Q + Q271E + I294E + Q329E + N383Q + S402Q + V431E, K8E + A41L + A83E + P111Q of the polypeptide of SEQ ID NO: 1. + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E+ Q329E + K394R + S402Q + V431E, A83E + P111Q + S123P + Q137K + Q147K + V159M+ L184M + V251E + S256Q + Q271E + I294E + Q329E + K347E + N383E + S402Q +V431E + A491V, K8E + A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M +V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0260] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + D210H + G237M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + E489R + P492D + K129T, S76E + Q82E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + V251E + S256Q + Q271E + I294E + Q329E + N383Q + S402Q + V431E + K129T, K8E +A41L + A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q +Q271E + I294E + Q329E + K394R + S402Q + V431E + K129T, A83E + P111Q + S123P +Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + K347E+ N383E + S402Q + V431E + A491V + K129T, K8E + A83E + P111Q + S123P + Q137K +Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V + K129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0261] In one aspect, the variant contains changes at positions corresponding to the groups selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + D210H + G237M + V251E + S256Q + Q271E + I294E + Q329E + S402Q + E489R + P492D + A129T, S76E + Q82E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + V251E + S256Q + Q271E + I294E + Q329E + N383Q + S402Q + V431E + A129T, K8E +A41L + A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V251E + S256Q +Q271E + I294E + Q329E + K394R + S402Q + V431E + A129T, A83E + P111Q + S123P +Q137K + Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + K347E+ N383E + S402Q + V431E + A491V + A129T, K8E + A83E + P111Q + S123P + Q137K +Q147K + V159M + L184M + V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V + A129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0262] In one aspect, the variant contains changes at positions corresponding to the group selected from the following components: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + K240F + V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V, S76E + A83E + P111Q + S123P + Q137K + Q147K + N155D + L184M + G237M + V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0263] In one aspect, the variant contains changes at positions corresponding to the group selected from the following composition: A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+K240F+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V+K129T, S76E+A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V+ K129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0264] In one aspect, the variant contains changes at positions corresponding to the group selected from the following composition: A83E + P111Q + S123P + Q137K + Q147K + V159M + L184M + V203T + K240F + V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V + A129T, S76E + A83E + P111Q + S123P + Q137K + Q147K + N155D + L184M + G237M + V251E + S256Q + Q271E + I294E + Q329E + N383E + S402Q + V431E + A491V + A129T, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0265] In one respect, variants include changes or combinations of changes selected from the following groups:

[0266] K394R of the polypeptide of SEQ ID NO: 1

[0267] S127D,

[0268] R211K,

[0269] S123P,

[0270] K488T,

[0271] S256Q,

[0272] K476R,

[0273] K217R,

[0274] Q271D,

[0275] S214Q,

[0276] L447M,

[0277] K482R,

[0278] K169R、

[0279] L152D、

[0280] R267K、

[0281] L152E、

[0282] D210R、

[0283] L152 、

[0284] R295K、

[0285] S127W、

[0286] E126P、

[0287] S127H、

[0288] T104G、

[0289] Q125K、

[0290] Q125P、

[0291] Q125S、

[0292] D395P、

[0293] G103V、

[0294] T104R、

[0295] Q125L、

[0296] A41E、

[0297] A41R、

[0298] Q125F、

[0299] S127L、

[0300] A226K、

[0301] A41L、

[0302] A226D、

[0303] A118K+S123P、

[0304] N155D、

[0305] Q137K、

[0306] N155E、

[0307] Q147K、

[0308] R276K、

[0309] V203T、

[0310] S94R、

[0311] K18E、

[0312] K252E、

[0313] V219T、

[0314] R267C+T427V、

[0315] Q243E、

[0316] K414E、

[0317] K445E、

[0318] R20K+S123P、

[0319] S123P+K206R、

[0320] R20K+S123P+R211K、

[0321] S123P+K347R、

[0322] S123P+K347R+K353R+D395P、

[0323] S123P+D395P、

[0324] S123P+S127D、

[0325] V159M、

[0326] K392E、

[0327] E489R+P492D、

[0328] Y503L+V505L、

[0329] Y503V+V505L、

[0330] L184M+V219A、

[0331] S123P+R211K+K217R+S256Q+K488T、

[0332] Q82E、

[0333] S76E、

[0334] A83E、

[0335] Q271E、

[0336] S256E、

[0337] I294E、

[0338] Q329E、

[0339] V431E、

[0340] R20K+Y105E+S123P+Q147K+R267K、

[0341] R20K+Y105E+S123P+R267K、

[0342] R20K+S123P+K220R、

[0343] R20K+Y105E+S123P+N136D、

[0344] R20K+S123P+Q137K+Q147K、

[0345] Y105E+A118K+S123P+K206R+K220R+R267K、

[0346] P111Q+S123P+V159M、

[0347] S94R+P111Q+S123P+V159M、

[0348] K87E+P111Q+S123P+V159M+S402Q、

[0349] K87E+P111Q+S123P+V159M、

[0350] P111Q+S123P+V159M+S402Q、

[0351] K87E+P111Q+V159M+I294Q+I473T、

[0352] K8E+P111Q+V159M、

[0353] K8E+K18E+P111Q+V159M+K206E、

[0354] R20K+P111Q+S123P+S127D+V159M、

[0355] P111Q+Q147K+V159M+K220R、

[0356] S94R+P111Q+V159M、

[0357] P111Q+V159M+K206E+I294Q、

[0358] P111Q+V159M+K206E+I294Q+K347E、

[0359] P111Q+Q137K+Q147K+V159M+K252E、

[0360] P111Q+Q137K+Q147K+N155D+K252E、

[0361] P111Q+Q137K+L152D+V203T+K217R、

[0362] P111Q+Q137K+V159M、

[0363] K8E+P111Q+N155D+V159M、

[0364] A41L+P111Q+S123P+Q147K+V159M+V203T、

[0365] A41L+P111Q+S123P+Q147K+V159M+K217R、

[0366] P111Q+S123P+Q137K+Q147K+V159M+S256Q+S402Q、

[0367] P111Q+S123P+Q147K+V159M+I294Q+S402Q、

[0368] A41L+P111Q+Q137K+V159M+N168R+Q271D+K488T、

[0369] P111Q+Q137K+Q147K+V159M+V203T+K217R、

[0370] P111Q+Q147K+V159M、

[0371] P111Q+Q137K+Q147K+V159M、

[0372] P111Q+S123P+Q137K+V159M+K488T、

[0373] P111Q+S123P+Q137K+V159M+S256Q、

[0374] K87E+P111Q+L152D+V159M+V203T+I294Q、

[0375] K87E+P111Q+Q147K+L152D+V159M、

[0376] R20K+A83E+S123P+K220R+S256E、

[0377] R20K+S76E+A83E+S123P+K220R+K252E、

[0378] R20K+A83E+S123P+K220R+K252E、

[0379] R20K+A42V+S123P+K220R+K252E+I294E、

[0380] R20K+Q82E+S123P+Q147K+K220R、

[0381] R20K+A83E+S123P+K220R+S256Q、

[0382] R20K+Q82E+S123P+N155D+K220R、

[0383] R20K+S123P+V203T+K220R+K252E、

[0384] R20K+S123P+K220R+I294E、

[0385] R20K+A83E+S123P+V203T+K220R+K252E、

[0386] R20K+A41L+Q82E+S123P+K220R、

[0387] R20K+S123P+N155D+K220R、

[0388] R20K+A42V+S76E+S123P+K220R、

[0389] R20K+S123P+V203T+V219T、

[0390] R20K+A42V+A83E+S123P+K220R、

[0391] R20K+A42V+S76E+S123P+V203T+K220R、

[0392] A83E+P111Q+S123P+V159M+S256E+I294E、

[0393] Q82E+P111Q+S123P+V159M+S256E+I294E、

[0394] Q82E+P111Q+S123P+Q147K+V159M+I294E、

[0395] S76E+Q82E+K87E+P111Q+S123P+V159M+V203T、

[0396] A83E+P111Q+S123P+Q137K+Q147K+V159M+S256Q+S402Q、

[0397] P111Q+S123P+Q137K+Q147K+N155D+S256Q+A289T+N302H、

[0398] S76E+P111Q+S123P+Q137E+Q147K+V159M+K252E+S256Q+S402Q、

[0399] P111Q+S123P+Q137K+Q147K+V159M+K252E+S256Q+S402Q、

[0400] P111Q+S123P+Q137K+Q147K+N155D+S256Q+I294E+S402Q、

[0401] Q82E+P111Q+S123P+Q137K+Q147K+V159M+L184M+A238S+S256Q+I294E+S402Q、

[0402] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256Q+I294E+S402Q、

[0403] P111Q+N121E+Q137K+Q147K+V159M+K169R+S256Q+I294E+S402Q、

[0404] P111Q+S123P+Q137K+Q147K+V159M+K169R+S256Q+I294E+S402Q、

[0405] P111Q+S123P+Q137K+Q147K+V159M+L184M+V219T+S256Q+S402Q、

[0406] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256Q+S402Q、

[0407] Q82E+P111Q+S123P+Q137K+Q147K+V159M+K252E+S256Q+S402Q、

[0408] S76E+P111Q+S123P+Q137K+Q147K+V159M+S256Q+S402Q、

[0409] K8R+P111Q+S123P+Q137K+Q147K+V159M+S256Q+S402Q、

[0410] S123P+S127D+N136D+Q137K+Q147K+L152E+N153E+N155E、

[0411] S123P+S127D+N136D+Q137K+Q147K+L152E+N153E+N155E+A491E、

[0412] R20K+S123P+K169R+K217T+K240F+S256Q+R267H+I294E、

[0413] K87E+P111Q+S123P+V159M+K217T+I294E、

[0414] A83E+P111Q+S123P+V159M+K240F+K252E、

[0415] A83E+P111Q+S123P+V159M+K252E、

[0416] K87E+P111Q+S123P+V159M+S256Q+I294E、

[0417] K87E+P111Q+S123P+V159M+K347E+N383E、

[0418] Q82E+P111Q+S123P+V159M+V203T+G237M+S256E+I294E、

[0419] Q82E+P111Q+S123P+N155D+S256E+I294E、

[0420] Q82E+P111Q+S123P+N155D+K169R+G237M+S256E+I294E、

[0421] Q82E+P111Q+S123P+Q147K+V159M+S256E+I294E、

[0422] Q82E+P111Q+S123P+Q137K+V159M+G237M+S256E+I294E、

[0423] Q82E+P111Q+S123P+Q137K+V159M+K240F+S256E+I294E、

[0424] Q82E+P111Q+S123P+Q147K+N155D+K240F+S256E+I294E、

[0425] K8E+Q82E+P111Q+S123P+V159M+S256E+I294E、

[0426] A83E+P111Q+S123P+Q147K+V159M+S256E+I294E+Q329E、

[0427] Q82E+P111Q+S123P+V159M+K240F+S256EI294E、

[0428] Q82E+P111Q+S123P+V159M+A177G+K240F+S256E+I294E+D384G、

[0429] K8R+Q82E+P111Q+S123P+V159M+K169R+K240F+S256E+I294E、

[0430] Q82E+P111Q+S123P+V159M+K169R+S256E+I294E+V431E、

[0431] Q82E+P111Q+S123P+V159M+G237M+V251E+I294E、

[0432] A41L+Q82E+P111Q+S123P+V159M+S256E+I294E+N383E、

[0433] A83E+P111Q+S123P+Q137K+F146D+Q147G+L148P+V159M+L184M+S256Q+I294E+S402Q、

[0434] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256Q+I294E+N298D+V300L+S402Q、

[0435] A83E+P111Q+S123P+Q137K+Q147K+V159M+K169R+L184M+K240L+S256Q+I294E+S402Q、

[0436] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+S256Q+I294E+S402Q+K488T、

[0437] A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+S256Q+I294E+S402Q、

[0438] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+K240F+S256Q+I294E+S402Q、

[0439] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+S256E+I294E+S402Q、

[0440] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K240F+S256Q+I294E+S402Q+E489R、

[0441] A83E+P111Q+S123P+Q137K+Q147K+V159M+F165H+L184M+S256Q+I294E+S402Q+V431E、

[0442] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+Q271E+I294E+Q329E+S402Q、

[0443] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0444] A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+S256Q+I294E+S402Q、

[0445] R20K+S123P+Q147K+N155D+K169R+K217T+K240F+S256Q+R267H+I294E、

[0446] R20K+S123P+Q137K+K169R+K217T+K240F+S256Q+R267H+I294E、

[0447] R20K+S123P+N155D+K169R+K217T+K240F+S256Q+R267H+I294E+D384G+E489R、

[0448] R20K+S123P+N155D+K169R+K217T+K240F+S256Q+R267H+I294E+S474E、

[0449] R20K+S123P+N155D+K169R+K217T+K240F+S256Q+R267H+I294E、

[0450] R20K+S123P+Q147K+K169R+V219T+K240F+S256Q+R267H+I294E、

[0451] R20K+A41L+S123P+L152P+K169R+K217T+K240F+S256Q+R267H+I294E、

[0452] K8R+R20K+S123P+K169R+D210H+K217T+K240F+S256Q+R267H+I294E、

[0453] R20K+S123P+K169R+K217T+K240F+S256Q+R267H+I294E+Q329E+V431E+E489R、

[0454] P111Q+S123P+Q137K+Q147K+V159M+K169R+D210H+K240F+S256E+I294E+S402Q+K488T、

[0455] P111Q+S123P+Q137K+Q147K+V159M+K169R+K252E+S256Q+I294E+K322E+S402Q、

[0456] P111Q+S123P+Q137K+Q147K+V159M+K169R+K240F+S256Q+I294E+K322E+S402Q、

[0457] S76E+P111Q+S123P+Q137K+Q147K+V159M+K169R+G237M+S256Q+I294E+S402Q、

[0458] S76E+P111Q+S123P+Q137K+Q147K+V159M+K169R+V203T+G237M+S256Q+I294E+S402Q、

[0459] P111Q+S123P+Q137K+Q147K+V159M+K169R+G237M+S256Q+I294E+P339S+S402Q+K488T、

[0460] P111Q+S123P+Q137K+Q147K+V159M+K169R+G237M+T244R+S256Q+I294E+S402Q、

[0461] P111Q+S123P+Q137K+Q147K+V159M+G237M+T244R+S256Q+I294E+S402Q、

[0462] P111Q+S123P+Q137K+Q147K+V159M+K169R+V219T+K240F+S256Q+I294E+S402Q、

[0463] P111Q+S123P+Q137K+Q147K+V159M+K169R+V203T+S256Q+I294E+S402Q、

[0464] Q82E+P111Q+S123P+Q137K+V159M+V203T+D210H+G237M+S256E+I294E、

[0465] Q82E+P111Q+S123P+V159M+V203T+G237M+K252E+S256E+I294E、

[0466] S76E+Q82E+P111Q+S123P+V159M+V203T+G237M+S256E+I294E、

[0467] Q82E+P111Q+S123P+Q147K+V159M+V203T+G237M+S256E+I294E、

[0468] S76E+Q82E+P111Q+S123P+V159M+V203T+G237M+S256E+I294E+S474E+E489R+P492D、

[0469] Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E、

[0470] Q82E+P111Q+S123P+V159M+V203T+G237M+T244R+S256E+I294E、

[0471] S76E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0472] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V219T+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0473] A83E+P111Q+S123P+Q137K+Q147K+V159M+K169R+L184M+K252E+S256Q+Q271E+I294E+Q329E+S402Q、

