Biopolymers for use in detergent

Abstract

The invention concerns biopolymers that are stable in a detergent composition comprising one or more enzymes having carbohydrase activity. In particular, the biopolymers are stable in the presence of the most widely used carbohydrases in detergents, i.e. amylase, pectate lyase, cellulase and mannanase.

Description

[0001] BIOPOLYMERS FOR USE IN DETERGENT

[0002] Reference to sequence listing

[0003] This application contains a Sequence Listing in computer readable form. The computer readable form is incorporated herein by reference.

[0004] FIELD OF THE INVENTION

[0005] The present invention relates to biopolymers that can be used in detergents, in particular laundry detergents, the use of said biopolymers as well as the enzymatic synthesis of these biopolymers.

[0006] BACKGROUND OF THE INVENTION

[0007] Polymers are found in many detergents for cleaning where they play an important role as e.g. dispersants, precipitation inhibitors, foam controllers, antiredeposition polymers and formulation aids, such as viscosity modifiers and viscosity reducing agents in liquid detergents.

[0008] However, polymers are often derived from petrochemical resources and have faced scrutiny due to environmental concerns, most of all for not being sustainable because they are from a nonrenewable source and are poorly biodegradable or even persistent in the environment. It is desirable to provide alternative polymers that have an improved sustainability profile while maintaining compatibility with other detergent ingredients, including enzymes. In addition, the consumer benefits and performance effects must be maintained.

[0009] WO 2014 / 052386 discloses the synthesis of poly-alpha-1 , 3-D-glucose by contacting an aqueos solution of sucrose with GtfJ glucosyltransferase isolated from Streptococcus salivarus.

[0010] EP 3 628 691 B1 discloses a composition comprising a polysaccharide substituted with at least one hydrophobic group and at least one hydrophilic group.

[0011] SUMMARY OF THE INVENTION

[0012] The invention provides biopolymers that are compatible with detergents, in particular detergents for cleaning, such as laundry detergents and detergents for hard surface cleaning.

[0013] The vast majority polymers for detergents are petrochemically derived and not sustainable because they are derived from a non-renewable source and are poorly biodegradable or even persistent in the environment. The inventors of the present invention have surprisingly found that more sustainable detergent compositions, i.e. detergent compositions with an improved sustainability profile, can be achieved by replacing petrochemically derived polymers in detergents partly or even completely with carbohydrate-based biopolymers that are stable in detergent compositions comprising enzymes that have carbohydrase activity, such as amylases, pectate lyases, mannanases, xanthan lyases, xyloglucanases and cellulases.

[0014] 1. The replacement of petrochemically derived polymers with biopolymers addresses the United Nations’ Sustainable Development Goals, in particular Goal 12 “Responsible consumption and production”: replacing petrochemically derived polymers with biopolymers allows the detergent producer - and thus the end user - to move from a fossil feedstock to a renewable feedstock and reduces the volume of persistent chemicals emitted to the environment. Consequently, the invention discloses biopolymers that, partly or fully, can replace petrochemically derived polymers, thereby improving the sustainability profile of the detergent, said biopolymer characterised in that a. The biopolymer consists of carbohydrate monomers selected from the group consisting of glucose, mannose, rhamnose, galactose, fructose, xylose and arabinose; and b. The carbohydrate monomers of the biopolymer are linked via alpha-1 ,2, alpha-1 ,3, alpha-1 ,4, alpha-1 ,6, beta-1 ,2, beta-1 ,3, beta-1 ,4, beta-1 ,6, or beta-2,1 glycosidic linkage or a combination thereof; and c. The degree of polymerization (DP) of the biopolymer is in the range 5-100.

[0015] DEFINITIONS

[0016] Bacterial:

[0017] The term “bacterial” in relation to polypeptide (such as an enzyme, e.g. a betagalactosidase, fruc- tosyltransferase or inulinase) refers to a polypeptide encoded by and thus directly derivable from the genome of a bacteria, where such bacteria has not been genetically modified to encode said polypeptide, e.g. by introducing the encoding sequence in the genome by recombinant DNA technology. In the context of the present invention, the term “bacterial enzymed” or “polypeptide having enzyme activity obtained from a bacterial source” or “polypeptide is of bacterial origin” thus refers to an enzyme encoded by and thus directly derivable from the genome of a bacterial species, where the bacterial species has not been subjected to a genetic modification introducing recombinant DNA encoding said enzymed. Thus, the nucleotide sequence encoding the bacterial polypeptide having the desired enzyme activity, such as betagalactosidase, fructosyltransferase or inulinase activity, is a sequence naturally in the genetic background of a bacterial species. A sequence encoding a bacterial polypeptide having enzyme activity may also be referred to a wildtype enzyme (or parent enzyme). Bacterial polypeptide having enzyme activity includes recombinant produced wild types. In a further aspect, the invention provides polypeptides having enzyme activity, such as betagalactosidase, fructosyltransferase or inulinase activity, wherein said polypeptides are substantially homologous to a bacterial enzyme. In the context of the present invention, the term “substantially homologous” denotes a polypeptide having enzyme activity (such as betagalactosidase, fructosyltransferase or inulinase) which is at least 80%, preferably at least 85%, more preferably at least 90%, more preferably at least 95%, even more preferably at least 96%, 97%, 98%, and most preferably at least 99% identical to the amino acid sequence of a selected (parent) bacterial enzyme. Beta-galactosidase

[0018] Beta-galactosisdase catalyzes hydrolysis of terminal non-reducing -D-galactose residues in - D-galactosides.

[0019] Biopolymer

[0020] Biopolymers consist of monomeric units that are covalently bonded in chains to form larger molecules, wherein the monomeric units are from renewable ressources, such as sugar or other carbohydrates. In the context of the present invention the term “biopolymers” encompasses oligomers and polymers. The biopolymer may be homooligomers, e.g. homooligosaccharides, heterooligomers, e.g. heterooligosaccharides, homopolymers, e.g. homopolysaccharides, and heteropolymers, e.g. heteropolysaccharides or combinations (e. g. blocks of oligomers). Further, the biopolymer can be linear or branched, and substituted or unsubstituted. Substituted biopolymers may also be referred to as derivatized biopolymers which are biopolymer backbones modified chemically to add functional groups with charge, hydrophobicity, hydrophilicity according to the performance characteristics. The biopolymers are considered stable in a detergent composition if no enzymes are present with the specific glycoside hydrolase activity that corresponds to the glycosidic links in the biopolymer. The stability of the biopolymer may be tested by use of standard analytical methods: Gel Permeation Chromatography (GPC), Fourier Transform Infrared Spectroscopy (FTIR), Nuclear Magnetic Resonance (NMR), and Mass Spectrometry (MS) can be used to detect changes in polymer structure or composition. Alternatively the stability of the biopolymer can be tested by performance assays after incubation of the biopolymer, all relevant carbohydrases for laundry in a laundry detergent after a certain time (e.g. 2 weeks at elevanted temperature, 37° C).

[0021] Color difference (L value):

[0022] The L value in the Cl ELAB color space is a measure of lightness or darkness of a color. It ranges from 0 (black) to 100 (white), with 50 being the neutral gray point.

[0023] Degree of polymerization (DP).

[0024] Degree of polymerization is the average count glycosides in an oligo or polysaccharide. For example DP 5 could be 5 glucose units or 1 glucose unit and 4 galactose units.

[0025] Degree of substitution (DS)

[0026] Polysaccharides of hexoses have three hydroxyl groups per structural unit. The hydrogen atoms of these three hydroxyl groups are available for being substituted. The degree of substitution is defined to be the average substitution of each structural unit and has at maximum a value of 3. This definition of the term ‘degree of substitution’ applies likewise to polysaccharides of other units, e.g. pentose. Degree of functionalization (DF)

[0027] The degree of functionalization is the overall average weight of the functionalization divided by the average mass of the full biopolymer. For example, if there are 10 DP glucose (a 180 g / mol) in the biopolymer backbone and DS 1 with sodium carboxymethyl (a 81 g / mol), then DF is 0.31.

[0028] Detergent adjunct ingredient:

[0029] The detergent adjunct ingredient is different to the biopolymers of this invention. The precise nature of these additional adjunct components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the operation for which it is to be used. Suitable adjunct materials include, but are not limited to the components described below such as surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, s, s, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and cobuilders, fabric hueing agents, anti-foaming agents, dispersants, processing aids, solvents, and / or pigments.

[0030] Detergent composition:

[0031] The term “detergent composition” refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles. The detergent composition may be used to e.g. clean textiles for both household cleaning and industrial cleaning. The terms encompass any materials / compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, bar, or spray compositions) and includes, but is not limited to, detergent compositions (e.g., liquid and / or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; laundry boosters; and textile and laundry pre-spotters / pre-treatment). In addition to containing the biopolymer the invention, the detergent formulation may contain one or more additional enzymes (such as proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, phosphodiesterases, dispersin, catalases and mannanases, or any mixture thereof), and / or detergent adjunct ingredients such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers (as set forth herein), fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, bluing agents and fluorescent dyes, antioxidants, and solubilizers. Enzyme detergency benefit:

[0032] The term “enzyme detergency benefit” is defined herein as the advantageous effect an enzyme may add to a detergent compared to the same detergent without the enzyme. Important detergency benefits which can be provided by enzymes are stain removal with no or very little visible soils after washing and / or cleaning, prevention or reduction of redeposition of soils released in the washing process (an effect that also is termed anti-redeposition), restoring fully or partly the whiteness of textiles which originally were white but after repeated use and wash have obtained a greyish or yellowish appearance (an effect that also is termed whitening). Also included is the maintenance of whiteness, e.g., the prevention of greying or dullness. Textile care benefits, which are not directly related to catalytic stain removal or prevention of redeposition of soils, are also important for enzyme detergency benefits. Examples of such textile care benefits are prevention or reduction of dye transfer from one fabric to another fabric or another part of the same fabric (an effect that is also termed dye transfer inhibition or anti-backstaining), removal of protruding or broken fibers from a fabric surface to decrease pilling tendencies or remove already existing pills or fuzz (an effect that also is termed anti-pilling), improvement of the fabric-softness, colour clarification of the fabric and removal of particulate soils which are trapped in the fibers of the fabric or garment. Enzymatic bleaching is a further enzyme detergency benefit where the catalytic activity generally is used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides.

[0033] Essentially water-free:

[0034] In the context of the present invention the term “essentially water-free” refers to an environment, such as a solvent, comprising less than 5% w / w water, less than 1 % w / w water, preferably less than 0.1 % w / w water.

[0035] Fragment:

[0036] The term “fragment” means a polypeptide having one or more (e.g., several) amino acids absent from the amino and / or carboxyl terminus of a mature polypeptide or domain; wherein the fragment has the desired activity (e.g., glycosyltransferase, betagalactosidase, fructosyltransferase or inulinase activity).

[0037] Fructosyltransferase:

[0038] Fructosyltransferase catalyzes hydrolysis of terminal non-reducing p-D-galactose residues in p- D-galactosides

[0039] Fungal:

[0040] In the context of the present invention the term “fungal” in relation to polypeptide (such as an enzyme) refers to a polypeptide encoded by and thus directly derivable from the genome of a fungus, where such fungus has not been genetically modified to encode said polypeptide, e.g. by introducing the encoding sequence in the genome by recombinant DNA technology. In the context of the present invention, the term “fungal enzyme” or “polypeptide having enzyme activity obtained from a fungal source” thus refers to an enzyme encoded by and thus directly derivable from the genome of a fungal species, where the fungal species has not been subjected to a genetic modification introducing recombinant DNA encoding said enzyme. Thus, the nucleotide sequence encoding the fungal polypeptide having enzyme activity is a sequence naturally in the genetic background of a fungal species. The fungal polypeptide having enzyme activity encoding by such sequence may also be referred to a wildtype enzyme (or parent enzyme). In a further aspect, the invention provides polypeptides having enzyme activity, wherein said polypeptides are substantially homologous to a fungal enzyme. In the context of the present invention, the term “substantially homologous” denotes a polypeptide having the same enzyme activity as the parent enzyme which is at least 80%, preferably at least 85%, more preferably at least 90%, more preferably at least 95%, even more preferably at least 96%, 97%, 98%, and most preferably at least 99% identical to the amino acid sequence of a selected (parent) fungal enzymee.