[0474] S76E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+A238S+S256E+Q271E+I294E+Q329E+S402Q、

[0475] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+A238S+S256E+Q271E+I294E+Q329E+S402Q、

[0476] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+E489R+V505L、

[0477] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+D210H+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+E489R+P492D、

[0478] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+D210H+T244R+K252E+S256Q+Q271E+I294E+Q329E+S402Q、

[0479] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E、

[0480] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+T244E+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E、

[0481] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+K347E+S402Q、

[0482] K8E+A83E+S94R+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0483] A83E+P111Q+S123P+Q137K+L152P+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E、

[0484] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E+K445E、

[0485] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K252E+S256Q+Q271E+I294E+Q329E+S402Q、

[0486] K8E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0487] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+D210H+K240F+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0488] A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0489] A41L+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K240F+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0490] Q82E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+D210H+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0491] A41L+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0492] A41L+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q、

[0493] P111Q+S123P+Q137K+Q147K+V159M+V251E+S256E+Q271E+I294E+Q329E+S402Q、

[0494] P111Q+S123P+Q137K+Q147K+V159M+A238T+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0495] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q、

[0496] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+T244R+W248V+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0497] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+T244R+V251E+S256Q+Q271E+I294E+Q329E+S402Q、

[0498] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+R295K+N298D+Q329E+S402Q+L447M、

[0499] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256E+Q271D+I294E+Q329E+S402Q、

[0500] Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+Q271E+I294E+Q329E+N383E、

[0501] Q82E+P111Q+S123P+Q137K+V159M+K169R+A189G+V203T+G237M+T244R+S256E+I294E、

[0502] Q82E+P111Q+S123P+Q137K+V159M+K169R+V203T+G237M+T244R+V251E+S256E+I294E、

[0503] Q82E+P111Q+S123P+L152P+V159M+K169R+V203T+G237M+T244R+S256E+I294E、

[0504] Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E+N383Q+V431E、

[0505] R20K+S76E+Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E+Q329E+P492D、

[0506] S76E+Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E+Q329E+E489R+P492D、

[0507] Q82E+P111Q+S123P+Q137K+N155D+V159M+K169R+V203T+G237M+T244R+S256E+I294E+K445E、

[0508] S76E+Q82E+S94R+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E、

[0509] K8E+A41L+S76E+Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E、

[0510] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256E+Q271E+I294E+Q329E+P339S+N383E+S402Q+V431E、

[0511] S76E+Q82E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q+V431E、

[0512] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K252E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V、

[0513] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q+V431E、

[0514] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+K240F+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V、

[0515] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V219T+G237M+S256Q+Q271E+I294E+Q329E+S402Q+V431E+S474E、

[0516] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+P492D、

[0517] S76E+A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V、

[0518] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+A189G+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q+V431E、

[0519] K8E+A41L+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+K394R+S402Q+V431E,

[0520] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271D+I294E+Q329E+N383E+S402Q+V431E+A459P,

[0521] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+K347E+N383E+S402Q+V431E+A491V,

[0522] K8E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V,

[0523] K8R+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E+E489K,

[0524] A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V, wherein the variant has xyloglucanase activity and wherein the variant has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, for example, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3.

[0525] Variations may be further included in substitutions at one or more other locations, such as those described in WO 2009 / 147210.

[0526] Amino acid alterations can be minor, i.e., conserved amino acid substitutions or insertions that do not significantly affect protein folding and / or activity; typically small deletions of 1–30 amino acids; small N-terminal or C-terminal extensions, such as methionine residues at the N-terminus; small linker peptides of up to 20–25 residues; or small extensions that facilitate purification by altering net charge or another function (such as polyhistidine fragments, antigenic epitopes, or binding domains).

[0527] Examples of conserved substitutions are found in the following group: 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 generally do not alter specific reactivity are known in the art and are described, for example, by H. Neurath and RL Hill, 1979, in *The Proteins*, Academic Press, New York. Common substitutes are Ala / Ser, Val / Ile, Asp / Glu, Thr / Ser, Ala / Gly, Ala / Thr, Ser / Asn, Ala / Val, Ser / Gly, Tyr / Phe, Ala / Pro, Lys / Arg, Asp / Asn, Leu / Ile, Leu / Val, Ala / Glu, and Asp / Gly.

[0528] Alternatively, these amino acid changes have the property of altering the physicochemical properties of the peptide. For example, amino acid changes can improve the peptide's thermal stability, alter its substrate specificity, change its optimal pH, and so on.

[0529] Essential amino acids in peptides can be identified using 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, a single alanine mutation is introduced at each residue in the molecule, and the xyloglucanase activity of the resulting mutant molecule is tested to identify amino acid residues essential to the activity of the molecule. See also Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708. The active sites of enzymes or other biological interactions can also be determined by physical analysis of the structure, such as by techniques including nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, along with mutation of the amino acid at the putative contact site. 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 comparisons with relevant polypeptides and described, for example, in WO 2009 / 147210.

[0530] These variants can consist of 445 to 524 amino acids, such as 471 to 524 amino acids or 497 to 524 amino acids.

[0531] In the examples, this variant exhibits improved washing performance compared to the parent enzyme.

[0532] In the examples, this variant has improved enzyme washing benefits compared to the parent enzyme.

[0533] In the examples, this variant exhibits improved stability compared to the parent enzyme.

[0534] In the examples, this variant exhibits improved thermal stability compared to the parent enzyme.

[0535] In the examples, this variant exhibits improved in-detergent storage stability compared to the parent enzyme.

[0536] In the examples, this variant exhibits improved whiteness compared to the parent enzyme.

[0537] Parental xyloglucanase

[0538] The parental xyloglucanase can be a polypeptide with at least 60% sequence identity to the polypeptide of SEQ ID NO: 1.

[0539] In one aspect, the parent has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with the polypeptide of SEQ ID NO: 1, and the parent has xyloglucanase activity. In another aspect, the amino acid sequence of the parent differs from that of the polypeptide of SEQ ID NO: 1 by up to 10 amino acids, for example, 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10. In another aspect, the parent comprises or is composed of the amino acid sequence of SEQ ID NO: 1. In yet another aspect, the parent is a fragment of the polypeptide of SEQ ID NO: 1 containing at least 445 amino acid residues, for example, at least 471 amino acid residues, and at least 497 amino acid residues.

[0540] In one aspect, the parent has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with the polypeptide of SEQ ID NO: 2, and the parent has xyloglucanase activity. In another aspect, the amino acid sequence of the parent differs from that of the polypeptide of SEQ ID NO: 2 by up to 10 amino acids, for example, 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10. In another aspect, the parent comprises or consists of the amino acid sequence of SEQ ID NO: 2. In yet another aspect, the parent is a fragment of the polypeptide of SEQ ID NO: 2 containing at least 445 amino acid residues, for example, at least 471 amino acid residues, and at least 497 amino acid residues.

[0541] In one aspect, the parent has at least 60%, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity with the polypeptide of SEQ ID NO: 3, and the parent has xyloglucanase activity. In another aspect, the amino acid sequence of the parent differs from that of the polypeptide of SEQ ID NO: 3 by up to 10 amino acids, for example, 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10. In another aspect, the parent comprises or is composed of the amino acid sequence of SEQ ID NO: 3. In yet another aspect, the parent is a fragment of the polypeptide of SEQ ID NO: 3 containing at least 445 amino acid residues, for example, at least 471 amino acid residues, and at least 497 amino acid residues.

[0542] Parental polypeptides can be hybrid polypeptides, in which a region of one polypeptide is fused to the N-terminus or C-terminus of a region of another polypeptide.

[0543] The parent peptide can be a fusion peptide or a cleavable fusion peptide, wherein another peptide is fused at the N-terminus or C-terminus of the peptide of the present invention. Fusion peptides are generated by fusing a polynucleotide encoding another peptide with the polynucleotide of the present invention. Techniques for generating fusion peptides are known in the art and include linking the coding sequences of the peptides such that they conform to reading frames, and that the expression of the fusion peptide is under the control of one or more identical promoters and terminators. Fusion peptides can also be constructed using intron technology, wherein the fusion peptide is generated post-translational (Cooper et al., 1993, EMBO J. [Journal of the European Society for Molecular Biology] 12: 2575-2583; Dawson et al., 1994, Science 266: 776-779).

[0544] The fusion peptide may further include a cleavage site between the two peptides. Upon secretion of the fusion protein, this site is cleaved, releasing both peptides. Examples of cleavage sites include, but are not limited to, those disclosed in the following literature: Martin et al., 2003, J. Ind. Microbiol. Biotechnol. [Journal of Industrial Microbiology and Biotechnology] 3: 568-576; Svetina et al., 2000, J. Biotechnol. [Journal of Biotechnology] 76: 245-251; Rasmussen-Wilson et al., 1997, Appl. Environ. Microbiol. [Applied and Environmental Microbiology] 63: 3488-3493; Ward et al., 1995, Biotechnology [Biotechnology] 13: 498-503; and Contreras et al., 1991, Biotechnology [Biotechnology] 9: 378-381; Eaton et al., 1986, Biochemistry [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.

[0545] Parental lines can be obtained from any genus of microorganisms. For the purposes of this invention, the term "obtained from" as used herein in conjunction with a given source should mean that a parental line encoded by a polynucleotide is produced by that source or by a strain in which a polynucleotide from that source has been inserted. In one aspect, the parental line is extracellularly secreted.

[0546] In another aspect, the parent xyloglucanase can be a bacterial xyloglucanase. For example, the xyloglucanase can be a Gram-positive bacterial polypeptide, such as Bacillus, preferably from the subphylum Bacillus / Lactobacillus, preferably from a species of Paenibacillus, especially Polymyxobacterium, such as Polymyxobacterium ATCC 832. Preferably, the xyloglucanase is a family 44 xyloglucanase, for example, as described in WO 01 / 62903.

[0547] It should be understood that, for the aforementioned species, this invention covers complete and incomplete stages, as well as other taxonomic equivalents, such as asexual forms, regardless of their known species names. Those skilled in the art will readily identify the appropriate equivalents.

[0548] Strains of these species are readily available to the public at many culture collections, such as the American Type Culture Collection (ATCC), the German Microbial Culture Collection (DSMZ), the Centralbureau Voor Schimmelcultures (CBS), and the Agricultural Research Service Patent Culture Collection, Northern Regional Research Center (NRRL).

[0549] The aforementioned probes can be used to identify and obtain the parent from other sources, including microorganisms isolated from nature (e.g., soil, compost, water, etc.) or DNA samples obtained directly from natural materials (e.g., soil, compost, water, etc.). Techniques for directly isolating microorganisms and DNA from natural habitats are well known in the art. The polynucleotide encoding the parent can then be obtained by similarly screening a library of genomic DNA or cDNA of another microorganism or a mixed DNA sample. Once the polynucleotide encoding the parent has been detected with one or more probes, it can be isolated or cloned using techniques known to those skilled in the art (see, for example, Sambrook et al., 1989, ibid.).

[0550] Preparation of variants

[0551] The present invention also relates to methods for obtaining variants having xyloglucanase activity, the methods comprising: (a) introducing a modified polypeptide of SEQ ID NO: 1 at one or more positions corresponding to positions selected from the group consisting of: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 237, 238, 240 243, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505, wherein the variant has xyloglucanase activity; and (b) the variant is recovered.

[0552] Variants can be prepared using any mutagenesis procedure known in the art, such as site-directed mutagenesis, synthetic gene construction, semi-synthetic gene construction, random mutagenesis, shuffling, etc.

[0553] Site-directed mutagenesis is a technique that introduces one or more (e.g., several) mutations at one or more designated sites in a polynucleotide encoding the parent.

[0554] Site-directed mutagenesis can be achieved in vitro via PCR involving primers containing oligonucleotides with the desired mutation. Site-directed mutagenesis can also be performed in vitro via cassette mutagenesis, which involves cleavage by a restriction enzyme at a site in a plasmid containing a polynucleotide encoding the parent, followed by ligation of the mutated oligonucleotide into the polynucleotide. Typically, the restriction enzymes digesting the plasmid and the oligonucleotide are the same, allowing the sticky ends of the plasmid and the insert to ligate together. See, for example, Scherer and Davis, 1979, Proc. Natl. Acad. Sci. USA [Proceedings of the National Academy of Sciences] 76: 4949-4955; and Barton et al., 1990, Nucleic Acids Res. [Nucleic Acids Research] 18: 7349-4966.