[0041] Glycosyltransferases:

[0042] Glycosyltransferases (GTFs, Gtfs) are enzymes (EC 2.4) that establish natural glycosidic linkages. They catalyze the transfer of saccharide moieties and are in this manner capable of forming oligosaccharide and polysaccharide. Glycosyltransferase encompass hexosyltransferase and pentosyltransferase as well as glycosyltransferases making branched glucan with 1 ,3-glucosidic linkages and 1 ,4-glucosidic linkages. Glycosidases can also be used to generate glycosidic bonds and build oligo- and polysaccharides from disaccharides.

[0043] Host cell:

[0044] The term "host cell" means any cell type that is susceptible to transformation, transfection, transduction, or the like with a nucleic acid construct or expression vector comprising a polynucleotide of the present invention. The term “host cell” encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that occur during replication.

[0045] Improved wash performance:

[0046] The term “improved wash performance” is defined herein as an biopolymerdisplaying an increased wash performance in a detergent composition relative to the wash performance of same detergent composition without the biopolymer e.g. by increased stain removal, increased whiteness or color maintainence or less redeposition. The term “improved wash performance” includes wash performance in laundry.

[0047] Inulinase:

[0048] Inulinase hydrolyzes the 2, 1-linked beta-glycosidic bonds between fructose monomers, and between fructo ant the terminal sucrose of fructans.

[0049] Isolated:

[0050] The term “isolated” means a substance in a form or environment that does not occur in nature. Non-limiting examples of isolated substances include (1) any non-naturally occurring substance, (2) any substance including, but not limited to, any enzyme, variant, nucleic acid, protein, peptide or cofactor, that is at least partially removed from one or more or all of the naturally occurring constituents with which it is associated in nature; (3) any substance modified by the hand of man relative to that substance found in nature; or (4) any substance modified by increasing the amount of the substance relative to other components with which it is naturally associated (e.g., recombinant production in a host cell; multiple copies of a gene encoding the substance; and use of a stronger promoter than the promoter naturally associated with the gene encoding the substance). An isolated substance may be present in a fermentation broth sample; e.g. a host cell may be genetically modified to express the polypeptide of the invention. The fermentation broth from that host cell will comprise the isolated polypeptide.

[0051] Laundering:

[0052] The term “laundering” relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a biopolymer of the present invention. The laundering process can for example be carried out using e.g. a household or an industrial washing machine or can be carried out by hand.

[0053] Malodor:

[0054] The term ’’malodor” means an odor which is not desired on clean items. The cleaned item should smell fresh and clean without malodors adhered to the item. One example of malodor is compounds with an unpleasant smell, which may be produced by microorganisms. Another example is unpleasant smells can be sweat or body odor adhered to an item which has been in contact with human or animal. Another example of malodor can be the odor from spices, which sticks to items for example curry or other exotic spices which smells strongly.

[0055] Mature polypeptide:

[0056] The term “mature polypeptide” means a polypeptide in its final form following translation and any post-translational modifications, such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc. Mature polypeptide coding sequence:

[0057] The term “mature polypeptide coding sequence” means a polynucleotide that encodes a mature polypeptide having enzyme activity.

[0058] Nucleic acid construct:

[0059] The term "nucleic acid construct" means a nucleic acid molecule, either single- or doublestranded, which is isolated from a naturally occurring gene or is modified to contain segments of nucleic acids in a manner that would not otherwise exist in nature or which is synthetic, which comprises one or more control sequences.

[0060] Operably linked:

[0061] The term “operably linked” means a configuration in which a control sequence is placed at an appropriate position relative to the coding sequence of a polynucleotide such that the control sequence directs expression of the coding sequence.

[0062] Primer:

[0063] The term “primer” refers to any molecule that can act as the initiator for an enzyme used in the process for producing a biopolymer. Monosaccharides, disaccharides and oligosaccharides consisting of 3-10 monosaccharides can serve as primers herein.

[0064] Rhamnolipid:

[0065] Rhamnolipid (RL) is a glycolipid that may be used as a biodegradable surfactant. RL may be in the form of mono-rhamnolipid or di-rhamnolipid, which consist of one or two rhamnose groups respectively, wherein the length of the chain may vary: m,n being 4 to 8.

[0066]

[0067] (Appl Microbiol Biotechnol (2005) 68: 718-725).

[0068] In the context of the present invention the term “rhamnolipid” includes mono-rhamnolipid or dirhamnolipid, mixtures thereof and varying chain length as well as salts of rhamnolipid. Sophorolipids (SL) is a glycolipid that may be used as a biodegradable surfactant. SL may be in the lactonic or acidic form.

[0069] Sequence difference:

[0070] The term "sequence difference" means the percent of amino acid differences between a polypeptide and the polypeptide of SEQ ID NO: X, where X has the value 1 , 2, 3, or 4, and is calculated as follows:

[0071] (Different Residues x 100) / (Length of SEQ ID NO: X) wherein the different residues comprise any substitution, deletion, or insertion (e.g., an extension at the N-terminus and / or C-terminus) in the sequence.

[0072] Sequence identity: The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”. For purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), pref-erably version 5.0.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled “longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows:

[0073] (Identical Residues x 100) / (Length of Alignment - Total Number of Gaps in Alignment).

[0074] For purposes of the present invention, the sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented in the Needle program of the EMBOSS package (EM-BOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), prefer-ably version 5.0.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NLIC4.4) substitution matrix. The output of Needle labeled “longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows:

[0075] (Identical Deoxyribonucleotides x 100) / (Length of Alignment - Total Number of Gaps in Alignment).

[0076] Substantially the same:

[0077] The term “substantially same” in the present invention is within the reasonable understanding of those skilled in the art, and may mean that the level of lipid removal of different detergent compositions is similar or no obvious difference, for example, the difference in the level of lipid removal is within e.g. 1%, 2% or 3% depending on the experimental errors.

[0078] Sustainability:

[0079] Sustainability and sustainable means use of renewable resources that cause little or no damage to the environment and are biodegradable.

[0080] Sustainability profile:

[0081] In the context of the present invention the term sustainability profile is used for comparing the sustainability of ingredients (e.g. in a detergent composition) where one or more ingredients can replace other less sustainable ingredients while maintaining the performance of the system (e.g. the performance of a detergent composition during wash of an item).

[0082] Textile:

[0083] The term “textile” means any textile material including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material, fabrics made of these materials and products made from fabrics (e.g., garments and other articles). The textile or fabric may be in the form of knits, wovens, denims, non-wovens, felts, yarns, and toweling. The textile may be cellulose based such as natural cellulosics, includ-ing cotton, flax / linen, jute, ramie, sisal or coir or manmade cellulosics (e.g. originating from wood pulp) including viscose / rayon, cellulose acetate fibers (tricell), lyocell or blends thereof. The textile or fabric may also be noncellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and span- dex / 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 with one or more companion material such as wool, synthetic fiber (e.g. polyamide fiber, acrylic fiber, polyester fiber, polyvinyl chloride fiber, polyurethane fiber, polyurea fiber, aramid fiber), and / or cellulose-containing fiber (e.g. rayon / viscose, ramie, flax / linen, jute, cellulose acetate fiber, lyocell). Fabric may be conventional washable laundry, for example stained household laundry. When the term fabric or garment is used it is intended to include the broader term textiles as well. In the context of the present invention, the term “textile” also covers fabrics. In the context of the present invention, the term “textile” is used interchangeably with fabric and cloth.

[0084] Used or worn:

[0085] The term “used or worn” used herein about a textile means that textile that has been used or worn by a consumer or has been in touch with human skin e.g. during manufacturing or retailing. A consumer can be a person that buys the textile, e.g. a person buying a textile (e.g. new clothes or bedlinen) in a shop or a business that buys the textile (e.g. bed linen, tea towel or table cloth) for use in the business e.g. a hotel, a restaurant, a professional kitchen, an institution, a hospital or the like. In some situations, such used or worn textile bear the conventional stains which has not been thoroughly washed out and can form a gluing base for attracting and accumulating more airborne particulate matter.

[0086] Variant:

[0087] The term “variant” means a polypeptide having same activity as the parent enzyme comprising an alteration, i.e., a substitution, insertion, and / or deletion, at one or more (e.g., several) positions. A substitution means replacement of the amino acid occupying a position with a different amino acid; a deletion means removal of the amino acid occupying a position; and an insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.

[0088] Wash cycle:

[0089] The term “wash cycle” is defined herein as a washing operation wherein textiles are immersed in the wash liquor, mechanical action of some kind is applied to the textile in order to release stains and to facilitate flow of wash liquor in and out of the textile and finally the superfluous wash liquor is removed. After one or more wash cycles, the textile is generally rinsed and dried.

[0090] Wash liquor:

[0091] The term “wash liquor” is defined herein as the solution or mixture of water and detergent components optionally including the enzyme invention.

[0092] Wash performance:

[0093] The term “wash performance” is used as detergent composition’s, enzyme’s or polymer’s capability to remove stains present on the object to be cleaned or maintain color and whiteness of textile during wash. The improvement in the wash performance may be quantified by calculating the so-called delta REM as described in Experimental section.

[0094] Weight percentage:

[0095] Weight percentage is abbreviated w / w%, wt% or w%. The abbreviations are used interchangeably.

[0096] Whiteness:

[0097] The term “Whiteness” is defined herein as a broad term with different meanings in different regions and for different consumers. Whiteness can be on white textiles or be used interchangely as brightness for colored textiles. Loss of whiteness or brightness can e.g. be due to greying, yellowing, or removal of optical brighteners / hueing agents. Greying and yellowing can be due to soil redeposition, stain redeposition, dirt / mud redeposition, pollution particles, body soils, colouring from e.g. iron and copper ions or dye transfer. Loss of whiteness might include one or several issues from the list below: colourant or dye effects; incomplete stain removal (e.g. body soils, sebum etc.); redeposition (greying, yellowing or other discolourations of the object) (removed soils reassociate with other parts of textile, soiled or unsoiled); chemical changes in textile during application; and clarification or brightening of colours.

[0098] Wild-type:

[0099] The term "wild-type" in reference to an amino acid sequence or nucleic acid sequence means that the amino acid sequence or nucleic acid sequence is a native or naturally-occurring sequence. As used herein, the term "naturally-occurring" refers to anything (e.g., proteins, amino acids, or nucleic acid sequences) that is found in nature. Conversely, the term "non-naturally occurring" refers to anything that is not found in nature (e.g., recombinant nucleic acids and protein sequences produced in the laboratory or modification of the wild- type sequence). CONVENTIONS FOR DESIGNATION OF VARIANTS

[0100] For purposes of the present invention, the polypeptide disclosed in SEQ I D NO: 1 , can be selected as the parent enzyme and used to determine the corresponding amino acid positions in another inulinase. E.g. the amino acid sequence of another inulinase is aligned with the polypeptide disclosed in the parent enzyme SEQ ID NO: 1 , and based on the alignment, the amino acid position number corresponding to any amino acid residue in the polypeptide disclosed in the parent (e.g., SEQ ID NO: 1) is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.

[0101] Analogously to the above, SEQ ID NO: 2, can be selected as the parent enzyme and used to determine the corresponding amino acid positions in another alternan sucrase; SEQ ID NO: 3, can be selected as the parent enzyme and used to determine the corresponding amino acid positions in another glycosyltransferase; and SEQ ID NO: 4, can be selected as the parent enzyme and used to determine the corresponding amino acid positions in another betagalactosidase.

[0102] In describing the variants of the present invention, the nomenclature described below is adapted for ease of reference. The accepted IIIPAC single letter or three letter amino acid abbreviation is employed.

[0103] Substitution of amino acids in peptides and polypeptides

[0104] For an amino acid substitution, the following nomenclature is used: Original amino acid, position, substituted amino acid. Accordingly, the substitution of threonine at position 226 with alanine is designated as “Thr226Ala” or “T226A”. Multiple mutations are separated by addition marks (“+”) or comma (“,”), e.g., “Gly205Arg + Ser411 Phe” or“G205R + “S411 F”, Gly205Arg,Ser411 Phe” or “G205R,S411 F” representing substitutions at positions 205 and 411 of glycine (G) with arginine (R) and serine (S) with phenylalanine (F), respectively.

[0105] Deletions

[0106] For an amino acid deletion, the following nomenclature is used: Original amino acid, position, *. Accordingly, the deletion of glycine at position 195 is designated as “Gly195*” or “G195*”. Multiple deletions are separated by addition marks (“+”) or commas (“,”), e.g., “Gly195* + Ser411*” or “G195* + S411*”. Insertions

[0107] For an amino acid insertion, the following nomenclature is used: Original amino acid, position, original amino acid, inserted amino acid. Accordingly, the insertion of lysine after glycine at position 195 is designated “Gly195GlyLys” or “G195GK”. An insertion of multiple amino acids is designated [Original amino acid, position, original amino acid, inserted amino acid #1 , inserted amino acid #2; etc.]. For example, the insertion of lysine and alanine after glycine at position 195 is indicated as “Gly195GlyLysAla” or “G195GKA”.

[0108] In such cases the inserted amino acid residue(s) are numbered by the addition of lower case letters to the position number of the amino acid residue preceding the inserted amino acid residue(s). In the above example, the sequence would thus be:

[0109] Multiple alterations

[0110] Variants comprising multiple alterations are separated by addition marks (“+”) or by commas e.g., “Arg170Tyr+Gly195Glu”, “R170Y+G195E”, “Arg170Tyr,Gly195Glu” or “R170Y.G195E” representing a substitution of arginine and glycine at positions 170 and 195 with tyrosine and glutamic acid, respectively.

[0111] Different alterations

[0112] Where different alterations can be introduced at a position, the different alterations are separated by a comma or slash e.g., “Arg170Tyr,Glu” or “Arg170Tyr / Glu” represents a substitution of arginine at position 170 with tyrosine or glutamic acid. Thus, “Tyr167Gly,Ala + Arg170Gly,Ala” or “Tyr167Gly / Ala + Arg170Gly / Ala” designates the following variants: “Tyr167Gly+Arg170Gly”, “Tyr167Gly+Arg170Ala”, “Tyr167Ala+Arg170Gly”, and “Tyr167Ala+Arg170Ala”.

[0113] Unspecified amino acid

[0114] Unless otherwise limited further, the amino acid X (or Xaa) is used herein to represent any of the 20 natural amino acids.

[0115] An “X” preceding a position means that any original amino acid at that position may be substituted. For example, X93Q means that any amino acid residue at position 93 other than Q is substituted with Q. This allows for designation of substitution to a particular amino acid in different parent mannanases, where the original amino acid may vary among different parent polypeptides.

[0116] DETAILED DESCRIPTION OF THE INVENTION

[0117] Polymers play an integral role in detergent compositions for textile cleaning where they contribute to a.o. soil-release, anti-redeposition of released soil, fiber protection, foam control, visual cues and opaqueness and dye-transfer inhibition. The vast majority of the polymers used today are derived from petrochemical ressources that are not renewable and many of the polymers used today are not readily biodegradable. This poses obviously an environmental problem and therefore there is a need for polymers from renewable sources, biopolymers. Bioplymers made of carbohydrates are particularly attractive as the building blocks, as carbohydrates are biodegradable, renewable and abundant. Carbohydrates can moreover be derivatized easily for tailoring chemical and physical properties towards a specific performance characteristic. The main challenge with the use of natural occurring polysaccharides from nature is that they are usually incompatible with liquid detergents, both due to large size not dissolving or creating undesired haze but also because they may be degraded by the commonly used carbohydrases used in laundry detergents.

[0118] Accordingly, the present invention concers biopolymers that are stable in a detergent composition comprising one or more enzymes having carbohydrase activity. In particular, the biopolymers are stable in the presence of the most widely used carbohydrases in detergents, i.e. amylases, pec- tate lyases, xyloglucanases, cellulases, and mannanases. The biopolymer of the present invention consists of carbohydrate monomers selected from the group consisting of glucose, mannose, rhamnose, galactose, fructose, xylose and arabinose comprising one or more glycosidic linkages selected from the group consisting of alpha-1 ,2, alpha-1 ,3, alpha-1 ,4, alpha-1 ,6, beta-1 ,2, beta- 1 ,3, beta-1 ,4, beta-1 ,6, or beta-2,1 glycosidic linkage. With the aim of strengthening the stability of the biopolymer, combinations of carbohydrate monomers and glycosidic linkages that are susceptible to hydrolysis by the most widely used in detergents (amylase, pectate lyase, cellulase, xyloglucanase and mannanase) are preferably avoided. Consequently, in a preferred embodiment the biopolymer comprises: a. at least two glucose monomers linked via alpha-1 ,2, beta-1 ,2, alpha-1 ,3, beta- 1 ,3, alpha-1 ,6, beta-1 ,6, or beta-2,1 glycosidic linkage; b. at least two mannose monomers linked via alpha-1 ,3, alpha-1 ,4, alpha-1 ,6, beta- 1 ,2, beta-1 ,6, or beta-2,1 glycosidic linkage; c. at least two rhamnose monomers linked via alpha-1 ,2, glycosidic linkage; and / or d. at least two galactose monomers linked via alpha-1 ,6, beta-1 ,3, beta-1 ,4, or beta- 1 ,6 glycosidic linkage; and / or e. at least two fructose monomers linked via alpha-1 ,2, beta-1 ,2, or beta-2,1 glycosidic linkage; and / or f. at least two xylose monomers linked via beta-1 ,3, or beta-1 ,4 glycosidic linkage; and / or g. at least two arabinose monomers linked via beta-1 ,3 glycosidic linkage; or a mixture or any of the glycosidic linkages of a. to g above. The number of monomer units in the biopolymer (degree of polymerization, DP), is preferably in the range 5 to 100, such as 5 to 90, 5 to 80, 5 to 70, 5 to 60, 5 to 50, 5 to 40, 5 to 30, 5 to 20, or 5 to 10.

[0119] The biopolymer may consist of a single type of monomeric unit (e.g. glucose, galactose or fructose) or it may consist of two or three diffent carbohydrate monomers, such as glucose and fructose or glucose, mannose and fructose. Further the biopolymer may be branched or linear, and it may be substituted.

[0120] The poly- or oligosaccharide may be extracted from natural sources, potentially degraded or hydrolyzed (chemically or enzymatically) or may be made from mono-, di- or oligosaccharides by the use of glycosyltransferases or carbohydrase hydrolases.

[0121] In an the embodiment the biopolymer is substituted (derivatized), preferably with a hydrophilic group or a hydrophobic group, or the substituted biopolymer may be a amphiphilic derivat containing both hydrophobic and hydrophilic groups. Amphiphilic biopolymer derivates are of interest due to their enhanced adsorption characteristics at interfaces, which can lead to a reduction in surface tensions. For laundry applications, amphiphilic biopolymer derivatives may function as soil release agents wherein the hydrophobic groups adsorb to the hydrophobic substrate surface and the hydrophilic group repels soil.

[0122] Suitable hydrophobic groups include a Ci to Cis alkyl, a C2 to C18 alkene, a C2 to C18 alkyne, a polyether comprising repeat units of (-CH2CH2O-), (-CH2CH(CH3)O-), or mixtures thereof, wherein the total number of repeat units is in the range of from 3 to 100, a Ce to C20 aryl, a benzyl, a C1- C18 alkyl sulfonyl, a C6-C20 aryl sulfonyl group, a p-toluenesulfonyl group, polystyrene; methyacry- late and styrene co-polymers, polyester (e. g. polyethylene terephthalate); and combinations or co-polymer options thereof.

[0123] Suitable hydrophilic groups include carboxylic acids, carboxylic acid salts, sulfonic acid derivatives, sulfonic acid derivative salts, sulfuric acid derivatives, sulfuric acid derivative salts, thiosulfate, thiosulfate salts, phosphoric acid derivatives, phosphoric acid derivative salts, alkyl amines, alkyl substituted ammonium salts, quaternized pyridine salts, quaternized imidazole salts, and a combination thereof. Examples include carboxymethyl, benzoylmethyl; vinylsulfone; poly or oligoacrylate, poly or oligo acrylate / maleate; acetylated / benzoylated polycarboxylic acids (eg polyvinylacetate); AMPS cross-polymer (polymerization of 2-Acrylamido-2-methylpropane sulfonic acid.

[0124] Hydrophilic and hydrophobic groups may be combined on the polysaccharide and may be combined as co-polymers, graft polymers or block polymers.

[0125] The hydrophobic and hydrophilic groups are independently linked to the polysaccharide through a chemical linkage such as alkylene, ester (COO-, -OOC), amide (-CONH-), carbamate (-NHCO- ), ether (-O-), thioether (-S-), sulfonate (-OSO2-), sulfate(-OSC>2O-), thiosulfate (-SS(C>2)O), carbonate (-OCOO-), urethane (-NHCOO-, -OOCNH), urea (-NHCONH-), amine (-NH-), phosphate (-OPC>2(OR)), or phosphonate (-PC>2(OR)-).

[0126] In a further embodiment the one or more substituents may be selected from the naturally occcur- ing amino acids.

[0127] In a preferred embodiment the substituent is selected from the group consisting of carboxymethyl, benzoylmethyl, acrylic / maleic acid copolymer, polyacrylate, PEG, PPG; sulfated PEG, polyvinylacetate, polyester, polyethylene terephthalate, styrene, methacrylate and styrene copolymers or a combination of one or more of the substituents.

[0128] The Degree of substitution (DS) is between 0.1-2; more preferably between 0.2-1.5 or 0.2-1 or 1- 1.5.

[0129] The degree of functionalization (DF) is between 0.1 -0.9; between 0.2-0.8. If the Degree of polymerization (DP) is lower, e.g 5-20, then DF is between 0.5-0.8; if DP is higher, e.g. 50-100, then DF is lower, e.g 0.2-0.5.

[0130] The size of the biopolymer including derivatization is preferably below 100,000 g / mol; below 50,000 g / mol; 25,000 g / mol or below 10,000 g / mol or is 1 ,000-10,000 g / mol or 10,000-50,000 g / mol.

[0131] The renewable carbon content (RCI) of the biopolymer including derivatization may be above 25%, above 40%, above 50% and more preferably above 80%.

[0132] The biopolymer has preferably a water solubility of at least 1% w / w, preferably at least 2% w / w in water at 20°C and 1 bar.

[0133] The biopolymer has a biodegradation of more than 30%, more than 50%, preferably more than 60% in 28 days in accordance with OECD Guideline for testing of chemicals (301 B).

[0134] Different types of current polymers

[0135] Polymers with antiredeposition benefits: “antiredeposition polymers” are polymers which are able to suspend or capture dirt in wash and are also commonly referred to as dispersants or water soluble dispersants and typically demonstrate performance difference versus a detergent without the polymer in Test 1 , test 2, test 3 and test 4 described in experimental section. Examples of synthetic antiredeposition polymers are homopolymers of polyacrylate (E.g Sokalan PA, BASF; Acusol 445N, Dow); co-polymers of acrylate and maleate (e.g. Sokalan CP 5); polyethylene glycol polyvinylacetate co-polymer (e.g. Sokalan HP 22, BASF).

[0136] Polymers with soil release benefits: “soil release polymers” (SRP) are polymers which are able to bind to textile and provide easier stain removal on stains applied after prewashing with a such polymer and typically demonstrate performance difference versus a detergent wo the polymer in testl , test 2, test 3 and test 5 described in experimental section. Examples of synthetic soil release polymers are nonionic polyester or polyethylene / propylene terephthalate polymers (T exCare SRN range, Clariant, Repel-o-tex, Solvay); polyether polyester co or block polymers (Marloquest, Sasol); anionic polyester or polyethyleneterephthalate sulfonated (TexCare SRA range, Clariant; Sokalan SR 400, BASF)

[0137] Polymers with cleaning benefits: “Cleaning polymers” are polymers which are able to assist surfactant system in suspending dirt and typically demonstrate performance difference versus a detergent wo the polymer in test 1 and test 2 described in experimental section. Examples of synthetic cleaning polymers include aziridine homopolymers like polyethylene polyamine ethoxylated or alkoxylated, PEI-EO (e. g. Sokalan HP 20, Sokalan HP 30 booster, BASF) and Sulfated ethoxylated hexamethylene diamine (e.g. Sokalan HP 96, BASF).