[0555] Site-directed mutagenesis can also be achieved in vivo using methods known in the art. See, for example, U.S. Patent Application Publication No. 2004 / 0171154; Storici et al., 2001, Nature Biotechnol. 19:773-776; Kren et al., 1998, Nat. Med. 4: 285-290; and Calissano and Macino, 1996, Fungal Genet. Newslett. 43: 15-16.

[0556] Any site-directed mutagenesis procedure can be used in this invention. Many commercially available kits are available for preparing variants.

[0557] Synthetic gene construction requires the in vitro synthesis of designed polynucleotide molecules to encode target peptides. Gene synthesis can be performed using a variety of techniques, such as the multi-channel microchip-based technique described by Tian et al. (2004, Nature 432: 1050-1054), and similar techniques for synthesizing and assembling oligonucleotides on optically programmable microfluidic chips.

[0558] Known mutagenesis, recombination, and / or tampering methods can be used, followed by relevant screening procedures to make and test single or multiple amino acid substitutions, deletions, and / or insertions, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95 / 17413; or WO 95 / 22625. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991, Biochemistry 30: 10832-10837; US Patent No. 5,223,409; WO 92 / 06204), and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Ner et al., 1988, DNA 7:127).

[0559] Mutagenesis / recombination methods can be combined with high-throughput, automated screening methods to detect the activity of cloned, mutagenesis-encoded peptides expressed by host cells (Ness et al., 1999, Nature Biotechnology 17: 893-896). Mutagenesis-encoded DNA molecules encoding active peptides can be recovered from host cells and rapidly sequenced using standard methods in the art. These methods allow for the rapid determination of the importance of individual amino acid residues within the peptide.

[0560] Semi-synthetic gene construction is achieved through a combination of synthetic gene construction, and / or site-directed mutagenesis, and / or random mutagenesis, and / or shuffling. Semi-synthetic construction typically combines the process of synthesizing polynucleotide fragments with PCR technology. Therefore, specific regions of the gene can be synthesized de novo, while other regions can be amplified using site-specific mutagenesis primers, and still others can be amplified using error-prone or non-error-prone PCR. The polynucleotide subsequence can then be shuffled.

[0561] Polynucleotides

[0562] The present invention also relates to polynucleotides encoding variants of the invention.

[0563] Nucleic acid constructs

[0564] The present invention also relates to a nucleic acid construct comprising a polynucleotide operably linked to one or more control sequences encoding a variant of the invention, the one or more control sequences guiding the expression of the coding sequence in a suitable host cell under conditions compatible with the control sequences.

[0565] Polynucleotides can be manipulated in a variety of ways to provide expression of variants. Depending on the expression vector, manipulation of the polynucleotide prior to insertion into the vector may be desired or necessary. Techniques for modifying polynucleotides using recombinant DNA methods are well known in the art.

[0566] The control sequence can be a promoter, a polynucleotide that is recognized by the host cell for expression. A promoter contains a transcriptional control sequence that mediates the expression of a variant. A promoter can be any polynucleotide that exhibits transcriptional activity in the host cell, including mutant promoters, truncated promoters, and heterozygous promoters, and can be derived from a gene encoding an extracellular or intracellular polypeptide that is homologous or heterologous to that of the host cell.

[0567] Examples of suitable promoters for directing the transcription of the nucleic acid constructs of this invention in bacterial host cells are promoters obtained from the following genes: Bacillus amyloliquefaciens α-amylase gene (amyQ), Bacillus licheniformis α-amylase gene (amyL), Bacillus licheniformis penicillinase gene (penP), Bacillus stearothermophilus maltose amylase gene (amyM), Bacillus subtilis fructansucrosease gene (sacB), Bacillus subtilis xylA and xylB genes, Bacillus thuringiensis cryIIIA gene (Agaisse and Lereclus, 1994, Molecular Microbiology 13: 97-107), Escherichia coli lac operon, and Escherichia coli trc promoter (Egon et al., 1988, Gene). 69: 301-315), the *Streptomyces coelicolor* agar hydrolase gene (dagA) and the prokaryotic β-lactamase gene (Villa-Kamaroff et al., 1978, Proc. Natl. Acad. Sci. USA [Proceedings of the National Academy of Sciences] 75: 3727-3731), and the tac promoter (DeBoer et al., 1983, Proc. Natl. Acad. Sci. USA [Proceedings of the National Academy of Sciences] 80: 21-25). Other promoters are described in Gilbert et al., 1980, Scientific American 242: 74-94, “Useful proteins from recombinant bacteria”; and Sambrook et al., 1989, ibid. Examples of tandem promoters are disclosed in WO 99 / 43835.

[0568] Examples of suitable promoters for guiding the transcription of the nucleic acid constructs of this invention in filamentous fungal host cells are promoters obtained from the genes of the following enzymes: Aspergillus nidulans acetamase, Aspergillus niger neutral α-amylase, Aspergillus niger acid-stable α-amylase, Aspergillus niger or Aspergillus awamori glucosylamylase (glaA), Aspergillus oryzae TAKA amylase, Aspergillus oryzae alkaline protease, Aspergillus oryzae triose phosphate isomerase, Fusarium oxysporum trypsin-like protease (WO 96 / 00787), Fusarium venenatum amylase (WO 00 / 56900), Fusarium venenatum Daria (WO 00 / 56900), Fusarium venenatum Quinn (WO 96 / 00787). 00 / 56900), Rhizomucormiehei lipase, Rhizomucormiehei aspartic protease, Trichoderma reesei β-glucosidase, Trichoderma reesei cellobiose hydrolase I, Trichoderma reesei cellobiose hydrolase II, Trichoderma reesei endoglucanase I, Trichoderma reesei endoglucanase II, Trichoderma reesei endoglucanase III, Trichoderma reesei endoglucanase IV, Trichoderma reesei endoglucanase V, Trichoderma reesei xylanase I, Trichoderma reesei xylanase II, Trichoderma reesei β-xylosidase , and the NA2-tpi promoter (a modified promoter derived from the Aspergillus neutral α-amylase gene, wherein the untranslated leader sequence is replaced by an untranslated leader sequence from the Aspergillus triose phosphate isomerase gene; non-restrictive examples include modified promoters derived from the Aspergillus niger neutral α-amylase gene, wherein the untranslated leader sequence has been replaced by an untranslated leader sequence from the Aspergillus nidus or Aspergillus oryzae triose phosphate isomerase gene); and its mutant promoters, truncated promoters and heterozygous promoters.

[0569] In yeast hosts, useful promoters are derived from the following genes: *Saccharomyces cerevisiae* enolase (ENO-1), *Saccharomyces cerevisiae* galactokinase (GAL1), *Saccharomyces cerevisiae* alcohol dehydrogenase / glyceraldehyde-3-phosphate dehydrogenase (ADH1, ADH2 / GAP), *Saccharomyces cerevisiae* triose phosphate isomerase (TPI), *Saccharomyces cerevisiae* metallothionein (CUP1), and *Saccharomyces cerevisiae* 3-phosphate glycerate kinase. Other useful promoters in yeast host cells are described by Romanos et al., 1992, Yeast [Yeast] 8: 423-488.

[0570] The control sequence can also be a transcription terminator recognized by the host cell to terminate transcription. The terminator sequence is operatively linked to the 3' end of the polynucleotide encoding that variant. Any terminator that is functional in the host cell can be used.

[0571] The preferred terminator for bacterial host cells is obtained from the following genes: Bacillus clausii alkaline protease (aprH), Bacillus licheniformis α-amylase (amyL), and Escherichia coli ribosomal RNA (rrnB).

[0572] The preferred terminator for filamentous fungal host cells is derived from the following genes: Aspergillus nidulans o-aminobenzoic acid synthase, Aspergillus niger glucosidase, Aspergillus niger α-glucosidase, Aspergillus oryzae TAKA amylase, and Fusarium oxysporum trypsin-like protease.

[0573] Preferred terminators for yeast host cells are derived from the following genes: *Saccharomyces cerevisiae* enolase, *Saccharomyces cerevisiae* cytochrome C (CYC1), and *Saccharomyces cerevisiae* glyceraldehyde-3-phosphate dehydrogenase. Other useful terminators for yeast host cells are described by Romanos et al. (1992, ibid.).

[0574] Control sequences can also be mRNA stabilizer regions downstream of the promoter and upstream of the gene's coding sequence, which increase the expression of the gene.

[0575] Examples of suitable mRNA stable regions are obtained from the following: Bacillus thuringiensis cryIIIA gene (WO94 / 25612) and Bacillus subtilis SP82 gene (Hue et al., 1995, Journal of Bacteriology 177: 3465-3471).

[0576] The control sequence can also be a leader sequence, which is the untranslated region of mRNA that is important for translation in the host cell. The leader sequence is operatively linked to the 5' end of the polynucleotide encoding that variant. Any leader sequence that is functional in the host cell can be used.

[0577] The preferred leader sequence for filamentous fungal host cells is obtained from the following genes: Aspergillus oryzae TAKA amylase and Aspergillus nidulans triose phosphate isomerase.

[0578] The appropriate leader sequence for yeast host cells is obtained from the following genes: Saccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiae 3-phosphoglycerate kinase, Saccharomyces cerevisiae α-factor, and Saccharomyces cerevisiae alcohol dehydrogenase / glyceraldehyde-3-phosphate dehydrogenase (ADH2 / GAP).

[0579] The control sequence can also be a polyadenylation sequence, which is a sequence operatively linked to the 3' end of the variant coding sequence and recognized by the host cell during transcription as a signal to add polyadenylation residues to the transcribed mRNA. Any polyadenylation sequence that is functional in the host cell can be used.

[0580] Preferred polyadenylation sequences for use in filamentous fungal host cells are derived from the genes of the following enzymes: Aspergillus nidulans anaminobenzoic acid synthase, Aspergillus niger glucosidase, Aspergillus niger α-glucosidase, Aspergillus oryzae TAKA amylase, and Fusarium oxysporum trypsin-like protease.

[0581] Useful polyadenylation sequences in yeast host cells are described by Guo and Sherman, 1995, Mol. Cellular Biol. [Molecular Cell Biology] 15: 5983-5990.

[0582] The control sequence can also be a signal peptide coding region that encodes a signal peptide linked to the N-terminus of the variant and directs the variant's entry into the cell's secretory pathway. The 5' end of the polynucleotide coding sequence may inherently contain a signal peptide coding sequence naturally linked within the translation reading frame to a segment encoding the variant's coding sequence. Alternatively, the 5' end of the coding sequence may contain a foreign signal peptide coding sequence relative to the coding sequence. In cases where the coding sequence does not naturally contain a signal peptide coding sequence, a foreign signal peptide coding sequence may be required. Alternatively, a foreign signal peptide coding sequence may simply replace the natural signal peptide coding sequence to enhance the variant's secretion. However, any signal peptide coding sequence that directs the expressed variant into the host cell's secretory pathway can be used.

[0583] The effective signal peptide coding sequences for bacterial host cells are derived from the following genes: maltose amylase produced by Bacillus NCIB 11837, subtilisin produced by Bacillus licheniformis, β-lactamase produced by Bacillus licheniformis, α-amylase produced by Bacillus thermophilus, neutral proteases (nprT, nprS, nprM) produced by Bacillus thermophilus, and prsA produced by Bacillus subtilis. Additional signal peptides are described by Simonen and Palva, 1993, Microbiological Reviews 57: 109-137.

[0584] The effective signal peptide coding sequences for filamentous fungal host cells are obtained from the following genes: Aspergillus niger neutral amylase, Aspergillus niger glucosylase, Aspergillus oryzae TAKA amylase, Humicolainsolens cellulase, Humicolainsolens endoglucanase V, Humicola lanuginosa lipase, and Rhizopus oryzae aspartic protease.

[0585] Useful signal peptides for yeast host cells are obtained from the genes of Saccharomyces cerevisiae α-factor and Saccharomyces cerevisiae invertase. Other useful signal peptide coding sequences are described by Romanos et al. (1992, ibid.).

[0586] The control sequence can also be a propeptide-coding sequence encoding a propeptide located at the N-terminus of the variant. The resulting polypeptide is called a proenzyme or propeptide progenitor (or, in some cases, a zymogen). The propeptide progenitor is usually inactive and can be converted into an active polypeptide by catalytic cleavage or autocatalytic cleavage of the propeptide progenitor. Propeptide-coding sequences can be obtained from the following genes: Bacillus subtilis alkaline protease (aprE), Bacillus subtilis neutral protease (nprT), Myceliophthora thermophila laccase (WO 95 / 33836), Rhizopus miltiorrhiza aspartic protease, and Saccharomyces cerevisiae α-factor.

[0587] In the presence of both the signal peptide sequence and the propeptide sequence, the propeptide sequence is positioned immediately adjacent to the N-terminus of the variant, and the signal peptide sequence is positioned immediately adjacent to the N-terminus of the propeptide sequence.

[0588] Also desirable is the addition of regulatory sequences that modulate variant expression relative to the growth of the host cell. Examples of regulatory systems are those that cause gene expression to turn on or off in response to chemical or physical stimuli, including the presence of regulatory compounds. Regulatory systems in prokaryotes include the lac, tac, and trp operon systems. In yeast, the ADH2 or GAL1 system can be used. In filamentous fungi, the *Aspergillus niger* glucosylamylase promoter, the *Aspergillus oryzae* TAKA α-amylase promoter, and the *Aspergillus oryzae* glucosylamylase promoter can be used. Other examples of regulatory sequences are those that amplify genes. In eukaryotic systems, these regulatory sequences include dihydrofolate reductase genes amplified in the presence of methotrexate and metallothionein genes amplified with heavy metals. In these cases, the polynucleotide encoding the variant will be operatively linked to the regulatory sequence.

[0589] expression carrier

[0590] The present invention also relates to recombinant expression vectors comprising a polynucleotide encoding a variant of the invention, a promoter, and transcription and translation termination signals. Various nucleotides and control sequences can be linked together to produce a recombinant expression vector, which may include one or more suitable restriction sites to allow insertion or substitution of the polynucleotide encoding the variant at such sites. Alternatively, the polynucleotide can be expressed by inserting the polynucleotide or a nucleic acid construct containing the polynucleotide into a suitable vector for expression. In producing the expression vector, the coding sequence is positioned in the vector such that the coding sequence is operatively linked to a suitable control sequence for expression.