[0138] Polymers with dye transfer inhibitor benefits: “dye transfer inhibitors” are polymers which are able to prevent color transfer from one textile to another and typically demonstrate performance difference versus a detergent wo the polymer in test 6 described in experimental section. Examples of synthetic dye transfer inhibitors include Vinylpyrrolidone / vinylimidazole co-polymers (PVP-NO) or modified (PVP-VI) (Sokalan HP 56, Sokalan HP 66, BASF) and polyvinylpyrrolidone (PVP) (Sokalan K 90).

[0139] “Opacifiers” are polymers which are low or insoluble in liquid detergents which creates an opague look but does not add cleaning benefit and typically demonstrate performance difference versus a detergent wo the polymer in Test 7 described in experimental section. Examples of synthetic opacifiers include styrene-acrylate copolymers (Acusol OP 301 , Dow)

[0140] The degree of substitution (DS) in a polymer refers to the average number of substituent groups per monomer unit in the polymer chain and is preferably in the of about 0.1 to about 3.0.

[0141] In another embodiment the present invention concerns a process for producing the biopolymers discussed above by the use of one or more enzymes. When the biopolymer is unsubstituted the process comprises the steps a) dissolving the carbohydrate, such as a monosaccharide, a disaccharide or a degradeable polysaccharide in a solvent, and b) adding an enzyme, such as a glycosyltransferase, to the solvent to obtain the desired biopolymer. Prefererred enzymes for use in the process are inulinase, betagalactosidase, glycosyltransferase and fructosyltransferase. It is immediate obvious that step a) and b) do not have to be separate steps but both carbohydrate and enzyme may be added to the solvent at the same time.

[0142] The above process for producing unsubstituted biopolymer is also useful for producing substituted biopolymers by reacting the unsubstituted biopolymer with a substituent to obtain the desired substituted biopolymer. The derivatization may take place in the same solvent as used for producing the biopolymer or in a subsequent step. The solvent used for producing may be essentially water free to avoid hydrolysis as the enzyme used may have hydrolase activity. Useful solvents include, but are not limited to, water (in the cases where the applied enzyme has essentially no hydrolase activity), alcohols, such as methanol, ethanol, ketones, such as acetone, 2-butanone (methyl ethyl ketone), and cyclohexanoneacetone, ethers, such as diethyl ether, tetrahydrofuran (THF), and dioxane , aromatics, organo- sulfur compounds, such as DMSO, or combinations thereof.

[0143] In a further aspect the invention concerns detergent compositions for textile and / or hard surface cleaning. Such detergent compositions, ingredients and formulation is discussed in more detail below.

[0144] In an aspect the invention concerns the use of a composition, preferably a detergent composition, comprising the bioplolymer of the invention, for cleaning of an item, such as a hard surface or a textile.

[0145] In a final aspect the the invention concerns a method for laundering an item comprising the steps of: a. Exposing an item to a wash liquor comprising a composition, preferably a detergent composition, comprising the polymer of the present inveention b. Completing at least one wash cycle; and c. Optionally rinsing the item, wherein the item is a textile.

[0146] Detergent Compositions

[0147] In one embodiment, the invention is directed to detergent compositions comprising a biopolymer of the invention in combination with one or more additional cleaning composition components. In one embodiment the detergent composition is in powder form. In another embodiment, the detergent composition is in a liquid or gel form. In another embodiment a bar form. In one embodiment the detergent may be wrapped in water soluble PVOH film. The choice of additional components is within the skill of the artisan and includes conventional ingredients, including the exemplary nonlimiting components set forth below.

[0148] Formulation of Detergent Products

[0149] The detergent composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid.

[0150] Pouches can be configured as single or multicompartments. It can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing the release of the composition to release of the composition from the pouch prior to water contact. The pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch. Preferred films are polymeric materials preferably polymers which are formed into a film or sheet. Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water-soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC). Preferably the level of polymer in the film for example PVA is at least about 60%. Preferred average molecular weight will typically be about 20,000 to about 150,000. Films can also be of blended compositions comprising hydrolytically degradable and water soluble polymer blends such as polylactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by MonoSol LLC, Indiana, USA) plus plasticisers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof. The pouches can comprise a solid laundry cleaning composition or part components and / or a liquid cleaning composition or part components separated by the water-soluble film. The compartment for liquid components can be different in composition than compartments containing solids: US2009 / 0011970 A1.

[0151] Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution.

[0152] A liquid or gel detergent, which is not unit dosed, may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water. Other types of liquids, including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel. An aqueous liquid or gel detergent may contain from 0-30% organic solvent. A liquid or gel detergent may be non-aqueous.

[0153] Laundry Soap Bars

[0154] The biopolymer of the invention may be added to laundry soap bars and used for hand washing laundry, fabrics and / or textiles. The term laundry soap bar includes laundry bars, soap bars, combo bars, syndet bars and detergent bars. The types of bar usually differ in the type of surfactant they contain, and the term laundry soap bar includes those containing soaps from fatty acids and / or synthetic soaps. The laundry soap bar has a physical form which is solid and not a liquid, gel or a powder at room temperature. The term solid is defined as a physical form which does not significantly change over time, i.e. if a solid object (e.g. laundry soap bar) is placed inside a container, the solid object does not change to fill the container it is placed in. The bar is a solid typically in bar form but can be in other solid shapes such as round or oval.

[0155] The laundry soap bar may contain one or more additional enzymes, protease inhibitors such as peptide aldehydes (or hydrosulfite adduct or hemiacetal adduct), boric acid, borate, borax and / or phenylboronic acid derivatives such as 4-formylphenylboronic acid, one or more soaps or synthetic surfactants, polyols such as glycerine, pH controlling compounds such as fatty acids, citric acid, acetic acid and / or formic acid, and / or a salt of a monovalent cation and an organic anion wherein the monovalent cation may be for example Na+, K+or NH4+and the organic anion may be for example formate, acetate, citrate or lactate such that the salt of a monovalent cation and an organic anion may be, for example, sodium formate.

[0156] The laundry soap bar may also contain complexing agents like EDTA and HEDP, perfumes and / or different type of fillers, surfactants e.g. anionic synthetic surfactants, builders, polymeric soil release agents, detergent chelators, stabilizing agents, fillers, dyes, colorants, dye transfer inhibitors, alkox- ylated polycarbonates, suds suppressers, structurants, binders, leaching agents, bleaching activators, clay soil removal agents, anti-redeposition agents, polymeric dispersing agents, brighteners, fabric softeners, perfumes and / or other compounds known in the art.

[0157] The laundry soap bar may be processed in conventional laundry soap bar making equipment such as, but not limited to, mixers, plodders, e.g. a two-stage vacuum plodder, extruders, cutters, logostampers, cooling tunnels and wrappers. The invention is not limited to preparing the laundry soap bars by any single method. The premix of the invention may be added to the soap at different stages of the process. For example, the premix containing a soap, biopolymer of the invention, optionally one or more enzymes, a protease inhibitor, and a salt of a monovalent cation and an organic anion may be prepared, and the mixture is then plodded. The biopolymer of the invention and optional additional enzymes may be added at the same time as the protease inhibitor for example in liquid form. Besides the mixing step and the plodding step, the process may further comprise the steps of milling, extruding, cutting, stamping, cooling and / or wrapping.

[0158] Granules

[0159] The present invention also relates to enzyme granules / particles comprising a biopolymer of the invention. In an embodiment, the granule comprises a core, and optionally one or more coatings (outer layers) surrounding the core.

[0160] The core may have a diameter, measured as equivalent spherical diameter (volume based average particle size), of 20-2000 pm, particularly 50-1500 pm, 100-1500 pm or 250-1200 pm. The core diameter, measured as equivalent spherical diameter, can be determined using laser diffraction, such as using a Malvern Mastersizer and / or the method described under ISO13320 (2020).

[0161] In an embodiment, the core comprises a biopolymer of the present invention.

[0162] The core may include additional materials such as fillers, fiber materials (cellulose or synthetic fibers), stabilizing agents, solubilizing agents, suspension agents, viscosity regulating agents, light spheres, plasticizers, salts, lubricants and fragrances.

[0163] The core may include a binder, such as synthetic polymer, wax, fat, or carbohydrate.

[0164] The core may include a salt of a multivalent cation, a reducing agent, an antioxidant, a peroxide decomposing catalyst and / or an acidic buffer component, typically as a homogenous blend. The core may include an inert particle with the polypeptide absorbed into it, or applied onto the surface, e.g., by fluid bed coating.

[0165] The core may have a diameter of 20-2000 pm, particularly 50-1500 pm, 100-1500 pm or 250- 1200 pm.

[0166] The core may be surrounded by at least one coating, e.g., to improve the storage stability, to reduce dust formation during handling, or for coloring the granule. The optional coating(s) may include a salt coating, or other suitable coating materials, such as polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA).

[0167] The coating may be applied in an amount of at least 0.1 % by weight of the core, e.g., at least 0.5%, at least 1 %, at least 5%, at least 10%, or at least 15%. The amount may be at most 100%, 70%, 50%, 40% or 30%.

[0168] The coating is preferably at least 0.1 pm thick, particularly at least 0.5 pm, at least 1 pm or at least 5 pm. In some embodiments, the thickness of the coating is below 100 pm, such as below 60 pm, or below 40 pm.

[0169] The coating should encapsulate the core unit by forming a substantially continuous layer. A substantially continuous layer is to be understood as a coating having few or no holes, so that the core unit has few or no uncoated areas. The layer or coating should, in particular, be homogeneous in thickness.

[0170] The coating can further contain other materials as known in the art, e.g. , fillers, antisticking agents, pigments, dyes, plasticizers and / or binders, such as titanium dioxide, kaolin, calcium carbonate or talc.

[0171] A salt coating may comprise at least 60% by weight of a salt, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% by weight.

[0172] To provide acceptable protection, the salt coating is preferably at least 0.1 pm thick, e.g., at least 0.5 pm, at least 1 pm, at least 2 pm, at least 4 pm, at least 5 pm, or at least 8 pm. In a particular embodiment, the thickness of the salt coating is below 100 pm, such as below 60 pm, or below 40 pm.

[0173] The salt may be added from a salt solution where the salt is completely dissolved or from a salt suspension wherein the fine particles are less than 50 pm, such as less than 10 pm or less than 5 pm.

[0174] The salt coating may comprise a single salt or a mixture of two or more salts. The salt may be water soluble, in particular, having a solubility at least 0.1 g in 100 g of water at 20°C, preferably at least 0.5 g per 100 g water, e.g., at least 1 g per 100 g water, e.g., at least 5 g per 100 g water. The salt may be an inorganic salt, e.g., salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids (less than 10 carbon atoms, e.g., 6 or less carbon atoms) such as citrate, malonate or acetate. Examples of cations in these salts are alkali or earth alkali metal ions, the ammonium ion or metal ions of the first transition series, such as sodium, potassium, magnesium, calcium, zinc or aluminum. Examples of anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, monobasic phosphate, dibasic phosphate, hypophosphite, dihydrogen pyrophosphate, tetraborate, borate, carbonate, bicarbonate, metasilicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, butyrate, propionate, benzoate, tartrate, ascorbate or gluconate. In particular, alkali- or earth alkali metal salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids such as citrate, malonate or acetate may be used.

[0175] The salt in the coating may have a constant humidity at 20°C above 60%, particularly above 70%, above 80% or above 85%, or it may be another hydrate form of such a salt (e.g., anhydrate). The salt coating may be as described in WO 00 / 01793 or WO 2006 / 034710.

[0176] Specific examples of suitable salts are NaCI (CH2o°c=76%), Na2CO3 (CH2o°c=92%), NaNO3(CH2O"C=73%), Na2HPO4(CH2o"c=95%), Na3PO4(CH25°c=92%), NH4CI (CH2o"c = 79.5%), (NH4)2HPO4(CH2O"C = 93,0%), NH4H2PO4(CH20°c = 93.1%), (NH4)2SO4(CH2o°c=81 .1%), KOI (CH2O"C=85%), K2HPO4(CH2O"C=92%), KH2PO4(CH2O°C=96.5%), KNO3(CH2O"C=93.5%), Na2SO4(CH2O"C=93%), K2SO4(CH2O"C=98%), KHSO4(CH2O"C=86%), MgSO4(CH2o"c=9O%), ZnSO4(CH2O°C=9O%) and sodium citrate (CH25°c=86%). Other examples include NaH3PO4, (NH4)H3PO4, CuSO4, Mg(NO3)2 and magnesium acetate.

[0177] The salt may be in anhydrous form, or it may be a hydrated salt, i.e., a crystalline salt hydrate with bound water(s) of crystallization, such as described in WO 99 / 32595. Specific examples include anhydrous sodium sulfate (Na3SO4), anhydrous magnesium sulfate (MgSO4), magnesium sulfate heptahydrate (MgSO47H3O), zinc sulfate heptahydrate (ZnSO47H3O), sodium phosphate dibasic heptahydrate (Na2HPO47H2O), magnesium nitrate hexahydrate (Mg(NO3)2(6H2O)), sodium citrate dihydrate and magnesium acetate tetrahydrate.

[0178] Preferably the salt is applied as a solution of the salt, e.g., using a fluid bed.

[0179] The coating materials can be waxy coating materials and film-forming coating materials. Examples of waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluid bed techniques are given in GB 1483591.

[0180] The granule may optionally have one or more additional coatings. Examples of suitable coating materials are polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are described in WO 93 / 07263 and WO 97 / 23606.

[0181] The core can be prepared by granulating a blend of the ingredients, e.g., by a method comprising granulation techniques such as crystallization, precipitation, pan-coating, fluid bed coating, fluid bed agglomeration, rotary atomization, extrusion, prilling, spheronization, size reduction methods, drum granulation, and / or high shear granulation. Methods for preparing the core can be found in the Handbook of Powder Technology; Particle size enlargement by C. E. Capes; Vol. 1 ; 1980; Elsevier. Preparation methods include known feed and granule formulation technologies, e.g.,

[0182] (a) Spray dried products, wherein a liquid enzyme-containing solution is atomized in a spray drying tower to form small droplets which during their way down the drying tower dry to form an enzyme-containing particulate material. Very small particles can be produced this way (Michael S. Showell (editor); Powdered detergents’, Surfactant Science Series; 1998; Vol. 71 ; pages 140-142; Marcel Dekker).

[0183] (b) Layered products, wherein the enzyme is coated as a layer around a pre-formed inert core particle, wherein an enzyme-containing solution is atomized, typically in a fluid bed apparatus wherein the pre-formed core particles are fluidized, and the enzyme-containing solution adheres to the core particles and dries up to leave a layer of dry enzyme on the surface of the core particle. Particles of a desired size can be obtained this way if a useful core particle of the desired size can be found. This type of product is described in, e.g., WO 97 / 23606.

[0184] (c) Absorbed core particles, wherein rather than coating the polypeptide as a layer around the core, the enzyme is absorbed onto and / or into the surface of the core. Such a process is described in WO 97 / 39116.

[0185] (d) Extrusion or pelletized products, wherein a polypeptide-containing paste is pressed to pellets or under pressure is extruded through a small opening and cut into particles which are subsequently dried. Such particles usually have a considerable size because of the material in which the extrusion opening is made (usually a plate with bore holes) sets a limit on the allowable pressure drop over the extrusion opening. Also, very high extrusion pressures when using a small opening increase heat generation in the enzyme paste, which is harmful to the enzyme (Michael S. Showell (editor); Powdered detergents’, Surfactant Science Series; 1998; Vol. 71 ; pages 140- 142; Marcel Dekker).

[0186] (e) Prilled products, wherein a polypeptide-containing powder is suspended in molten wax and the suspension is sprayed, e.g., through a rotating disk atomizer, into a cooling chamber where the droplets quickly solidify (Michael S. Showell (editor); Powdered detergents’, Surfactant Science Series; 1998; Vol. 71 ; pages 140-142; Marcel Dekker). The product obtained is one wherein the polypeptide is uniformly distributed throughout an inert material instead of being concentrated on its surface. US 4,016,040 and US 4,713,245 describe this technique.

[0187] (f) Mixer granulation products, wherein a polypeptide-containing liquid is added to a dry powder composition of conventional granulating components. The liquid and the powder in a suitable proportion are mixed and as the moisture of the liquid is absorbed in the dry powder, the components of the dry powder will start to adhere and agglomerate and particles will build up, forming granulates comprising the enzyme. Such a process is described in US 4,106,991 , EP 170360, EP 304332, EP 304331 , WO 90 / 09440 and WO 90 / 09428. In a particular aspect of this process, various high-shear mixers can be used as granulators. Granulates consisting of polypeptide, fillers and binders etc. are mixed with cellulose fibers to reinforce the particles to produce a so-called T-granulate. Reinforced particles, are more robust, and release less enzymatic dust.

[0188] (g) Size reduction, wherein the cores are produced by milling or crushing of larger particles, pellets, tablets, briquettes etc. containing the enzyme. The wanted core particle fraction is obtained by sieving the milled or crushed product. Over and undersized particles can be recycled. Size reduction is described in Martin Rhodes (editor); Principles of Powder Technology; 1990; Chapter 10; John Wiley & Sons.

[0189] (h) Fluid bed granulation. Fluid bed granulation involves suspending particulates in an air stream and spraying a liquid onto the fluidized particles via nozzles. Particles hit by spray droplets get wetted and become tacky. The tacky particles collide with other particles and adhere to them to form a granule.

[0190] (i) The cores may be subjected to drying, such as in a fluid bed drier. Other known methods for drying granules in the feed or enzyme industry can be used by the skilled person. The drying preferably takes place at a product temperature of from 25 to 90°C. For some enzymes, it is important the cores comprising the polypeptide contain a low amount of water before coating with the salt. If water sensitive enzymes are coated with a salt before excessive water is removed, the excessive water will be trapped within the core and may affect the activity of the enzyme negatively. After drying, the cores preferably contain 0.1-10% w / w water.

[0191] Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 and US 4,661 ,452 and may optionally be coated by methods known in the art.

[0192] The granulate may further comprise one or more additional enzymes. Each enzyme will then be present in more granules securing a more uniform distribution of the enzymes, and also reduces the physical segregation of different enzymes due to different particle sizes. Methods for producing multi-enzyme co-granulates is disclosed in the ip.com disclosure IPCOM000200739D. Another example of formulation of enzymes by the use of co-granulates is disclosed in WO 2013 / 188331.

[0193] In an embodiment, the granule further comprises one or more additional enzymes, e.g., hydrolase, isomerase, ligase, lyase, oxidoreductase, and transferase. The one or more additional enzymes are preferably selected from the group consisting of acetylxylan esterase, acylglycerol lipase, amylase, alpha-amylase, beta-amylase, arabinofuranosidase, cellobiohydrolases, cellulase, feruloyl esterase, galactanase, alpha-galactosidase, beta-galactosidase, beta- glucanase, beta-glucosidase, lysophospholipase, lysozyme, alpha-mannosidase, beta- mannosidase (mannanase), phytase, phospholipase A1 , phospholipase A2, phospholipase D, protease, pullulanase, pectin esterase, triacylglycerol lipase, xylanase, beta-xylosidase or any combination thereof. Liquid Formulations

[0194] The present invention also relates to liquid compositions comprising a biopolymer of the invention. The composition may comprise an enzyme stabilizer (examples of which include polyols such as propylene glycol or glycerol, sugar or sugar alcohol, lactic acid, reversible protease inhibitor, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid).

[0195] In some embodiments, filler(s) or carrier material(s) are included to increase the volume of such compositions. Suitable filler or carrier materials include, but are not limited to, various salts of sulfate, carbonate and silicate as well as talc, clay and the like. Suitable filler or carrier materials for liquid compositions include, but are not limited to, water or low molecular weight primary and secondary alcohols including polyols and diols. Examples of such alcohols include, but are not limited to, methanol, ethanol, propanol and isopropanol. In some embodiments, the compositions contain from about 5% to about 90% of such materials.

[0196] In an aspect, the liquid formulation comprises 20-80% w / w of polyol. In one embodiment, the liquid formulation comprises 0.001-2% w / w preservative.

[0197] In another embodiment, the invention relates to liquid formulations comprising:

[0198] (A) 0.001-25% w / w of an enzyme;

[0199] (B) 20-80% w / w of polyol;

[0200] (C) optionally 0.001-2% w / w preservative; and

[0201] (D) water.

[0202] In another embodiment, the invention relates to liquid formulations comprising:

[0203] (A) 0.001-25% w / w of a polypeptide of an enzyme;

[0204] (B) 0.001-2% w / w preservative;

[0205] (C) optionally 20-80% w / w of polyol; and

[0206] (D) water.

[0207] In another embodiment, the liquid formulation comprises one or more formulating agents, such as a formulating agent selected from the group consisting of polyol, sodium chloride, sodium benzoate, potassium sorbate, sodium sulfate, potassium sulfate, magnesium sulfate, sodium thiosulfate, calcium carbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol, lactose, starch, PVA, acetate and phosphate, preferably selected from the group consisting of sodium sulfate, dextrin, cellulose, sodium thiosulfate, kaolin and calcium carbonate. In one embodiment, the polyols is selected from the group consisting of glycerol, sorbitol, propylene glycol (MPG), ethylene glycol, diethylene glycol, triethylene glycol, 1 ,2-propylene glycol or 1 ,3-propylene glycol, dipropylene glycol, polyethylene glycol (PEG) having an average molecular weight below about 600 and polypropylene glycol (PPG) having an average molecular weight below about 600, more preferably selected from the group consisting of glycerol, sorbitol and propylene glycol (MPG) or any combination thereof. In another embodiment, the liquid formulation comprises 20-80% polyol ( / .e., total amount of polyol), e.g., 25-75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% polyol. In one embodiment, the liquid formulation comprises 20-80% polyol, e.g., 25-75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% polyol, wherein the polyol is selected from the group consisting of glycerol, sorbitol, propylene glycol (MPG), ethylene glycol, diethylene glycol, triethylene glycol, 1 ,2- propylene glycol or 1 ,3-propylene glycol, dipropylene glycol, polyethylene glycol (PEG) having an average molecular weight below about 600 and polypropylene glycol (PPG) having an average molecular weight below about 600. In one embodiment, the liquid formulation comprises 20-80% polyol ( / .e., total amount of polyol), e.g., 25-75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% polyol, wherein the polyol is selected from the group consisting of glycerol, sorbitol and propylene glycol (MPG).

[0208] In another embodiment, the preservative is selected from the group consisting of sodium sorbate, potassium sorbate, sodium benzoate and potassium benzoate or any combination thereof. In one embodiment, the liquid formulation comprises 0.02-1.5% w / w preservative, e.g., 0.05-1 % w / w preservative or 0.1 -0.5% w / w preservative. In one embodiment, the liquid formulation comprises 0.001-2% w / w preservative ( / .e., total amount of preservative), e.g., 0.02-1.5% w / w preservative, 0.05-1% w / w preservative, or 0.1 -0.5% w / w preservative, wherein the preservative is selected from the group consisting of sodium sorbate, potassium sorbate, sodium benzoate and potassium benzoate or any combination thereof.