[0591] Recombinant expression vectors can be any vector (e.g., plasmids or viruses) that can readily undergo recombinant DNA procedures and induce polynucleotide expression. The choice of vector will typically depend on its compatibility with the host cell to which it will be introduced. Vectors can be linear or closed circular plasmids.

[0592] The vector can be a self-replicating vector, that is, a vector that exists as an extrachromosomal entity and replicates independently of chromosome replication, such as a plasmid, extrachromosomal element, microchromosome, or artificial chromosome. The vector can contain any tools used to ensure self-replication. Alternatively, the vector can be one that, when introduced into a host cell, integrates into the genome and replicates along with one or more chromosomes in which it has been integrated. Furthermore, a single vector or plasmid, or two or more vectors or plasmids collectively containing the total DNA of the host cell genome to be introduced, or transposons can be used.

[0593] The vector preferably contains one or more selective markers that allow for convenient selection of cells such as transformed cells, transfected cells, and transduced cells. A selective marker is a gene whose product provides resistance to biocides or viruses, resistance to heavy metals, or prototrophic auxotrophic traits, etc.

[0594] Examples of selective bacterial markers include the dal gene in Bacillus licheniformis or Bacillus subtilis, or markers that confer antibiotic resistance (such as ampicillin, chloramphenicol, kanamycin, neomycin, spectinomycin, or tetracycline resistance). Suitable markers for yeast host cells include, but are not limited to, ADE2, HIS3, LEU2, LYS2, MET3, TRP1, and URA3. Selective markers for use in filamentous fungal host cells include, but are not limited to, amdS (acetamipase), argB (ornithine carbamoyltransferase), bar (glufosinate-amylase), hph (hygromycin phosphotransferase), niaD (nitrate reductase), pyrG (orotidine-5'-phosphate decarboxylase), sC (adenosyl sulfate transtransferase), and trpC (o-aminobenzoic acid synthase), along with their equivalents. Preferred markers for use in Aspergillus cells are the amdS and pyrG genes from Aspergillus nidus or Aspergillus oryzae, and the bar gene from Streptomyces hygroscopicus.

[0595] The vector preferably contains one or more elements that allow the vector to integrate into the host cell’s genome or to replicate autonomously in the cell independently of the genome.

[0596] To integrate into the host cell genome, the vector can rely on a coding variant polynucleotide sequence or any other vector element for integration into the genome via homologous or non-homologous recombination. Alternatively, the vector can contain additional polynucleotides to guide integration into one or more precise locations on one or more chromosomes within the host cell genome via homologous recombination. To increase the likelihood of integration at precise locations, the integrative element should contain a sufficient number of nucleic acids, such as 100 to 10,000 base pairs, 400 to 10,000 base pairs, and 800 to 10,000 base pairs, that have high sequence identity with the corresponding target sequence to enhance the probability of homologous recombination. The integrative element can be any sequence homologous to the target sequence within the host cell genome. Furthermore, the integrative element can be a non-coding or coding polynucleotide. On the other hand, the vector can integrate into the host cell genome via non-homologous recombination.

[0597] For autonomous replication, the vector may further include an origin of replication, which enables the vector to replicate autonomously within the host cell discussed in this context. The origin of replication can be any plasmid replicon that mediates autonomous replication and functions within the cell. The terms "origin of replication" or "plasmid replicon" refer to the polynucleotide that enables a plasmid or vector to replicate in vivo.

[0598] Examples of bacterial origins of replication are the origins of replication of plasmids pBR322, pUC19, pACYC177, and pACYC184, which allow replication in Escherichia coli, and the origins of replication of plasmids pUB110, pE194, pTA1060, and pAMß1, which allow replication in Bacillus.

[0599] Examples of replication origins used in yeast host cells include the 2-micron replication origin, ARS1, ARS4, a combination of ARS1 and CEN3, and a combination of ARS4 and CEN6.

[0600] Examples of useful origins of replication in filamentous fungal cells are AMA1 and ANS1 (Gems et al., 1991, Gene 98: 61-67; Cullen et al., 1987, Nucleic Acids Res. 15: 9163-9175; WO 00 / 24883). The AMA1 gene can be isolated and plasmids or vectors containing it can be constructed according to the methods disclosed in WO 00 / 24883.

[0601] More than one copy of the polynucleotide of the present invention can be inserted into a host cell to increase the generation of variants. An increased number of copies of the polynucleotide can be obtained by integrating at least one additional copy of the sequence into the host cell genome or by including an amplifiable selectable marker gene along with the polynucleotide, wherein cells containing amplified copies of the selectable marker gene and thus additional copies of the polynucleotide can be selected by culturing cells in the presence of a suitable selectivity reagent.

[0602] The procedures for connecting the above-described elements to construct the recombinant expression vector of the present invention are well known to those skilled in the art (see, for example, Sambrook et al., 1989, ibid.).

[0603] host cells

[0604] This invention also relates to recombinant host cells containing a polynucleotide operably linked to one or more control sequences encoding variants of the invention, which in turn direct the generation of variants of the invention. A construct or vector containing the polynucleotide is introduced into the host cell such that the construct or vector is maintained as a chromosomal integrase or as a self-replicating extrachromosomal vector, as previously described. The term "host cell" encompasses any parental cell progeny that is not identical to the parental cell due to mutations occurring during replication. The selection of the host cell will depend largely on the gene encoding the variant and its origin.

[0605] The host cell can be any cell that is useful in the recombinant production of variants, such as prokaryotes or eukaryotes.

[0606] Prokaryotic host cells can be any Gram-positive or Gram-negative bacteria. Gram-positive bacteria include, but are not limited to: Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Oceanobacillus, Staphylococcus, Streptococcus, and Streptomyces. Gram-negative bacteria include, but are not limited to: Campylobacter, Escherichia coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.

[0607] The bacterial host cell can be any Bacillus genus cell, including but not limited to Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus croceus, Bacillus coagulans, Bacillus firmus, Bacillus lautus, Bacillus tibetica, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus stearophilus, Bacillus subtilis, and Bacillus thuringiensis cells.

[0608] The bacterial host cell can also be any streptococcus cell, including but not limited to Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis, and Streptococcus equi subsp. Zooepidemicus.

[0609] The bacterial host cell can also be any Streptomyces cell, including but not limited to Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces griseus, and Streptomyces lividans.

[0610] DNA can be introduced into Bacillus cells through the following methods: protoplast transformation (see, for example, Chang and Cohen, 1979, Mol. Gen. Genet. [Molecular Genetics and Genomics] 168: 111-115), competent cell transformation (see, for example, Young and Spizizen, 1961, J. Bacteriol. [Journal of Bacteriology] 81:823-829; or Dubnau and Davidoff-Abelson, 1971, J. Mol. Biol. [Journal of Molecular Biology] 56:209-221), electroporation (see, for example, Shigekawa and Dower, 1988, Biotechniques [Biotechnology] 6:742-751), or conjugation (see, for example, Koehler and Thorne, 1987, J. Bacteriol. [Journal of Bacteriology] 169: 5271-5278). DNA can be introduced into E. coli cells through protoplast transformation (see, for example, Hanahan, 1983, J. Mol. Biol. [Journal of Molecular Biology] 166: 557-580) or electroporation (see, for example, Dower et al., 1988, Nucleic Acids Res. [Nucleic Acid Research] 16: 6127-6145). DNA can be introduced into Streptomyces cells through protoplast transformation, electroporation (see, for example, Gong et al., 2004, Folia Microbiol. (Praha) [Leaf Microbiology (Praha)] 49: 399-405), conjugation (see, for example, Mazodier et al., 1989, J. Bacteriol. [Journal of Bacteriology] 171: 3583-3585), or transduction (see, for example, Burke et al., 2001, Proc. Natl. Acad. Sci. USA [Proceedings of the National Academy of Sciences of the United States of America] 98: 6289-6294). DNA can be introduced into Pseudomonas cells by electroporation (see, for example, Choi et al., 2006, J. Microbiol. Methods 64: 391-397) or conjugation (see, for example, Pinedo and Smets, 2005, Appl. Environ. Microbiol. 71: 51-57).Introducing DNA into Streptococcus cells can be achieved through: native competent cells (see, for example, Perry and Kuramitsu, 1981, Infect. Immun. 32: 1295-1297), protoplast transformation (see, for example, Catt and Jollick, 1991, Microbios 68: 189-207), electroporation (see, for example, Buckley et al., 1999, Appl. Environ. Microbiol. 65: 3800-3804), or conjugation (see, for example, Clewell, 1981, Microbiol. Rev. 45: 409-436). However, any method known in the art for introducing DNA into host cells can be used.

[0611] The host cell can also be a eukaryotic cell, such as a mammalian, insect, plant, or fungal cell.

[0612] The host cell can be a fungal cell. As used herein, “fungus” includes Ascomycota, Basidiomycota, Chytridiomycota, Zygomycota, Oomycota, and all mitotic fungi (as defined by Hawksworth et al. in Ainsworth and Bisby’s Dictionary of The Fungi, 8th edition, 1995, CAB International, University Press, Cambridge, UK).

[0613] The host cell for fungi can be a yeast cell. As used herein, “yeast” includes ascosporogenous yeast (Endomycetales), basidiosporogenous yeast, and yeasts belonging to the class Fungi Imperfecti (Blastomycetes). Because yeast classification may change in the future, for the purposes of this invention, yeast should be defined as described in *Biology and Activities of Yeast* (edited by Skinner, Passmore, and Davenport, Soc. App. Bacteriol. Symposium Series No. 9, 1980).

[0614] Yeast host cells can be cells from the genera *Candida*, *Hansenula*, *Kluyveromyces*, *Pichia*, *Saccharomyces*, *Schizosaccharomyces*, or *Yarrowia*, such as *Kluyveromyces lactis*, *Saccharomyces carlsbergensis*, *Saccharomyces diastaticus*, *Saccharomyces douglasii*, *Saccharomyces kluyveri*, *Saccharomyces norbensis*, *Saccharomyces oviformis*, or *Yarrowia lipolytica*.

[0615] Fungal host cells can be filamentous fungal cells. "Filamentous fungi" includes all filamentous forms within the phylum Eumycota and the subphylum Oomycetes (as defined by Hawksworth et al., 1995, ibid.). Filamentous fungi are generally characterized by a hyphal wall composed of chitin, cellulose, glucan, chitosan, mannan, and other complex polysaccharides. Vegetative growth occurs through hyphal elongation, and carbon metabolism is obligate aerobic. In contrast, yeast (such as Saccharomyces cerevisiae) undergoes vegetative growth through budding of single-celled cells, and carbon metabolism can be fermentative.

[0616] The host cells of filamentous fungi can be *Acremonium*, *Aspergillus*, *Aureobasidium*, *Bjerkandera*, *Ceriporiopsis*, *Chrysosporium*, *Coprinus*, *Coriolus*, *Cryptococcus*, *Filibasidium*, *Fusarium*, *Humicola*, *Magnaporthe*, *Mucor*, and *Myceliop*. hthora, Neocallimastix, Neurospora, Paecilomyces, Penicillium, Phanerochaete, Phlebia, Piromyces, Pleurotus, Schizophyllum, Bassicrys, Thermoascus, Thievia, Tolypocladium, Trametes, or Trichoderma cells.

[0617] For example, the host cells of filamentous fungi can be *Aspergillus foetidus*, *Aspergillus fumigatus*, *Aspergillus japonicus*, *Aspergillus nidus*, *Aspergillus niger*, *Aspergillus oryzae*, *Bjerkandera adusta*, *Ceriporiopsis aneirina*, *Ceriporiopsis caregiea*, *Ceriporiopsis gilvescens*, *Ceriporiopsis pannocinta*, *Ceriporiopsis rivulosa*, *Ceriporiopsis subrufa*, *Ceriporiopsis subvermispora*, *Chrysosporium inops*, and *Chrysosporium horneri*. *Chrysosporium keratinophilum*, *Chrysosporium lucknowense*, *Chrysosporium merdarium*, *Chrysosporium pannicola*, *Chrysosporium queenslandicum*, *Chrysosporium tropicum*, *Chrysosporium zonatum*, *Coprinus cinereus*, *Coriolushirsutus*, *Fusarium bactridioides*, *Fusarium cerealis*, *Fusarium crookwellense*, *Fusarium culmorum*, *Fusarium graminearum*, *Fusarium graminum*, *Fusarium heterosporum*, *Fusarium scabra* Fusarium negundi, Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusarium elderberry*Fusarium sarcochroum*, *Fusarium sporotrichioides*, *Fusarium sulphureum*, *Fusarium torulosum*, *Fusarium torulosum*, *Fusarium sporotrichioides*, *Mucor miehei*, *Neurospora crassa*, *Penicillium purpurogenum*, *Phanerochaete chrysosporium*, *Phlebia radiata*, *Pleurotus eryngii*, *Thielavia terrestris*, *Trametes villosa*, *Trametes versicolor*, *Trichoderma* Trichoderma harzianum, Trichoderma koningii, Trichoderma longibrachiatum, Trichoderma reesei, or green Trichoderma cells.

[0618] Fungal cells can be transformed in a manner known per se through processes involving protoplast formation, protoplast transformation, and cell wall regeneration. Suitable procedures for transforming Aspergillus and Trichoderma host cells are described in EP 238023 and Yelton et al., 1984, Proc. Natl. Acad. Sci. USA [Proceedings of the National Academy of Sciences] 81: 1470-1474, and Christensen et al., 1988, Bio / Technology [Biology / Technology] 6: 1419-1422. Suitable methods for transforming Fusarium species are described by Malardier et al., 1989, Gene [Gene] 78: 147-156 and WO 96 / 00787. Yeast can be transformed using procedures described in the following literature: Becker and Guarente, in Abelson, JN and Simon, MI (eds.), Guide to Yeast Genetics and Molecular Biology, Methods in Enzymology, Vol. 194, pp. 182-187, Academic Press, Inc., New York; Ito et al., 1983, J. Bacteriol. 153: 163; and Hinnen et al., 1978, Proc. Natl. Acad. Sci. USA 75: 1920.

[0619] Production methods

[0620] The present invention also relates to methods for generating variants, the methods comprising: (a) culturing the recombinant host cells of the present invention under conditions suitable for the expression of the variant; and optionally (b) recovering the variant.

[0621] Recombinant host cells are cultured in a nutrient medium suitable for generating variants using methods known in the art. For example, cells can be cultured by shake flask culture or by small-scale or large-scale fermentation (including continuous fermentation, batch fermentation, feed-feed fermentation, or solid-state fermentation) in a suitable medium and under conditions that allow for variant expression and / or isolation in a laboratory or industrial fermenter. Using procedures known in the art, culture occurs in a suitable nutrient medium containing carbon and nitrogen sources and inorganic salts. Suitable media are available from commercial suppliers or can be prepared according to publicly available compositions (e.g., in the catalogue of the U.S. Center for Type Culture Collection). If the variant is secreted into the nutrient medium, the variant can be recovered directly from the medium. If the variant is not secreted, it can be recovered from cell lysates.

[0622] The variant can be detected using methods known in the art that are specific to the variant. These detection methods include, but are not limited to, the use of specific antibodies, the formation of enzyme products, or the disappearance of enzyme substrates. For example, enzyme assays can be used to determine the activity of the variant.

[0623] Variants can be recovered using methods known in the art. For example, variants can be recovered from nutrient media using routine procedures, including but not limited to collection, centrifugation, filtration, extraction, spray drying, evaporation, or precipitation.

[0624] Variants can be purified to obtain substantially pure variants by a variety of procedures known in the art, including but not limited to chromatography (e.g., ion exchange chromatography, affinity chromatography, hydrophobic interaction chromatography, chromatographic focusing, and size exclusion chromatography), electrophoresis procedures (e.g., preparative isoelectric point focusing), differential solubility (e.g., ammonium sulfate precipitation), SDS-PAGE, or extraction (see, for example, Protein Purification, edited by Janson and Ryden, VCH Publishers, New York, 1989).

[0625] Alternatively, instead of recycling variants, the host cells of the present invention expressing variants are used as the source of the variants.

[0626] Fermentation broth preparations or cell compositions

[0627] The present invention also relates to fermentation broth formulations or cell compositions comprising variants of the invention. The fermentation broth product further comprises additional components used in the fermentation process, such as cells (including host cells containing genes encoding variants of the invention, these host cells being used to produce the desired variant), cell debris, biomass, fermentation medium, and / or fermentation product. In some embodiments, the composition is a cell-killing whole culture medium containing one or more organic acids, killed cells and / or cell debris, and a culture medium.

[0628] As used herein, the term "fermentation broth" refers to a preparation produced by cell fermentation that undergoes little or no recovery and / or purification. For example, fermentation broth is produced when a microbial culture is incubated to saturation under carbon-limited conditions that enable protein synthesis (e.g., expression of enzymes by the host cell) and secretion of proteins into the cell culture medium. Fermentation broth may contain unfractionated or fractionated contents of fermentation material derived at the end of fermentation. Typically, fermentation broth is unfractionated and contains used culture medium and cell debris remaining after, for example, removal of microbial cells (e.g., filamentous fungal cells) by centrifugation. In some embodiments, fermentation broth contains used cell culture medium, extracellular enzymes, and viable and / or non-viable microbial cells.

[0629] In the embodiments, the fermentation broth formulation and cell composition comprise a first organic acid component (an organic acid containing at least one to five carbons and / or its salt) and a second organic acid component (an organic acid containing at least six or more carbons and / or its salt). In specific embodiments, the first organic acid component is acetic acid, formic acid, propionic acid, its salt, or a mixture of two or more of the foregoing; and the second organic acid component is benzoic acid, cyclohexanecarboxylic acid, 4-methylvaleric acid, phenylacetic acid, its salt, or a mixture of two or more of the foregoing.

[0630] In one aspect, the composition contains one or more organic acids and optionally further contains killed cells and / or cell debris. In one embodiment, these killed cells and / or cell debris are removed from the cell-killing whole culture medium to provide a composition free of these components.

[0631] These fermentation broth formulations or cell compositions may further contain preservatives and / or antimicrobial (e.g., bacteriostatic) agents, including but not limited to sorbitol, sodium chloride, potassium sorbate, and other reagents known in the art.

[0632] The cell-killing whole culture or composition may contain ungraded contents of fermentation material derived at the end of fermentation. Typically, the cell-killing whole culture or composition contains used culture medium and cell debris present after microbial cells (e.g., filamentous fungal cells) have grown to saturation under carbon-limited conditions that allow for protein synthesis. In some embodiments, the cell-killing whole culture or composition contains used cell culture medium, extracellular enzymes, and killed filamentous fungal cells. In some embodiments, methods known in the art can be used to permeate and / or lyse the microbial cells present in the cell-killing whole culture or composition.

[0633] The whole culture medium or cell composition described herein is typically a liquid, but may contain insoluble components, such as killed cells, cell debris, culture medium components, and / or one or more insoluble enzymes. In some embodiments, insoluble components may be removed to provide a clear liquid composition.

[0634] The whole culture medium formulations and cell compositions of the present invention can be produced by the methods described in WO 90 / 15861 or WO 2010 / 096673.

[0635] Composition

[0636] In one embodiment, the present invention relates to cleaning compositions, such as detergent compositions, comprising a variant of the xyloglucanase of the present invention in combination with one or more additional cleaning composition components and, preferably, detergent adjuvant components as described herein. The selection of additional components is within the skill of a person skilled in the art and includes conventional ingredients, including exemplary non-limiting components set forth below. The detergent compositions can be used to clean items to be cleaned, such as textiles, tableware, and hard surfaces, to pre-treat stains on such items, to prevent, reduce, or remove redeposition of dirt during a washing cycle, and to maintain or improve the whiteness of the items.

[0637] Preferably, these compositions are enriched with such variants. The term "enriched" indicates that the xyloglucanase activity of the composition has increased, for example, by an enrichment factor of at least 1.1.

[0638] These compositions may contain variants of the invention as the main enzyme component, for example, a single-component composition. Alternatively, these compositions may contain a variety of enzyme activities, such as one or more enzymes selected from the group consisting of: hydrolases, isomerases, ligases, lyases, oxidoreductases, or transferases, for example, α-galactosidase, α-glucosidase, aminopeptidase, amylase, β-galactosidase, β-glucosidase, β-xylosidase, glycosylase, carboxypeptidase, catalase, cellobiase, cellulase, chitinase, keratinase, cyclodextrin glucosyltransferase, deoxyribonuclease, endoglucanase, esterase, glucosylamylase, invertase, laccase, lipase, mannosidase, polysaccharidase, nuclease, oxidase, pectinase, peroxidase, phytase, polyphenol oxidase, proteolytic enzyme, ribonuclease, transglutaminase, or xylanase.

[0639] The composition can be prepared according to methods known in the art, and the composition can be in the form of a liquid or a dry composition. The composition can be stabilized according to methods known in the art.

[0640] Examples of preferred uses of the compositions of the present invention are given below. The dosage of the composition and other conditions for using the composition can be determined based on methods known in the art.

[0641] For textile care, the selection of components may include considerations such as the type of textile to be cleaned, the type and / or extent of soiling, the temperature at which cleaning is performed, and the formulation of the detergent product. Although the components mentioned below are classified under a general heading according to specific functionality, this is not to be construed as limiting, as components may contain additional functionality as would be understood by a person skilled in the art.

[0642] In one embodiment of the invention, the composition (e.g., a detergent composition) comprises a xyloglucanase variant and a detergent adjuvant as disclosed herein.

[0643] In one embodiment of the invention, the detergent adjuvant component is selected from the group consisting of: surfactants, detergent builders, flocculants, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleaching activators, hydrogen peroxide, hydrogen peroxide sources, pre-formed peracids, polymerized dispersants, clay detergents / anti-redeposition agents, brighteners, defoamers, dyes, fragrances, structural elastic agents, fabric softeners, carriers, water-soluble auxiliaries, detergent builders and co-detergent builders, fabric colorants, defoamers, dispersants, processing aids, and / or pigments.

[0644] Detergent adjuvants can be surfactants. One advantage of including surfactants in detergent compositions containing xyloglucanase variants is improved washing performance. In one embodiment, the detergent adjuvant is a builder or a clay detergent / anti-redeposition agent.

[0645] In one embodiment, the detergent adjuvant ingredient is an enzyme. The detergent composition may contain one or more enzymes, as specified below. These one or more enzymes may be selected from the group consisting of: proteases, lipases, keratins, amylases, glycoses, cellulases, pectins, mannanases, arabinosylases, galactanases, xylanases, nucleases, and oxidases. Specific enzymes suitable for the detergent compositions of the present invention are described below.

[0646] The detergent composition can be formulated as strips, uniform tablets, and tablets having two or more layers, bags having one or more chambers, regular or compressed powders, granules, pastes, gels, or regular, compressed or concentrated liquids. The detergent composition can be a liquid detergent, a powder detergent, or a granular detergent.

[0647] The xyloglucanase of the present invention is suitable for use in cleaning, such as laundry. The present invention further relates to a method for washing articles, the method comprising the following steps:

[0648] a. Exposing articles to a detergent containing a variant polypeptide with xyloglucanase activity or a detergent composition containing such polypeptide;

[0649] b. Complete at least one washing cycle; and

[0650] c. Optional: Rinse the item.

[0651] The item in question is a textile.

[0652] The pH of the liquid solution is in the range of 1 to 11, such as in the range of 5.5 to 11, such as in the range of 7 to 9, such as in the range of 7 to 8, or in the range of 7 to 8.5.

[0653] The washing liquid may have a temperature in the range of 5°C to 95°C, or in the range of 10°C to 80°C, or in the range of 10°C to 70°C, or in the range of 10°C to 60°C, or in the range of 10°C to 50°C, or in the range of 15°C to 40°C, or in the range of 20°C to 30°C. In one embodiment, the temperature of the washing liquid is 30°C.

[0654] In one embodiment of the invention, the method for washing articles further includes draining the washing solution or a portion thereof after a washing cycle is completed. The washing solution can then be reused in subsequent washing cycles or subsequent rinsing cycles. During the first and optionally the second or third washing cycle, the article may be exposed to the washing solution. In one embodiment, after exposure to the washing solution, the article is rinsed. The article may be rinsed with water or with water including a conditioning agent. The invention further relates to articles washed according to the method of the invention. A variant of the xyloglucanase of the invention may be added to the washing solution.

[0655] Therefore, one embodiment of the present invention relates to a detergent composition comprising one or more anionic surfactants; an enzyme selected from the group consisting of proteases, lipases, keratases, amylases, glycoses, cellulases, pectins, mannanases, arabinases, galactanases, xylanases, nucleases, and oxidases; and the xyloglucanase variant of the present invention.

[0656] One embodiment further relates to a washing method for textiles, the method comprising:

[0657] a. Exposing textiles to a detergent solution containing a xyloglucanase variant or a detergent composition containing at least one of these xyloglucanase variants.

[0658] b. Complete at least one washing cycle; and

[0659] c. Optionally rinse the textile.

[0660] The xyloglucanase variant contains alterations at one or more positions corresponding to the group selected from the following: 111, 123, 159, 256, 294, 8, 18, 20, 41, 42, 76, 82, 83, 87, 94, 103, 104, 105, 121, 125, 126, 127, 136, 137, 146, 147, 148, 152, 153, 155, 165, 168, 169, 177, 184, 189, 203, 206, 210, 211, 214, 217, 219, 220, 226, 2 37, 238, 240, 243, 244, 248, 251, 252, 267, 271, 276, 289, 295, 298, 300, 302, 322, 329, 339, 347, 347, 353, 383, 384, 392, 394, 395, 402, 414, 427, 431, 445, 447, 459, 473, 474, 476, 482, 488, 489, 491, 492, 503, and 505.

[0661] Another embodiment relates to textiles washed according to the method of the present invention.

[0662] The concentration of xyloglucanase variants in the washing solution is typically in the range of 0.00004-100 ppm enzyme protein, such as in the range of 0.00008-100, 0.0001-100, 0.0002-100, 0.0004-100, 0.0008-100, 0.001-100 ppm enzyme protein, 0.01-100 ppm enzyme protein, preferably 0.05-50 ppm enzyme protein, more preferably 0.1-50 ppm enzyme protein, more preferably 0.1-30 ppm enzyme protein, more preferably 0.5-20 ppm enzyme protein, and most preferably 0.5-10 ppm enzyme protein.

[0663] The xyloglucanase variant of the present invention can be added to the detergent composition in an amount corresponding to at least 0.002 mg of xyloglucanase protein, such as at least 0.004 mg of xyloglucanase protein, at least 0.006 mg of xyloglucanase protein, at least 0.008 mg of xyloglucanase protein, at least 0.01 mg of xyloglucanase protein, at least 0.1 mg of protein, preferably at least 1 mg of protein, more preferably at least 10 mg of protein, even more preferably at least 15 mg of protein, most preferably at least 20 mg of protein, and even most preferably at least 25 mg of protein. Therefore, the detergent composition may contain at least 0.00008% xyloglucanase protein, preferably at least 0.002%, 0.003%, 0.004%, 0.005%, 0.006%, 0.008%, 0.01%, 0.02%, 0.03%, 0.05%, 0.1%, 0.2%, 0.3%, 0.4%, 0.6%, 0.7%, 0.8%, 0.9%, or 1.0% xyloglucanase protein.