[0209] In another embodiment, the liquid formulation further comprises one or more additional enzymes, e.g., hydrolase, isomerase, ligase, lyase, oxidoreductase, and transferase. The one or more additional enzymes are preferably selected from the group consisting of acetylxylan esterase, acylglycerol lipase, amylase, alpha-amylase, beta-amylase, arabinofuranosidase, cellobiohydrolases, cellulase, feruloyl esterase, galactanase, alpha-galactosidase, betagalactosidase, beta-glucanase, beta-glucosidase, lysophospholipase, lysozyme, alpha- mannosidase, beta-mannosidase (mannanase), phytase, phospholipase A1 , phospholipase A2, phospholipase D, protease, pullulanase, pectin esterase, triacylglycerol lipase, xylanase, beta- xylosidase or any combination thereof.

[0210] Detergent Ingredients

[0211] The choice of detergent components may include, for textile care, the consideration of the type of textile to be cleaned, the type and / or degree of soiling, the temperature at which cleaning is to take place, and the formulation of the detergent product. Although components mentioned below are categorized by general header according to a particular functionality, this is not to be construed as a limitation, as a component may comprise additional functionalities as will be appreciated by the skilled artisan.

[0212] Any detergent components known in the art for use in detergents may also be utilized. Other optional detergent components include anti-corrosion agents, anti-shrink agents, anti-soil redeposition agents, anti-wrinkling agents, bactericides, binders, corrosion inhibitors, disintegrants / disintegra- tion agents, dyes, enzyme stabilizers (including boric acid, borates, and / or polyols such as propylene glycol), fabric conditioners including clays, fillers / processing aids, fluorescent whitening agents / optical brighteners, foam boosters, foam (suds) regulators, perfumes, soil-suspending agents, softeners, suds suppressors, tarnish inhibitors, and wicking agents, either alone or in combination. Any ingredient known in the art for use in detergents may be utilized. The choice of such ingredients is well within the skill of the artisan and includes conventional ingredients, including the exemplary non-limiting components set forth below.

[0213] Surfactants

[0214] The cleaning composition may comprise one or more surfactants, which may be anionic and / or cationic and / or non-ionic and / or semi-polar and / or zwitterionic, or a mixture thereof. In a particular embodiment, the detergent composition includes a surfactant system (comprising more than one surfactant) e.g. a mixture of one or more nonionic surfactants and one or more anionic surfactants. In one embodiment the detergent comprises at least one anionic surfactant and at least one non-ionic surfactant, the weight ratio of anionic to nonionic surfactant may be from 20:1 to 1 :20. In one embodiment the amount of anionic surfactant is higher than the amount of non-ionic surfactant e.g. the weight ratio of anionic to non-ionic surfactant may be from 10:1 to 1.1 :1 or from 5:1 to 1.5:1. The amount of anionic to non-ionic surfactant may also be equal and the weight ratios 1 :1. In one embodiment the amount of non-ionic surfactant is higher than the amount of anionic surfactant and the weight ratio may be 1 : 10 to 1 : 1.1. Preferably the weight ratio of anionic to non-ionic surfactant is from 10: 1 to 1 : 10, such as from 5: 1 to 1 :5, or from 5: 1 to 1 : 1.2. Preferably, the weight fraction of non-ionic surfactant to anionic surfactant is from 0 to 0.5 or 0 to 0.2 thus non-ionic surfactant can be present or absent if the weight fraction is 0, but if non-ionic surfactant is present, then the weight fraction of the nonionic surfactant is preferably at most 50% or at most 20% of the total weight of anionic surfactant and non-ionic surfactant. Light duty detergent usually comprises more nonionic than anionic surfactant and there the fraction of non-ionic surfactant to anionic surfactant is preferably from 0.5 to 0.9. The total weight of surfactant(s) is typically present at a level of from about 0.1% to about 60% by weight, such as about 1% to about 40%, or about 3% to about 20%, or about 3% to about 10%. The surfactant(s) is chosen based on the desired cleaning application, and may include any conventional surfactant(s) known in the art. When included therein the detergent will usually contain from about 1% to about 40% by weight of an anionic surfactant, such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant. Non-limiting examples of anionic surfactants include sulfates and sulfonates, typically available as sodium or potassium salts or salts of monoethanolamine (MEA, 2- aminoethan-1-ol) or triethanolamine (TEA, 2,2',2"-nitrilotriethan-1-ol); in particular, linear alkylbenzenesulfonates (LAS), isomers of LAS such as branched alkylbenzenesulfonates (BABS) and phenylalkanesulfonates; olefin sulfonates, in particular alpha-olefinsulfonates (AOS); alkyl sulfates (AS), in particular fatty alcohol sulfates (FAS), i.e., primary alcohol sulfates (PAS) such as dodecyl sulfate (SLS); alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates); paraffin sulfonates (PS) including alkane-1 -sulfonates and secondary alkanesulfonates (SAS); ester sulfonates, including sulfonated fatty acid glycerol esters and alphasulfo fatty acid methyl esters (alpha-SFMe or SES or MES); alkyl- or alkenylsuccinic acids such as dodecenyl / tetradecenyl succinic acid (DTSA); diesters and monoesters of sulfosuccinic acid; fatty acid derivatives of amino acids. Anionic surfactants may be added as acids, as salts or as ethanolamine derivatives.

[0215] When included therein the detergent will usually contain from about 0, 1 % to about 40% by weight of a cationic surfactant, for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%. Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyl- distearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and combinations thereof.

[0216] When included therein the detergent will usually contain from about 0.2% to about 40% by weight of a nonionic surfactant, for example from about 0.5% to about 30%, in particular from about 1% to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%. Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO) e.g. the AEO-series such as AEO-7, alcohol propoxylates, in particular propoxylated fatty alcohols (PFA), ethoxylated and propoxylated alcohols, alkoxylated fatty acid alkyl esters, such as ethoxylated and / or propoxylated fatty acid alkyl esters (in particular methyl ester ethoxylates, MEE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof.

[0217] When included therein the detergent will usually contain from about 0.01 to about 10 % by weight of a semipolar surfactant. Non-limiting examples of semipolar surfactants include amine oxides (AO) such as alkyldimethylamine oxides, in particular N-(coco alkyl)-N,N-dimethylamine oxide and N-(tal- low-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, and combinations thereof.

[0218] When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a zwitterionic surfactant. Non-limiting examples of zwitterionic surfactants include betaines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.

[0219] Additional bio-based surfactants may be used e.g. wherein the surfactant is a sugar-based non-ionic surfactant which may be a hexyl-p-D-maltopyranoside, thiomaltopyranoside or a cyclic-maltopyra- noside, such as described in EP2516606 B1. Other biosurfactants may include rhamnolipids and sophorolipids.

[0220] Hydrotropes

[0221] A hydrotrope is a compound that solubilises hydrophobic compounds in aqueous solutions (or oppositely, polar substances in a non-polar environment). Typically, hydrotropes have both hydrophilic and a hydrophobic character (so-called amphiphilic properties as known from surfactants); however, the molecular structure of hydrotropes generally do not favor spontaneous selfaggregation, see e.g. review by Hodgdon and Kaier (2007), Current Opinion in Colloid & Interface Science 12: 121-128. Hydrotropes do not display a critical concentration above which self-aggregation occurs as found for surfactants and lipids forming miceller, lamellar or other well defined meso-phases. Instead, many hydrotropes show a continuous-type aggregation process where the sizes of aggregates grow as concentration increases. However, many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing substances of polar and non-polar character, including mixtures of water, oil, surfactants, and polymers. Hydrotropes are classically used across industries from pharma, personal care, food, to technical applications. Use of hydrotropes in detergent compositions allow for example more concentrated formulations of surfactants (as in the process of compacting liquid detergents by removing water) without inducing undesired phenomena such as phase separation or high viscosity.

[0222] The detergent may contain 0-10% by weight, for example 0-5% by weight, such as about 0.5 to about 5%, or about 3% to about 5%, of a hydrotrope. Any hydrotrope known in the art for use in detergents may be utilized. Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof.

[0223] Builders and Co-Builders

[0224] The detergent composition may contain about 0-65% by weight, such as about 5% to about 50% of a detergent builder or co-builder, or a mixture thereof. The builder and / or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and / or co- builder known in the art for use in cleaning detergents may be utilized.

[0225] Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP orSTPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Clariant), ethanolamines such as 2- aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2'-iminodiethan-1-ol), triethanolamine (TEA, also known as 2,2',2"-nitrilotriethan-1-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

[0226] The detergent composition may also contain from about 0-50% by weight, such as about 5% to about combination with a builder, for example a zeolite builder. Non-limiting examples of co-builders include or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid / maleic acid) (PAA / PMA). According to the present invention, these components can be included in lower levels than in currently available detergent compositions. Further non-limiting examples include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid. Additional specific examples include 2, 2’, 2”-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N’-disuccinic acid (EDDS), methyl glycinedi acetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1 ,1- diylbis(phosphonic acid (HEDP),ethylenediaminetetramethylenetetrakis(phosphonic acid) (EDTMPA),diethylenetriaminepentamethylenepentakis(phosphonic acid) (DTMPA or DTPMPA), N- (2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid- N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SEAS), N-(2-sulfomethyl)glu- tamic acid (SMGL), N-(2-sulfoethyl)glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), a-al- anine-N,N-diacetic acid (a-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N -di acetic acid (ANDA), sulfan- ilic acid-N,N -di acetic acid (SLDA) , taurine-N,N-diacetic acid (TLIDA) and sulfomethyl-N,N-diacetic acid (SMDA), N-(2-hydroxyethyl)ethylenediamine-N,N’,N”-triacetic acid (HEDTA), diethanolglycine (DEG), aminotrimethylenetris(phosphonic acid) (ATMP), and combinations and salts thereof. Further exemplary builders and / or co-builders are described in, e.g., WO 09 / 102854 and US 5977053.

[0227] Polymers and Dispersants

[0228] Generally, detergent compositions may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1 % of a polymer. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as mentioned above, or may provide anti-redeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and / or anti-foaming properties. Some polymers may have more than one of the above-mentioned properties and / or more than one of the below-mentioned motifs. Exemplary polymers include poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of polyethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine- / V-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (PVPVI). Further exemplary polymers include polyethylene oxide and polypropylene oxide (PEO-PPO), diquaternium ethoxy sulfate, styrene / acrylic copolymer and perfume capsules Other exemplary polymers are disclosed in, e.g., WO 2006 / 130575. Salts of the above-mentioned polymers are also contemplated.

[0229] The detergent compositions of the present invention can also contain dispersants. In particular powdered detergents may comprise dispersants. Suitable water-soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms. Suitable dispersants are for example described in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc.

[0230] Fabric Hueing Agents

[0231] The detergent compositions of the present invention may also include fabric hueing agents such as dyes or pigments, which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liguor comprising said detergent compositions and thus altering the tint of said fabric through absorption / reflection of visible light. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum. Suitable fabric hueing agents include dyes and dye-clay conjugates and may also include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.l.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in W02005 / 03274, W02005 / 03275, W02005 / 03276 and EP1876226 (hereby incorporated by reference). The detergent composition preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.0001 wt% to about 0.04 wt% fabric hueing agent. The composition may comprise from 0.0001 wt% to 0.2 wt% fabric hueing agent, this may be especially preferred when the composition is in the form of a unit dose pouch. Suitable hueing agents are also disclosed in, e.g. WO 2007 / 087257 and W02007 / 087243.

[0232] Dye Transfer Inhibiting Agents

[0233] The detergent compositions of the present invention may also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine / V-oxide polymers, copolymers of / V-vinylpyrrolidone and / V-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about 0.0001 % to about 10%, from about 0.01% to about 5% or even from about 0.1% to about 3% by weight of the composition.

[0234] Fluorescent Whitening Agent

[0235] The detergent compositions of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent or optical brighteners. Where present the brightener is preferably at a level of about 0.01 % to about 0.5%. Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention. The most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives. Examples of the diaminostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4'-bis-(2-diethanola- mino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(2,4-dianilino-s-triazin-6-yla- mino) stilbene-2.2'-disulfonate, 4,4'-bis-(2-anilino-4-( / V-methyl- / \ / -2-hydroxy-ethylamino)-s-triazin- 6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1 ,2,3-triazol-2-yl)stilbene-2,2'-disulfonate and sodium 5-(2 / 7-naphtho[1 ,2-d][1 ,2,3]triazol-2-yl)-2-[(E)-2-phenylvinyl]benzenesulfonate. Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of 4,4'-bis-(2-morpholino-4-anilino-s- triazin-6-ylamino) stilbene-2,2'-disulfonate. Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl- styryl)-disulfonate. Also preferred are fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India. Tinopal CBS-X is a 4.4'-bis-(sulfostyryl)-biphenyl disodium salt also known as Disodium Distyrylbiphenyl Disulfonate. Other fluorescers suitable for use in the invention include the 1 -3-diaryl pyrazolines and the 7-alkylaminocoumarins.

[0236] Suitable fluorescent brightener levels include lower levels of from about 0.01 , from 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt%.

[0237] Soil Release Polymers

[0238] The detergent compositions of the present invention may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics. The soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc. Another type of soil release polymers are amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure. The core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009 / 087523 (hereby incorporated by reference). Furthermore, random graft co-polymers are suitable soil release polymers. Suitable graft co-polymers are described in more detail in WO 2007 / 138054, WO 2006 / 108856 and WO 2006 / 113314 (hereby incorporated by reference).

[0239] Anti-redeposition Agents

[0240] The detergent compositions of the present invention may also include one or more anti-redepo- sition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyoxyethylene and / or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid. The cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents.

[0241] Rheology Modifiers

[0242] The detergent compositions of the present invention may also include one or more rheology modifiers, structurants or thickeners, as distinct from viscosity reducing agents. The rheology modifiers are selected from the group consisting of non-polymeric crystalline, hydroxy-functional materials, polymeric rheology modifiers which impart shear thinning characteristics to the aqueous liquid matrix of a liquid detergent composition. The rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example as shown in EP 2169040.

[0243] Other suitable adjunct materials include, but are not limited to, anti-shrink agents, anti-wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and / or structure elasticizing agents.

[0244] Enzymes

[0245] The detergent additive as well as the detergent composition may comprise one or more enzymes such as a protease, a lipase, a cutinase, a cellulase, an amylase, carbohydrase, DNase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and / or peroxidase.

[0246] In general, the properties of the selected enzyme(s) should be compatible with the selected detergent, ( / .e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.

[0247] Cellulases

[0248] The term “cellulase” means one or more (e.g., several) enzymes that hydrolyze a cellulosic material. The two terms polypeptide having cellulase activity and cellulase are used interchangeably. Cellulases may be selected from the group consisting of cellulases belonging to GH5, GH44, GH45, EC 3.2.1.4, EC 3.2.1.21 , EC 3.2.1.91 and EC 3.2.1.172. Such enzymes include endoglu- canase(s) (e.g. EC 3.2.1.4), cellobiohydrolase(s), beta-glucosidase(s), or combinations thereof.

[0249] Suitable cellulases include mono-component and mixtures of enzymes of bacterial or fungal origin. Chemically modified or protein engineered mutants are also contemplated. The cellulase may for example be a mono-component or a mixture of mono-component endo-1 ,4-beta-glu- canase also referred to as endoglucanase.

[0250] Suitable cellulases include those from the genera Bacillus, Pseudomonas, Humicola, Myceli- ophthora, Fusarium, Thielavia, Trichoderma, and Acremonium. Exemplary cellulases include a fungal cellulase from Humicola insolens (US 4,435,307) or from Trichoderma, e.g. T. reesei or T. viride. Other suitable cellulases are from Thielavia e.g. Thielavia terrestris as described inWO 96 / 29397 or the fungal cellulases produced from Myceliophthora thermophila and Fusarium ox- ysporum disclosed in US 5,648,263, US 5,691 ,178, US 5,776,757, WO 89 / 09259 and WO 91 / 17244. Also relevant are cellulases from Bacillus as described in WO 02 / 099091 and JP 2000210081. Suitable cellulases are alkaline or neutral cellulases having care benefits. Examples of cellulases are described in EP 0 495 257, EP 0 531 372, WO 96 / 11262, WO 96 / 29397, WO 98 / 08940. Other examples are cellulase variants such as those described in WO 94 / 07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95 / 24471 , WO 98 / 12307.

[0251] Other cellulases are endo-beta-1 ,4-glucanase enzyme having a sequence of at least 97% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO:2 of WO 2002 / 099091 or a family 44 xyloglucanase, which a xyloglucanase enzyme having a sequence of at least 60% identity to positions 40-559 of SEQ ID NO: 2 of WO 2001 / 062903.

[0252] Yet another group of suitable cellulases comprise a stabilized linker between the core and the CBM. Particularly useful are such cellulase having at least 80% identity to SEQ ID NO: 397, SEQ ID NO: 398 or SEQ ID NO: 399 of WO 2023 / 061928.

[0253] Commercially available cellulases include Carezyme®, Carezyme® Premium, Celluzyme®, Carezyme Elite®, Celluclean®, Celluclast®, Endolase®, Renozyme®; Whitezyme® Celluclean® Classic, Cellusoft® (Novozymes A / S), Puradax®, Puradax HA, and Puradax EG; Revitalenz 1000; Revitalenz 200; Revitalenz 2000 (Dupont Industrial Biosciences) , KAC-500(B)™ (Kao Corporation), Biotouch DCL; Biotouch FLX1 (AB enzymes).

[0254] The two basic approaches for measuring cellulolytic enzyme activity include: (1) measuring the total cellulolytic enzyme activity, and (2) measuring the individual cellulolytic enzyme activities (endoglucanases, cellobiohydrolases, and beta-glucosidases) as reviewed in Zhang et al., 2006, Biotechnology Advances 24: 452-481. Total cellulolytic enzyme activity can be measured using insoluble substrates, including Whatman N°1 filter paper, microcrystalline cellulose, bacterial cellulose, algal cellulose, cotton, pretreated lignocellulose, etc. The most common total cellulolytic activity assay is the filter paper assay using Whatman N°1 filter paper as the substrate. The assay was established by the International Union of Pure and Applied Chemistry (IUPAC) (Ghose, 1987, Pure Appl. Chem. 59: 257-68).

[0255] Nucleases (DNase, RNase)

[0256] The term “DNase” means a polypeptide with DNase activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, thus degrading DNA. Suitable nucleases include deoxyribonucleases (DNases) and ribonucleases (RNases) which are any enzyme that catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA or RNA backbone respectively, thus degrading DNA and RNA. There are two primary classifications based on the locus of activity. Exonucleases digest nucleic acids from the ends. Endonucleases act on regions in the middle of target molecules. The nuclease is preferably a DNase, which is preferable is obtainable from a microorganism, preferably a fungi or bacterium. In particular, a DNase which is obtainable from a species of Bacillus is preferred; in particular a DNase which is obtainable from Bacillus cibi, Bacillus subtilis or Bacillus licheniformis is preferred. Examples of such DNases are described in WO 2011 / 098579, WQ2014 / 087011 and WQ2017 / 060475. Particularly preferred is also a DNase obtainable from a species of Aspergillus; in particular a DNase which is obtainable from Aspergillus oryzae, such as a DNase described in WO 2015 / 155350.

[0257] Mannanases

[0258] Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. The mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens. Suitable mannanases are described in WO 1999 / 064619. A commercially available mannanase include Mannaway (Novozymes A / S) and Mannaway 200L (Novozymes A / S). Preferably, the mannanase is a GH5 mannanase (WO2018 / 206300, WO2018 / 206302, WO18185367, WO18184767, WO18220273, WO18220274, WO 2020207882, WO2021058452, WO17079751) or a GH26 mannanase (WO2019 / 068713, WO2019 / 068715, WO 2023 / 247348).

[0259] Proteases

[0260] Suitable proteases may be of any origin, but are preferably of bacterial or fungal origin, optionally in the form of protein engineered or chemically modified mutants. The protease may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as a subtilisin. A metalloprotease may for example be a thermolysin, e.g. from the M4 family, or another metalloprotease such as those from the M5, M7 or M8 families.

[0261] The term "subtilases" refers to a sub-group of serine proteases according to Siezen et al., Protein Eng. 4 (1991) 719-737 and Siezen et al., Protein Sci. 6 (1997) 501-523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate. The subtilases may be divided into six subdivisions, the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.

[0262] Although proteases suitable for detergent use may be obtained from a variety of organisms, including fungi such as Aspergillus, detergent proteases have generally been obtained from bacteria and in particular tromBacillus. Examples of Bacillus species from which subtilases have been derived include Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus and Bacillus gibsonii. Particular subtilisins include subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, subtilisin BPN’, subtilisin 309, subtilisin 147 and subtilisin 168 and e.g. protease PD138 (described in WO 93 / 18140). Other useful proteases are e.g. those described in WO 01 / 16285 and WO 02 / 16547.

[0263] Examples of trypsin-like proteases include the Fusarium protease described in WO 94 / 25583 and WO 2005 / 040372, and the chymotrypsin proteases derived from Cellumonas described in WO 2005 / 052161 and WO 2005 / 052146. Examples of metalloproteases include the neutral metalloproteases described in WO 2007 / 044993 such as those derived from Bacillus amyloliquefaciens, as well as e.g. the metalloproteases described in WO 2015 / 158723 and WO 2016 / 075078.

[0264] Examples of useful proteases are the protease variants described in WO 89 / 06279 WO 92 / 19729, WO 96 / 34946, WO 98 / 20115, WO 98 / 20116, WO 99 / 11768, WO 01 / 44452, WO 03 / 006602, WO 2004 / 003186, WO 2004 / 041979, WO 2007 / 006305, WO 2011 / 036263, WO 2014 / 207227, WO 2016 / 087617 and WO 2016 / 174234.

[0265] Suitable commercially available protease enzymes include those sold under the trade names Al- calase®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Pri- mase™, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Co- ronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Blaze Evity® 200T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® In and Progress® Excel (Novozymes A / S), those sold under the tradename Maxatase™, Maxacai™, Maxapem®, Pura- fect® Ox, Purafect® OxP, Puramax®, FN2™, FN3™, FN4ex™, Excellase®, Excellenz™ P1000, Excellenz™ P1250, Eraser™, Preferenz® P100, Purafect Prime, Preferenz P110™, Effectenz P1000™, Purafect®, Effectenz P1050™, Purafect® Ox, Effectenz ™ P2000, Purafast™, Properase®, Opticlean™ and Optimase® (Danisco / DuPont), BLAP (sequence shown in Figure 29 of US 5352604) and variants hereof (Henkel AG), and KAP (Bacillus alkalophilus subtilisin) from Kao.

[0266] Lipases and Cutinases

[0267] Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96 / 13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcali- genes (EP218272), P. cepacia (EP331376), P. sp. strain SD705 (W095 / 06720 & W096 / 27002), P. wisconsinensis (WO96 / 12012), GDSL-type Streptomyces lipases (W010 / 065455), cutinase from Magnaporthe grisea (WO10 / 107560), cutinase from Pseudomonas mendocina (US5,389,536), lipase from Thermobifida fusca (W011 / 084412), Geobacillus stearothermophilus lipase (W011 / 084417), lipase from Bacillus subtilis (W011 / 084599), and lipase from Streptomyces griseus (WO11 / 150157) and S. pristinaespiralis (WO12 / 137147).

[0268] Other examples are lipase variants such as those described in EP407225, WO92 / 05249, WO94 / 01541 , WO94 / 25578, WO95 / 14783, WO95 / 30744, WO95 / 35381 , WO95 / 22615,

[0269] W096 / 00292, W097 / 04079, W097 / 07202, WO00 / 34450, WO00 / 60063, W001 / 92502,

[0270] W007 / 87508 and WO09 / 109500.

[0271] Preferred commercial lipase products include include Lipolase 100T / L, Lipex 100T / L, Lipex 105T, Lipex Evity 100L, Lipex Evity 200L (all Novozymes A / S), Preferenz® L 100 (DuPont). Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10 / 111143), acyltransferase from Mycobacterium smegmatis (WO05 / 56782), perhydrolases from the CE 7 family (WO09 / 67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO10 / 100028).

[0272] Amylases

[0273] Suitable amylases include an alpha-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1 ,296,839.