[0664] The enzymes present in the detergents of the present invention can be stabilized using conventional stabilizers, such as polyols like propylene glycol or glycerol, sugars or sugar alcohols, and various salts like NaCl and KCl. The protease present in the detergents of the present invention may be stabilized using: lactic acid, formic acid, boric acid, or boric acid derivatives (e.g., aromatic borate esters), or phenyl boric acid derivatives (e.g., 4-formylphenylboronic acid), or peptide aldehydes (e.g., dipeptide aldehydes, tripeptide aldehydes, or tetrapeptide aldehydes or aldehyde analogs) (or having the form B1-B0-R, wherein R is H, CH3, CX3, CHX2, or CH2X (X = halogen), B0 is a single amino acid residue (preferably having optionally substituted aliphatic or aromatic side chains); and B1 consists of one or more amino acid residues (preferably one, two, or three), optionally containing an N-terminal protecting group, or as described in WO 09118375, WO 98 / 13459) or protein-type protease inhibitors, such as RASI, BASI, WASI (bifunctional α-amylase / subtilis protease inhibitors for rice, barley, and wheat), or CI2 or SSI. The composition can be formulated as described, for example, in WO 92 / 19709, WO 92 / 19708 and US 6,472,364. In some embodiments, the enzymes used herein are stabilized by a water-soluble source of zinc (II), calcium (II) and / or magnesium (II) ions present in the finished composition providing such ions for the enzymes, along with other metal ions (e.g., barium (II), scandium (II), iron (II), manganese (II), aluminum (III), tin (II), cobalt (II), copper (II), nickel (II), and vanadium oxide (IV)).

[0665] In one embodiment, a peptide aldehyde or ketone is used to stabilize the polypeptide. Suitable peptide aldehydes are described in WO 94 / 04651, WO 95 / 25791, WO 98 / 13458, WO 98 / 13459, WO 98 / 13460, WO 98 / 13461, WO 98 / 13462, WO07 / 141736, WO 07 / 145963, WO 09 / 118375, WO 10 / 055052, and WO 11 / 036153. The polypeptides of the present invention can also be incorporated into detergent formulations disclosed in WO 97 / 07202, which is hereby incorporated by reference.

[0666] In another embodiment, a phenylboronic acid derivative is used to stabilize the polypeptide, the phenylboronic acid derivative being 4-formylphenylboronic acid (4-FPBA) having the following formula:

[0667]

[0668] Detergent compositions may contain two or more stabilizers, such as those selected from the group consisting of propylene glycol, glycerin, 4-formylphenylboronic acid, and borate.

[0669] Detergent compositions may contain two or more stabilizers, such as those selected from the group consisting of propylene glycol, glycerin, 4-formylphenylboronic acid, and borate.

[0670] The amount of one or more stabilizers present in the detergent composition is preferably from 0.001 to about 5.0 wt%, from 0.01 to about 2.0 wt%, from 0.1 to about 3 wt%, or from 0.5% to about 1.5 wt%.

[0671] surfactants

[0672] Detergent compositions may contain one or more surfactants, which may be anionic and / or cationic and / or nonionic and / or semi-polar and / or zwitterionic, or mixtures thereof. In certain embodiments, the detergent composition comprises a mixture of one or more nonionic surfactants and one or more anionic surfactants. The one or more surfactants are typically present at levels from about 5% to 60% by weight (e.g., about 5% to about 50%, or about 10% to about 50%, or about 20% to about 50%). The one or more surfactants are selected based on the desired cleaning application, and the one or more surfactants may include any one or more conventional surfactants known in the art.

[0673] When included, detergents will typically contain one or more anionic surfactants by weight, ranging from about 5% to about 60% (e.g., from about 5% to about 40%, including from about 10% to about 25%). Non-limiting examples of anionic surfactants include sulfates and sulfonates, particularly linear alkylbenzene sulfonates (LAS), isomers of LAS, branched alkylbenzene sulfonates (BABS), phenyl alkyl sulfonates, α-olefin sulfonates (AOS), olefin sulfonates, chain olefin sulfonates, alkyl-2,3-dimethylbis(sulfate), hydroxyalkyl sulfonates and disulfonates, alkyl sulfates (AS) (such as sodium dodecyl sulfate (SDS)), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), and alcohol ethers. Sulfates (AES or AEOS or FES, also known as alcohol ethoxy sulfates or fatty alcohol ether sulfates), secondary alkyl sulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerides, α-sulfo fatty acid methyl esters (α-SFMe or SES) (including methyl ester sulfonates (MES)), alkyl succinic acids or alkenyl succinic acids, dodecenyl / tetradecenyl succinic acids (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfosuccinic acids or fatty acid salts (soaps) or fatty acids, and combinations thereof.

[0674] When included therein, the detergent will typically contain from about 0.1% to about 10% by weight (e.g., from about 0.1% to about 5%) of a cationic surfactant. Non-limiting examples of cationic surfactants include alkyl dimethyl ethanol quaternary ammonium (ADMEAQ), hexadecyl trimethyl ammonium bromide (CTAB), dimethyl distearate ammonium chloride (DSDMAC), and alkyl benzyl dimethyl ammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quaternary ammonium, and combinations thereof.

[0675] When included, detergents will typically contain from about 0.2% to about 60% by weight (e.g. from about 1% to about 40%, particularly from about 5% to about 20%, from about 3% to about 15%) of nonionic surfactants. Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters (e.g., ethoxylated and / or propoxylated fatty acid alkyl esters), alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkyl polysaccharides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucosamide (GA) or fatty acid glucosamide (FAGA)), methyl ester ethoxylates (MEE), together with products available under the trade names SPAN and TWEEN, and combinations thereof.

[0676] When included therein, the detergent will typically contain from about 0.1% to about 10% by weight of a semi-polar surfactant. Non-limiting examples of semi-polar surfactants include amine oxides (AOs), such as alkyl dimethylamine oxides, N-(cocoylalkyl)-N,N-dimethylamine oxides, and N-(butter-alkyl)-N,N-bis(2-hydroxyethyl)amine oxides, and combinations thereof.

[0677] When included, detergents will typically contain from about 0.1% to about 10% by weight of a facultative zwitterionic surfactant. Non-limiting examples of facultative zwitterionic surfactants include betaines, such as alkyl dimethyl betaine, sulfobetaine, and combinations thereof.

[0678] Solvent System: A solvent system is required to dissolve surfactants and other detergent components. Solvents are typically water, alcohols, polyols, sugars, and / or mixtures thereof. Preferred solvents are water, glycerol, sorbitol, propylene glycol (MPG, 1,2-propanediol, or 1,3-propanediol), dipropylene glycol (DPG), polyethylene glycol family (PEG300-600), hexanediol, inositol, mannitol, ethanol, isopropanol, n-butoxypropoxypropanol, ethanolamines (monoethanolamine, diethanolamine, and triethanolamine), sucrose, dextrose, glucose, ribose, xylose, and related mono- and dipyranoside and furanoside.

[0679] The solvent system typically exists in total amounts of 5%-90%, 5%-60%, 5%-40%, and 10%-30% by weight.

[0680] The water content per unit dose encapsulated in PVA film typically ranges from 1% to 15%, 2% to 12%, 3% to 10%, and 5% to 10%.

[0681] The polyol content per unit dose encapsulated in PVA film is typically in the range of 5%-50%, 10%-40%, or 20%-30%.

[0682] In the embodiments, the surfactant is a non-naturally occurring surfactant.

[0683] Water-soluble additives

[0684] Water-soluble additives are compounds that dissolve hydrophobic compounds in aqueous solutions (or conversely, polar substances in nonpolar environments). Typically, water-soluble additives possess both hydrophilic and hydrophobic characteristics (as known from surfactants as so-called amphiphilic properties); however, the molecular structure of water-soluble additives generally does not favor spontaneous self-aggregation, see, for example, the review by Hodgdon and Kaler (2007), Current Opinion in Colloid & Interface Science 12: 121-128. Water-soluble additives do not exhibit the critical concentrations (above which self-aggregation occurs) seen in surfactants and lipids that form micelles, thin layers, or other well-defined meso-phases. Instead, many water-soluble additives exhibit a continuous type of aggregation process in which the size of the aggregates increases with increasing concentration. However, many water-soluble additives alter the phase behavior, stability, and colloidal properties of systems containing substances with both polar and nonpolar characteristics, including mixtures of water, oils, surfactants, and polymers. Water-soluble adjuvants are routinely used in a variety of industries, from pharmaceuticals and personal care to food and technical applications. The use of water-soluble adjuvants in detergent compositions allows for, for example, more concentrated surfactant formulations (such as in the process of compressing liquid detergents by removing water) without causing undesirable phenomena such as phase separation or high viscosity.

[0685] Detergents may contain 0-10% by weight, for example 0-5% by weight, such as about 0.5% to about 5%, or about 3% to about 5% of water-soluble additives. Any water-soluble additive known in the art for use in detergents may be used. Non-limiting examples of water-soluble additives include sodium benzenesulfonate, sodium p-toluenesulfonate (STS), sodium xylenesulfonate (SXS), sodium cumenesulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyethylene glycol ethers, sodium hydroxynaphthoate, sodium hydroxynaphthoate, sodium ethylhexyl sulfonate, sodium ethylhexyl sulfonate, and combinations thereof.

[0686] Builders and co-builders

[0687] Detergent compositions may contain about 0-65%, 0-20%, or 0.5%-5% of detergent builders or co-builders, or mixtures thereof. In dishwashing detergents, the level of builders is typically 10%-65%, particularly 20%-40%. Builders and / or co-builders may be chelating agents, particularly those that form water-soluble complexes with Ca and Mg. Any builders and / or co-builders known in the art for use in laundry detergents may be used. Non-limiting examples are citrates, sodium carbonate, sodium bicarbonate, and sodium citrate. Examples of phosphonates include 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP, etidronic acid), diethylenetriaminepenta (DTPMP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), aminotri(methylenephosphonic acid) (ATMP), nitrotrimethylenephosphonic acid (NTMP), 2-aminoethylphosphonic acid (AEPn), dimethylmethylphosphonate (DMPP), tetramethylenediaminetetra(methylenephosphonic acid) (TDTMP), hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP), phosphonate butane-tricarboxylic acid (PBTC), N-(phosphonomethyl)iminodiacetic acid (PMIDA), 2-carboxyethylphosphonic acid (CEPA), 2-hydroxyphosphonocarboxylic acid (HPAA), and amino-tri-(methylene-phosphonic acid) (AMP). Other examples include tetrasodium L-glutamic acid N,N-diacetic acid (GLDA) and methylglycine diacetic acid (MGDA). Non-limiting examples of detergent builders include homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copolymers (acrylic acid / maleic acid) (PAA / PMA). Other non-limiting examples include citrates, chelating agents (e.g., aminocarboxylates, aminopolycarboxylates, and phosphonates), and alkyl succinic acids or alkenyl succinic acids.Other specific examples include 2,2',2”-nitrotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N'-disuccinic acid (EDDS), methylglycine diacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diphosphonic acid (HEDP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), diethylenetriaminepenta(methylenephosphonic acid) (DTMPA or DTPMPA), N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic-N-monoacetic acid (ASMA), aspartic-N,N-diacetic acid (ASDA), aspartic-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)-aspartic acid (SMAS), N-(2-sulfoethyl)-aspartic acid (SEAS), N- (2-Sulfomethyl)-glutamic acid (SMGL), N-(2-sulfoethyl)-glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), α-alanine-N,N-diacetic acid (α-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N-diacetic acid (SLDA), taurine-N,N-diacetic acid (TUDA), and sulfomethyl-N,N-diacetic acid (SMDA), N-(2-hydroxyethyl)-ethylenediamine-N,N',N''-triacetic acid (HEDTA), diethanolamine glycine (DEG), diethylenetriaminepenta (methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations thereof and salts thereof. Further exemplary builders and / or co-builders are described in, for example, WO 09 / 102854, US 5977053.

[0688] In the embodiments, the builder or co-builder is a non-naturally occurring builder or co-builder.

[0689] bleaching system

[0690] The detergent may contain 0-30% by weight, for example, about 1% to about 20%, of a bleaching system. Any bleaching system known in the art for use in laundry detergents may be used. Suitable bleaching system components include bleaching catalysts, photobleaching agents, bleaching activators, hydrogen peroxide sources such as sodium percarbonate, sodium perborate, and hydrogen peroxide-urea (1:1), preformed peracids, and mixtures thereof. Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids and their salts, disperoxydicarboxylic acids, perimidic acids and their salts, peroxymonosulfate and their salts (e.g., potassium persulfate (Oxone(R))), and mixtures thereof. Non-limiting examples of bleaching systems include peroxide-based bleaching systems that combine with peracids to form bleaching activators, which may contain, for example, inorganic salts, including sodium salts of alkali metal salts such as perborates (typically monohydrates or tetrahydrates), percarbonates, persulfates, superphosphates, and persilicates. The term bleaching activator herein refers to a compound that reacts with hydrogen peroxide to form a peracid via perhydrolysis. The resulting peracid constitutes the activated bleaching agent. Suitable bleaching activators for use herein include those belonging to the classes of esters, amides, imides, or anhydrides. Suitable examples are tetraacetylethylenediamine (TAED), sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1-sulfonate (ISONOBS), 4-(dodecanoyloxy)benzene-1-sulfonate (LOBS), 4-(decanoyloxy)benzene-1-sulfonate, 4-(decanoyloxy)benzoate (DOBS or DOBA), 4-(nonanoyloxy)benzene-1-sulfonate (NOBS), and / or those disclosed in WO 98 / 17767. Specific families of desired bleaching activators are disclosed in EP 624154, and a particularly preferred family is triethyl acetylacetate (ATC). ATC or short-chain triglycerides (like triacetin) have the advantage of being environmentally friendly. Furthermore, triethyl acetyl citrate and triacetin exhibit good hydrolytic stability in the product during storage and are highly effective bleaching activators. Finally, ATC is versatile because the citrate released during the hydrolysis reaction can act as a washing aid. Alternatively, the bleaching system may contain peroxy acids of the type such as amides, imides, or sulfones. The bleaching system may also contain peracids such as 6-(phthalimide)peroxyhexanoic acid (PAP). The bleaching system may also include a bleaching catalyst. In some embodiments, the bleaching component may be an organic catalyst selected from the group consisting of organic catalysts having the following formula:

[0691]

[0692] (iii) and its mixtures,

[0693] Each R 1Independently, it is a branched alkyl group containing 9 to 24 carbons or a straight-chain alkyl group containing 11 to 24 carbons, preferably each R 1 Independently, it is a branched alkyl group containing 9 to 18 carbons or a straight-chain alkyl group containing 11 to 18 carbons, more preferably each R 1 Independently selected from the group consisting of: 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isothidecyl, isothidecyl, and isopentachidyl. Other exemplary bleaching systems are described, for example, in WO 2007 / 087258, WO 2007 / 087244, WO 2007 / 087259, EP 1867708 (Vitamin K) and WO 2007 / 087242. Suitable photobleaching agents may be, for example, sulfonated zinc phthalocyanine or aluminum phthalocyanine.

[0694] Preferably, in addition to the bleaching catalyst, particularly an organic bleaching catalyst, the bleaching component also contains a peracid source. The peracid source may be selected from (a) pre-formed peracid; (b) percarbonate, perborate, or persulfate (hydrogen peroxide source), preferably in combination with a bleaching activator; and (c) perhydrolase and esters, used to form the peracid in situ in the presence of water during textile or hard surface treatment steps.

[0695] In this embodiment, the bleaching system is a non-naturally occurring bleaching system.

[0696] polymer

[0697] The detergent may contain 0-10% (e.g., 0.5%-5%, 2%-5%, 0.5%-2%, or 0.2%-1%) of a polymer by weight. Any polymer known in the art for use in detergents may be used. The polymer may function as a co-adjuvant as mentioned above, or may provide anti-redeposition, fiber protection, dirt release, dye transfer inhibition, grease removal, and / or defoaming properties. Some polymers may have more than one of the properties mentioned above and / or more than one of the motifs mentioned below. Exemplary polymers include (carboxymethyl) cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethylene glycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylate esters (such as PAA, PAA / PMA, poly-aspartic acid, and lauryl methacrylate / acrylic acid copolymers), hydrophobically modified CMC (HM-CMC) and silicone, copolymers of terephthalic acid and oligomeric polyethylene glycol, copolymers of poly(ethylene terephthalate) and poly(ethylene oxide terephthalate) (PET-POET), PVP, poly(vinylimidazolium) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO), and polyvinylpyrrolidone-vinylimidazolium (PVPVI). Other exemplary polymers include sulfonated polycarboxylate esters, polyethylene oxide and polypropylene oxide (PEO-PPO), and diquaternary ammonium ethoxysulfate. Other exemplary polymers are disclosed, for example, in WO 2006 / 130575. Salts of the polymers mentioned above are also considered.

[0698] In the embodiments, the polymer is a non-naturally occurring polymer.

[0699] Fabric colorant

[0700] The detergent compositions of the present invention may further include fabric colorants, such as dyes or pigments, which, when formulated in the detergent composition, can deposit on the fabric when the fabric comes into contact with a washing liquid containing the detergent composition, and thus alter the color of the fabric by absorption / reflection of visible light. Fluorescent whitening agents emit at least some visible light. Conversely, fabric colorants alter the color of the surface when they absorb at least a portion of the visible spectrum. Suitable fabric colorants include dyes and dye-clay conjugates, and may also include pigments. Suitable dyes include small molecule dyes and polymer dyes. Suitable small molecule dyes include those selected from the group consisting of dyes falling into the Colour Index (CI) classification: Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet, and Basic Red, or mixtures thereof, such as those described in WO 2005 / 03274, WO 2005 / 03275, WO 2005 / 03276 and EP1876226 (which are hereby incorporated by reference). The detergent composition preferably contains 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% of a fabric toner. The composition may contain from 0.0001 wt% to 0.2 wt% of a fabric toner, which may be particularly preferred when the composition is in the form of unit dose packets. Suitable toners are also disclosed, for example, in WO 2007 / 087257 and WO2007 / 087243.

[0701] Other enzymes

[0702] The detergent additive, together with the detergent composition, may contain one or more [additional] enzymes, such as hydrolases (EC 3.-.-.-), such as ester-linked hydrolases (EC 3.1.-.-), glycosidases (EC 3.2.-.-), and peptide-linked hydrolases (EC 3.4.-.-), oxidoreductases (EC 1.-.-.-), such as laccase (EC 1.10.-.-) or peroxidases (EC 1.11.-.-), or lyases (EC 4.-.-.-), such as carbon-oxygen lyases (EC 4.2.-.-). In certain embodiments, the detergent composition may contain one or more [additional] enzymes, such as proteases, lipases, keratins, amylases, glycoses, cellulases, pectins, mannanases, arabinases, galactanases, xylanases, nucleases, oxidases (e.g., laccase), and / or peroxidases.

[0703] Generally, the properties of one or more enzymes selected should be compatible with the selected detergent (i.e., optimal pH, compatibility with other enzyme or non-enzyme components, etc.), and the one or more enzymes should be present in an effective amount.

[0704] Cellulase

[0705] Suitable cellulases include those of bacterial or fungal origin. This includes chemically modified mutants or protein-engineered mutants. Suitable cellulases include those from the genera *Bacillus*, *Pseudomonas*, *Pyrophyllus*, *Fusarium*, *Clostridium*, and *Cladosporium*, such as the fungal cellulases produced by *Pyrophyllus*, *Thermophyllus*, and *Fusarium* as disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757, and WO 89 / 09259.

[0706] Particularly suitable cellulases are alkaline or neutral cellulases, which provide or maintain whiteness and prevent redeposition or have color-care benefits. Examples of such cellulases are those described in EP 0 495 257, EP0 531 372, WO 96 / 11262, WO 96 / 29397, and WO 98 / 08940. Other examples are, for instance, those cellulases described in WO 94 / 07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95 / 24471, WO 98 / 12307, and WO 99 / 001544.

[0707] Other cellulases are endoglucanases having the following sequence, which has at least 97% identity with the amino acid sequence at positions 1 to 773 of SEQ ID NO: 2 of WO 2002 / 099091, or family 44 xyloglucanases having the following sequence, which has at least 60% identity with positions 40-559 of SEQ ID NO: 2 of WO 2001 / 062903.

[0708] Commercially available cellulases include Celluzyme™ and Carezyme™ (Novozymes A / S), Carezyme Premium™ (Novozymes), Cellluclean™ (Novozymes), CelllucleanClassic™ (Novozymes), Cellusoft™ (Novozymes), Whitezyme™ (Novozymes), Clazinase™ and Puradax HA™ (Genencor International Inc.), and KAC-500(B)™ (Kao Corporation).

[0709] Mannanase

[0710] Suitable mannanases include those of bacterial or fungal origin. This includes chemically or genetically modified mutants. Mannanases can be basic mannanases of families 5 or 26. They can be wild-type from the genera *Bacillus* or *Pythium*, particularly from *Bacillus mucosa*, *Bacillus licheniformis*, *Bacillus halodurans*, *Bacillus cladosporium*, or specific *Pythium* species. Suitable mannanases are described in WO 1999 / 064619. Commercially available mannanases are from Mannaway (Novozymes).

[0711] protease

[0712] Suitable proteases include those of bacterial, fungal, plant, viral, or animal origin, such as those of plant or microbial origin. Microbial origin is preferred. This includes chemically modified mutants or protein-engineered mutants. It can be an alkaline protease, such as a serine protease or a metalloproteinase. Serine proteases can be, for example, serine proteases of the S1 family (such as trypsin) or the S8 family (such as subtilisin). Metalloproteinases can be, for example, thermophilic bacterial proteases from the M4 family or other metalloproteinases, such as those from the M5, M7, or M8 families.

[0713] The term "subtilisinase" refers to the serine protease subgroup according to Siezen et al., Protein Eng. 4 (1991) 719-737 and Siezen et al., Protein Science 6 (1997) 501-523. Serine proteases are a subgroup of proteases characterized by the presence of a serine residue at its active site that forms a covalent adduct with the substrate. Subtilisins can be classified into six subclasses: the subtilisin family, the thermophilic protease family, the proteinase K family, the lanathionine antibiotic peptidase family, the Kexin family, and the Pyrolysin family.

[0714] Examples of subtilisinases are those derived from the genus Bacillus, such as *Bacillus tarda*, *Bacillus alkalophilus*, *Bacillus subtilis*, *Bacillus amyloliquefaciens*, *Bacillus pumilus*, and *Bacillus gibsonii* as described in US 7262042 and WO 09 / 021867; and *Bacillus tarda* protease, *Bacillus subtilis protease Novo*, *Bacillus subtilis protease Carlsberg*, *Bacillus licheniformis*, *Bacillus subtilis protease BPN'*, *Bacillus subtilis protease 309*, *Bacillus subtilis protease 147*, and *Bacillus subtilis protease 168* as described in WO 89 / 06279, and protease PD138 as described in (WO 93 / 18140). Other useful proteases may be those described in WO 92 / 175177, WO 01 / 016285, WO 02 / 026024, and WO 02 / 016547. Examples of trypsin-like proteases are trypsin (e.g., those of porcine or bovine origin) and Fusarium proteases (described in WO 89 / 06270, WO 94 / 25583 and WO 05 / 040372), as well as chymotrypsin derived from Cellumonas (described in WO 05 / 052161 and WO 05 / 052146).

[0715] Other preferred proteases are alkaline proteases from Bacillus tarda DSM 5483 (as described in, for example, WO 95 / 23221) and their variants (described in WO 92 / 21760, WO 95 / 23221, EP 1921147 and EP 1921148).

[0716] Examples of metalloproteinases are neutral metalloproteinases as described in WO 07 / 044993 (Genetronics International Ltd.), such as those derived from Bacillus amylolyticus.

[0717] Examples of useful proteases are the variants described in the following: WO 92 / 19729, WO 96 / 034946, WO98 / 20115, WO 98 / 20116, WO 99 / 011768, WO 01 / 44452, WO 03 / 006602, WO 04 / 03186, WO 04 / 041979, W...

Claims

1. A xyloglucanase variant, wherein the variant comprises one or more of the following changes at a position corresponding to the following location: SEQ ID NO: The polypeptide of 1 contains P111, S123, V159, S256, I294, K8, K18, R20, A41, A42, S76, Q82, A83, K87, S94, G103, T104, Y105, A118, N121, Q125, E126, S127, N136, Q137, F146, Q147, L148, L152, N153, N155, F165, N168, K169, A177, L184, A189, V203, K206, D210, R211, S214, K217, V219, K220, A226, G237, A238, K240, Q 243, T244, W248, V251, K252, R267, Q271, R276, A289, R295, N298, V300, N302, K322, Q329, P339, K347, R347, K353, R353, N383, D384, K392, K394, D395, P395, S402, K414, T427, V431, K445, L447, A459, I473, S474, K476, K482, K488, E489, A491, P492, Y503, and V505, wherein the variant possesses xyloglucanase activity, and wherein the variant is related to SEQ The polypeptides of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3 have at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity but less than 100% sequence identity.

2. The variant of claim 1, wherein the variant comprises one or more of the following changes at positions corresponding to the following locations: P111Q, S123P, V159M, S256E, S256Q, I294E, I294Q, K8E, K8R, K18E, R20K, A41L, A41E, A41R, A42V, S76E, Q82E, A83E, K87E, S94R, G103V, T104G, T104 of the polypeptide of SEQ ID NO:

1. R, Y105E, A118K, N121E, Q125F, Q125K, Q125L, Q125P, Q125S, E126P, S127H, S 127L, S127W, S127D, N136D, Q137E, Q137K, F146D, Q147G, Q147K, L148P, L152 , L152D, L152E, L152P, N153E, N155D, N155E, F165H, N168R, K169E, K169R, A 177G, L184M, A189G, V203T, K206E, K206R, D210H, D210R, R211K, S214Q, K217 R, K217T, V219A, V219T, K220R, A226D, A226K, G237M, A238S, A238T, K240F, K 240L, Q243E, T244E, T244R, W248V, V251E, K252E, R267C, R267H, R267K, Q271 D. Q271E, R276K, A289T, R295K, N298D, V300L, N302H, K322E, Q329E, P339S, K347E, K347R, K353R, N383E, N383Q, D384G, K392E, K394R, D395P, S402Q, K41 4E, T427V, V431E, K445E, L447M, A459P, I473T, S474E, K476R, K482R, K488T, E489K, E489R, A491E, A491V, P492D, Y503L, Y503V, and V505L, among which this variant has xyloglucanase activity.

3. The variant as claimed in claim 1 or 2, wherein the variant comprises changes or combinations of changes selected from the group consisting of: K394R of the polypeptide of SEQ ID NO: 1 S127D, R211K, S123P, K488T, S256Q, K476R, K217R, Q271D, S214Q, L447M, K482R, K169R, L152D, R267K, L152E, D210R, L152 、 R295K, S127W, E126P, S127H, T104G, Q125K, Q125P, Q125S, D395P, G103V, T104R, Q125L, A41E, A41R, Q125F, S127L, A226K, A41L, A226D, A118K+S123P, N155D, Q137K, N155E, Q147K, R276K, V203T, S94R, K18E, K252E, V219T, R267C+T427V, Q243E, K414E、 K445E、 R20K+S123P、 S123P+K206R、 R20K+S123P+R211K、 S123P+K347R、 S123P+K347R+K353R+D395P、 S123P+D395P、 S123P+S127D、 V159M、 K392E、 E489R+P492D、 Y503L+V505L、 Y503V+V505L、 L184M+V219A、 S123P+R211K+K217R+S256Q+K488T、 Q82E、 S76E、 A83E、 Q271E、 S256E、 I294E、 Q329E、 V431E、 R20K+Y105E+S123P+Q147K+R267K、 R20K+Y105E+S123P+R267K、 R20K+S123P+K220R、 R20K+Y105E+S123P+N136D、 R20K+S123P+Q137K+Q147K、 Y105E+A118K+S123P+K206R+K220R+R267K、 P111Q+S123P+V159M、 S94R+P111Q+S123P+V159M、 K87E+P111Q+S123P+V159M+S402Q、 K87E+P111Q+S123P+V159M、 P111Q+S123P+V159M+S402Q、 K87E+P111Q+V159M+I294Q+I473T、 K8E+P111Q+V159M、 K8E+K18E+P111Q+V159M+K206E、 R20K+P111Q+S123P+S127D+V159M、 P111Q+Q147K+V159M+K220R、 S94R+P111Q+V159M、 P111Q+V159M+K206E+I294Q、 P111Q+V159M+K206E+I294Q+K347E、 P111Q+Q137K+Q147K+V159M+K252E、 P111Q+Q137K+Q147K+N155D+K252E、 P111Q+Q137K+L152D+V203T+K217R、 P111Q+Q137K+V159M、 K8E+P111Q+N155D+V159M、 A41L+P111Q+S123P+Q147K+V159M+V203T、 A41L+P111Q+S123P+Q147K+V159M+K217R、 P111Q+S123P+Q137K+Q147K+V159M+S256Q+S402Q、 P111Q+S123P+Q147K+V159M+I294Q+S402Q、 A41L+P111Q+Q137K+V159M+N168R+Q271D+K488T、 P111Q+Q137K+Q147K+V159M+V203T+K217R、 P111Q+Q147K+V159M、 P111Q+Q137K+Q147K+V159M、 P111Q+S123P+Q137K+V159M+K488T、 P111Q+S123P+Q137K+V159M+S256Q、 K87E+P111Q+L152D+V159M+V203T+I294Q、 K87E+P111Q+Q147K+L152D+V159M、 R20K+A83E+S123P+K220R+S256E、 R20K+S76E+A83E+S123P+K220R+K252E、 R20K+A83E+S123P+K220R+K252E、 R20K+A42V+S123P+K220R+K252E+I294E、 R20K+Q82E+S123P+Q147K+K220R、 R20K+A83E+S123P+K220R+S256Q、 R20K+Q82E+S123P+N155D+K220R、 R20K+S123P+V203T+K220R+K252E、 R20K+S123P+K220R+I294E、 R20K+A83E+S123P+V203T+K220R+K252E、 R20K+A41L+Q82E+S123P+K220R、 R20K+S123P+N155D+K220R、 R20K+A42V+S76E+S123P+K220R、 R20K+S123P+V203T+V219T、 R20K+A42V+A83E+S123P+K220R、 R20K+A42V+S76E+S123P+V203T+K220R、 A83E+P111Q+S123P+V159M+S256E+I294E、 Q82E+P111Q+S123P+V159M+S256E+I294E、 Q82E+P111Q+S123P+Q147K+V159M+I294E、 S76E+Q82E+K87E+P111Q+S123P+V159M+V203T、 A83E+P111Q+S123P+Q137K+Q147K+V159M+S256Q+S402Q、 P111Q+S123P+Q137K+Q147K+N155D+S256Q+A289T+N302H、 S76E+P111Q+S123P+Q137E+Q147K+V159M+K252E+S256Q+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+K252E+S256Q+S402Q、 P111Q+S123P+Q137K+Q147K+N155D+S256Q+I294E+S402Q、 Q82E+P111Q+S123P+Q137K+Q147K+V159M+L184M+A238S+S256Q+I294E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256Q+I294E+S402Q、 P111Q+N121E+Q137K+Q147K+V159M+K169R+S256Q+I294E+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+K169R+S256Q+I294E+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+L184M+V219T+S256Q+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256Q+S402Q、 Q82E+P111Q+S123P+Q137K+Q147K+V159M+K252E+S256Q+S402Q、 S76E+P111Q+S123P+Q137K+Q147K+V159M+S256Q+S402Q、 K8R+P111Q+S123P+Q137K+Q147K+V159M+S256Q+S402Q、 S123P+S127D+N136D+Q137K+Q147K+L152E+N153E+N155E、 S123P+S127D+N136D+Q137K+Q147K+L152E+N153E+N155E+A491E、 R20K+S123P+K169R+K217T+K240F+S256Q+R267H+I294E、 K87E+P111Q+S123P+V159M+K217T+I294E、 A83E+P111Q+S123P+V159M+K240F+K252E、 A83E+P111Q+S123P+V159M+K252E、 K87E+P111Q+S123P+V159M+S256Q+I294E、 K87E+P111Q+S123P+V159M+K347E+N383E、 Q82E+P111Q+S123P+V159M+V203T+G237M+S256E+I294E、 Q82E+P111Q+S123P+N155D+S256E+I294E、 Q82E+P111Q+S123P+N155D+K169R+G237M+S256E+I294E、 Q82E+P111Q+S123P+Q147K+V159M+S256E+I294E、 Q82E+P111Q+S123P+Q137K+V159M+G237M+S256E+I294E、 Q82E+P111Q+S123P+Q137K+V159M+K240F+S256E+I294E、 Q82E+P111Q+S123P+Q147K+N155D+K240F+S256E+I294E、 K8E+Q82E+P111Q+S123P+V159M+S256E+I294E、 A83E+P111Q+S123P+Q147K+V159M+S256E+I294E+Q329E、 Q82E+P111Q+S123P+V159M+K240F+S256EI294E、 Q82E+P111Q+S123P+V159M+A177G+K240F+S256E+I294E+D384G、 K8R+Q82E+P111Q+S123P+V159M+K169R+K240F+S256E+I294E、 Q82E+P111Q+S123P+V159M+K169R+S256E+I294E+V431E、 Q82E+P111Q+S123P+V159M+G237M+V251E+I294E、 A41L+Q82E+P111Q+S123P+V159M+S256E+I294E+N383E、 A83E+P111Q+S123P+Q137K+F146D+Q147G+L148P+V159M+L184M+S256Q+I294E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256Q+I294E+N298D+V300L+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+K169R+L184M+K240L+S256Q+I294E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+S256Q+I294E+S402Q+K488T、 A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+S256Q+I294E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+K240F+S256Q+I294E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+S256E+I294E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K240F+S256Q+I294E+S402Q+E489R、 A83E+P111Q+S123P+Q137K+Q147K+V159M+F165H+L184M+S256Q+I294E+S402Q+V431E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+S256Q+I294E+S402Q、 R20K+S123P+Q147K+N155D+K169R+K217T+K240F+S256Q+R267H+I294E、 R20K+S123P+Q137K+K169R+K217T+K240F+S256Q+R267H+I294E、 R20K+S123P+N155D+K169R+K217T+K240F+S256Q+R267H+I294E+D384G+E489R、 R20K+S123P+N155D+K169R+K217T+K240F+S256Q+R267H+I294E+S474E、 R20K+S123P+N155D+K169R+K217T+K240F+S256Q+R267H+I294E、 R20K+S123P+Q147K+K169R+V219T+K240F+S256Q+R267H+I294E、 R20K+A41L+S123P+L152P+K169R+K217T+K240F+S256Q+R267H+I294E、 K8R+R20K+S123P+K169R+D210H+K217T+K240F+S256Q+R267H+I294E、 R20K+S123P+K169R+K217T+K240F+S256Q+R267H+I294E+Q329E+V431E+E489R、 P111Q+S123P+Q137K+Q147K+V159M+K169R+D210H+K240F+S256E+I294E+S402Q+K488T、 P111Q+S123P+Q137K+Q147K+V159M+K169R+K252E+S256Q+I294E+K322E+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+K169R+K240F+S256Q+I294E+K322E+S402Q、 S76E+P111Q+S123P+Q137K+Q147K+V159M+K169R+G237M+S256Q+I294E+S402Q、 S76E+P111Q+S123P+Q137K+Q147K+V159M+K169R+V203T+G237M+S256Q+I294E+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+K169R+G237M+S256Q+I294E+P339S+S402Q+K488T、 P111Q+S123P+Q137K+Q147K+V159M+K169R+G237M+T244R+S256Q+I294E+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+G237M+T244R+S256Q+I294E+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+K169R+V219T+K240F+S256Q+I294E+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+K169R+V203T+S256Q+I294E+S402Q、 Q82E+P111Q+S123P+Q137K+V159M+V203T+D210H+G237M+S256E+I294E、 Q82E+P111Q+S123P+V159M+V203T+G237M+K252E+S256E+I294E、 S76E+Q82E+P111Q+S123P+V159M+V203T+G237M+S256E+I294E、 Q82E+P111Q+S123P+Q147K+V159M+V203T+G237M+S256E+I294E、 S76E+Q82E+P111Q+S123P+V159M+V203T+G237M+S256E+I294E+S474E+E489R+P492D、 Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E、 Q82E+P111Q+S123P+V159M+V203T+G237M+T244R+S256E+I294E、 S76E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V219T+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+K169R+L184M+K252E+S256Q+Q271E+I294E+Q329E+S402Q、 S76E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+A238S+S256E+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+A238S+S256E+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+E489R+V505L、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+D210H+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+E489R+P492D、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+D210H+T244R+K252E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+T244E+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+K347E+S402Q、 K8E+A83E+S94R+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+L152P+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E+K445E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K252E+S256Q+Q271E+I294E+Q329E+S402Q、 K8E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+D210H+K240F+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A41L+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K240F+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 Q82E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+D210H+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A41L+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A41L+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+V251E+S256E+Q271E+I294E+Q329E+S402Q、 P111Q+S123P+Q137K+Q147K+V159M+A238T+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+T244R+W248V+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+T244R+V251E+S256Q+Q271E+I294E+Q329E+S402Q、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+R295K+N298D+Q329E+S402Q+L447M、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256E+Q271D+I294E+Q329E+S402Q、 Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+Q271E+I294E+Q329E+N383E、 Q82E+P111Q+S123P+Q137K+V159M+K169R+A189G+V203T+G237M+T244R+S256E+I294E、 Q82E+P111Q+S123P+Q137K+V159M+K169R+V203T+G237M+T244R+V251E+S256E+I294E、 Q82E+P111Q+S123P+L152P+V159M+K169R+V203T+G237M+T244R+S256E+I294E、 Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E+N383Q+V431E、 R20K+S76E+Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E+Q329E+P492D、 S76E+Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E+Q329E+E489R+P492D、 Q82E+P111Q+S123P+Q137K+N155D+V159M+K169R+V203T+G237M+T244R+S256E+I294E+K445E、 S76E+Q82E+S94R+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E、 K8E+A41L+S76E+Q82E+P111Q+S123P+V159M+K169R+V203T+G237M+T244R+S256E+I294E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+S256E+Q271E+I294E+Q329E+P339S+N383E+S402Q+V431E、 S76E+Q82E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q+V431E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+K252E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q+V431E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V203T+K240F+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V219T+G237M+S256Q+Q271E+I294E+Q329E+S402Q+V431E+S474E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+P492D、 S76E+A83E+P111Q+S123P+Q137K+Q147K+N155D+L184M+G237M+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+A189G+V251E+S256Q+Q271E+I294E+Q329E+N383Q+S402Q+V431E、 K8E+A41L+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+K394R+S402Q+V431E、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271D+I294E+Q329E+N383E+S402Q+V431E+A459P、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+K347E+N383E+S402Q+V431E+A491V、 K8E+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V、 K8R+A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+S402Q+V431E+E489K、 A83E+P111Q+S123P+Q137K+Q147K+V159M+L184M+V251E+S256Q+Q271E+I294E+Q329E+N383E+S402Q+V431E+A491V, wherein the variant has xyloglucanase activity and wherein the variant has at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, such as at least 96%, at least 97%, at least 98%, or at least 99% sequence identity with the polypeptide of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 3, but less than 100% sequence identity.

4. A xyloglucanase variant comprising a substitution at position 129T of the polypeptide corresponding to SEQ ID NO: 2, wherein the variant has xyloglucanase activity.

5. The variant of claim 4, wherein the variant has at least 99% but less than 100% sequence identity with the polypeptide of SEQ ID NO:

2.

6. A variant according to any one of claims 4-5, wherein the variant comprises or is composed of the polypeptide of SEQ ID NO:

3.

7. A variant according to any one of claims 1-6, wherein the variant has improved properties relative to the parent, such as improved thermal stability, improved detergent storage stability, detergent storage stability in the presence of a chelating agent or chelating reagent, improved washing performance, and / or improved enzyme washing benefits.

8. The variant of any one of claims 1-7, having at least 1.1, for example at least 1.2, at least 1.3, at least 1.4, at least 1.5 half-life improving factor (HIF) and / or stability improving factor (SIF) compared to the reference polypeptide of SEQ ID NO: 2 or SEQ ID NO:

3.

9. A detergent composition comprising a variant as described in any one of claims 1-8.

10. The detergent composition of claim 9, wherein the detergent composition is in the form of: strips, uniform tablets, tablets having two or more layers, unit dose products such as bags having one or more chambers, regular or compressed powders, granules, pastes, gels, or regular, compressed or concentrated liquids.

11. An isolated polynucleotide encoding a variant as described in any one of claims 1-8.

12. A nucleic acid construct or expression vector comprising the polynucleotide as described in claim 11.

13. A recombinant host cell, wherein the recombinant host cell is converted with the polynucleotide as described in claim 11.

14. A method for generating a variant of a variant, the method comprising: a. Culture the recombinant host cells as described in claim 13 under conditions suitable for expressing the variant; as well as b. Recycle the variant.

15. The use of the variants of any one of claims 1-8 or the detergent composition of claims 9-10 for cleaning articles, for pretreating stains on the articles, for preventing, reducing or removing redeposition of dirt during a washing cycle, and / or for maintaining or improving the whiteness of the articles.

16. The use as described in claim 15, wherein the article is a textile or a hard surface, such as tableware.

17. A washing method for washing articles, the washing method comprising: c. Exposing the article to a detergent solution comprising a variant of any one of claims 1-8 or a detergent composition as described in any one of claims 9-10; d. Complete at least one washing cycle; and e. Optional: Rinse the item. The item in question is a textile.

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