[0274] Suitable amylases include amylases having SEQ ID NO: 2 in WO 95 / 10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94 / 02597, WO 94 / 18314, WO 97 / 43424 and SEQ ID NO: 4 of WO 99 / 019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 211 , 243, 264, 304, 305, 391 , 408, and 444.

[0275] Different suitable amylases include amylases having SEQ ID NO: 6 in WO 02 / 010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.

[0276] Other amylases which are suitable are hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006 / 066594 or variants having 90% sequence identity thereof.

[0277] Other examples are amylase variants such as those described in WO2011 / 098531 , WO2013 / 001078 and WO2013 / 001087.

[0278] Commercially available amylases are Duramyl™, Termamyl™, Fungamyl™, StainzymeTM, Stainzyme Plus™, Natalase™, Liquozyme X and BAN™ Amplify; Amplify Prime; (from Novo- zymes A / S), and Rapidase™ , Purastar™ / Effectenz™, Powerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Genencor International Inc. / DuPont).

[0279] Peroxidases / Oxidases

[0280] Suitable peroxidases / oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257. Commercially available peroxidases include Guar- dzyme™ (Novozymes A / S).

[0281] A suitable peroxidase is preferably a peroxidase enzyme comprised by the enzyme classification EC 1.11.1.7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom, exhibiting peroxidase activity. Suitable peroxidases also include a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.11.1.10) catalyze formation of hypochlorite from chloride ions. The haloperoxidase may be a chloroperoxidase. Preferably, the haloperoxidase is a vanadium haloperoxidase, i.e., a van- adate-containing haloperoxidase. In a preferred method the vanadate-containing haloperoxidase is combined with a source of chloride ion.

[0282] Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.

[0283] Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.

[0284] The haloperoxidase may be derivable from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95 / 27046; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97 / 04102; or from Drechslera hartlebii as described in WO 01 / 79459, Dendryphiella salina as described in WO 01 / 79458, Phaeotrichoconis crotalarie as described in WO 01 / 79461 , or Geniculosporium sp. as described in WO 01 / 79460.

[0285] Suitable oxidases include, in particular, any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1), an o-aminophenol oxidase (EC 1.10.3.4), or a bilirubin oxidase (EC 1.3.3.5).

[0286] Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts).

[0287] Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Pomes, Lentinus, Pleurotus, Trametes, e.g., T. vil- losa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinopsis, e.g., C. cinerea, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P. papilionaceus, My- celiophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (\NO 92 / 01046), or Coriolus, e.g., C. hirsutus (JP 2238885).

[0288] Suitable examples from bacteria include a laccase derivable from a strain of Bacillus. A laccase derived from Coprinopsis or Myceliophthora is preferred; in particular a laccase derived from Coprinopsis cinerea, as disclosed in WO 97 / 08325; or from Myceliophthora thermophila, as disclosed in WO 95 / 33836.

[0289] Licheninases

[0290] Licheninases (or lichenases) (e.g. EC 3.2.1.73) hydrolyse (1 ,4)-beta-D-glucosidic linkages in beta-D-glucans containing (1 ,3)- and (1 ,4)-bonds and can act on lichenin and cereal beta-D-glu- cans, but not on beta-D-glucans containing only 1 ,3- or 1 ,4-bonds.

[0291] Pectate Lyases

[0292] Pectate lyases catalyze the cleavage of a-1 ,4-D-galacturonan (i.e., homogalacturonan or polyga- lacturonic acid) by an eliminative pathway leaving a double bond between C4 and C5 at the +1 subsite and a reducing sugar at the -1 subsite. Pectate lyases may also have pectin lyase activity.

[0293] Formulation of Detergent Products

[0294] The detergent composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, a sheet, or a regular, compact or concentrated liquid. Pouches can be configured as single or multicompartments. It can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing the release of the composition to release of the composition from the pouch prior to water contact. The pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch. Preferred films are polymeric materials preferably polymers which are formed into a film or sheet. Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water-soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC). Preferably the level of polymer in the film for example PVA is at least about 60%. Preferred average molecular weight will typically be about 20,000 to about 150,000. Films can also be of blended compositions comprising hydrolytically degradable and water soluble polymer blends such as polylactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by MonoSol LLC, Indiana, USA) plus plasticisers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof. The pouches can comprise a solid laundry cleaning composition or part components and / or a liquid cleaning composition or part components separated by the water-soluble film. The compartment for liquid components can be different in composition than compartments containing solids: US2009 / 0011970 A1.

[0295] Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution.

[0296] A liquid or gel detergent, which is not unit dosed, may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water. Other types of liquids, including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel. An aqueous liquid or gel detergent may contain from 0-30% organic solvent. A liquid or gel detergent may be non-aqueous.

[0297] PREFERRED EMBODIMENTS

[0298] The invention is further summarized in the following embodiments:

[0299] 1 . A biopolymer characterised in that a. The biopolymer consists of carbohydrate monomers selected from the group consisting of glucose, mannose, rhamnose, galactose, fructose, xylose and arabinose or a mixture thereof; and b. The carbohydrate monomers of the biopolymer are linked via alpha-1 ,2, alpha-1 ,3, alpha-1 ,4, alpha-1 ,6, beta-1 ,2, beta-1 ,3, beta-1 ,4, beta-1 ,6, or beta-2,1 glycosidic linkage or a combination thereof; and c. The degree of polymerization (DP) of the biopolymer is in the range 5-100, such as 5- 75, 5-50 or 5-25 or 5-10; and d. The biopolymer optionally is substituted.

[0300] 2. The biopolymer of embodiment 1 , wherein the biopolymer comprises a. at least two glucose monomers linked via alpha-1 ,2, beta-1 ,2, beta-1 ,3, beta-1 ,6, or beta-2,1 glycosidic linkage; b. at least two mannose monomers linked via alpha-1 ,3, alpha-1 ,4, alpha-1 ,6, beta-1 ,2, beta-1 ,6, or beta-2,1 glycosidic linkage; c. at least two rhamnose monomers linked via alpha-1 ,2, glycosidic linkage; and / or d. at least two galactose monomers linked via alpha-1 ,6, beta-1 ,3, beta-1 ,4, or beta-1 ,6 glycosidic linkage; and / or e. at least two fructose monomers linked via alpha-1 ,2, beta-1 ,2, or beta-2, 1 glycosidic linkage; and / or f. at least two xylose monomers linked via beta-1 ,3, or beta-1 ,4 glycosidic linkage; and / or g. at least two arabinose monomers linked via beta-1 ,3 glycosidic linkage; or a mixture or any of the glycosidic linkages of a. to g.

[0301] 3. The biopolymer of embodiments 1 or 2, wherein the biopolymer is a homopolysaccharide. 4. The biopolymer of embodiments 1 or 2, wherein the biopolymer is a heteropolysaccharide comprising two or three different carbohydrate monomers.

[0302] 5. The biopolymer of any of embodiments 1 to 4, wherein the biopolymer is branched or linear.

[0303] 6. The biopolymer of any of embodiments 1 to 5, wherein the biopolymer is substituted with one or more substitutents, such as but not limited to the substituent selected from the group consisting of carboxy methyl, benzoylmethyl, acrylic / maleic acid copolymer, polyacrylate, PEG, PPG; sulfated PEG, polyvinylacetate, polyester, polyethylene terephthalate, styrene, methacrylate and styrene copolymers, or combinations of any of the substitutents.

[0304] 7. The biopolymer of embodiment 6, wherein the biopolymer is an amphiphilic derivative.

[0305] 8. The biopolymer of embodiment 6 or 7, wherein the degree of substitution [DS] is from about 0.1 to about 3.0, such as from about 0.1 to about 2.0, such as from about 0.1 to about 1.0, such as from about 0.1 to about 0.5 such as from about 0.1 to about 0.25.

[0306] 9. A process for producing the biopolymer of any of embodiments 1 to 5, wherein the biopolymer is unsubstituted, wherein the process comprises the steps a. Dissolving the one or more carbohydrate monomers in a solvent; b. Adding an enzyme selected from the group consisting of inulinase, betagalactosidase, glycosyltransferase, fructosyltransferase to the solvent to obtain the unsubstituted biopolymer.

[0307] 10. A process for producing the biopolymer of any of embodiments 1 to 8, wherein the biopolymer is substituted, wherein the process comprises the steps a. Dissolving the one or more carbohydrate monomers in a solvent; b. Adding an enzyme selected from the group consisting of alternan sucrase, inulinase, betagalactosidase, glycosyltransferase, fructosyltransferase to the solvent to obtain the unsubstituted biopolymer; c. Reacting the unsubstituted biopolymer obtained in step b. above with a substituent to obtain the substituted biopolymer.

[0308] 11 . The process according to any of embodiment 9 or 10, wherein the solvent is essentially water-free.

[0309] 12. The process according to any of embodiments 9 to 11 , wherein the enzyme has at least 80%, such as 85%, 90%, 95%, 96%, 97%, 98%, 99% or even 100% sequence identity to the mature part of any of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4

[0310] 13. A detergent composition comprising a biopolymer of embodiments 1-8. 14. The detergent composition of embodiment 13 comprising one or more enzymes selected from the group consisting of amylases, proteases, peroxidases, betaglucanases, xyloglu- canases, hemicellulases, xanthan lyases, lipases, pectate lyases, lipoxygenases, endo-beta- mannanases, exo-beta-mannanases, and cellobiohydrolases.

[0311] 15. Use of the composition of embodiment 13 or 14 for cleaning of an item, such as a hard surface or a textile.

[0312] 16. A method for laundering a textile comprising the steps of: a. Exposing an item to a wash liquor comprising a composition, preferably a detergent composition such as the detergent composition of embodiments 13 or 14, comprising the biopolymer of the present invention b. Completing at least one wash cycle; and c. Optionally rinsing the item.

[0313] 17. The biopolymer of any of embodiments 1 to 8, wherein the biopolymer is selected from the group consisting of a. A biopolymer (BP1a) with antiredeposition benefits: Polysaccharide with 1 glucose and 20 galactose units linked beta-1 ,3. Degree of substitution of 2 with Carboxymethyl b. A biopolymer (BP1b) with antiredeposition benefits: Polysaccharide with 1 glucose and 5 galactose units linked beta-1 ,3. Degree of substitution of 1 ,5 with polyacrylic / maleic acid copolymer. Degree of functionalization (DF) 0.80 c. A biopolymer (BP1c) with antiredeposition benefits: Polysaccharide with 1 glucose and 20 galactose units linked beta-1 ,3. Degree of substitution of 2 with benzoylmethyl d. A biopolymer (BP2) with soil release benefits: Polysaccharide with 1 glucose units linked beta-2, 1. Degree of substitution of 1 ,5 with polyethylene and polyethylene terephthalate co-polymers. Degree of functionalization (DF) 0.80 e. A biopolymer (BP3) with dye transfer inhibitor benefits: Polysaccharide with 1 glucose and 10 galactose units linked beta-1 ,3. Degree of substitution of 1 ,5 with polyvinylpyrrolidone. Degree of functionalization 0.80 f. A biopolymer (BP4a) with cleaning polymer benefits: Polysaccharide with 20 glucose units linked alpha 1 ,6. Degree of substitution of 1 ,5 with polyethylene glycol. Degree of functionalization (DF) 0.80 g. A biopolymer (BP4b) with cleaning polymer benefits: Polysaccharide with 1 glucose and 5 galactose units linked beta-1 ,3. Degree of substitution of 1 ,8 with polyethylene glycol. Degree of functionalization (DF) 0.80 h. A biopolymer (BP5) with opacifier benefits: Polysaccharide with 1 glucose and 5 galactose units linked beta-1 ,3. Degree of substitution of 1 ,8 with styrene / methacrylate. Degree of functionalization (DF) 0.80.

[0314] EXAMPLES Examples of biopolymers of the invention:

[0315] Materials and Methods

[0316] Test swatches for wash performance assay to evaluate the relevant parameter, e.g. whitheness, anti-redeposition or colour maintenance (anti-graying), may be obtained from CFT, Vlaardingen,

[0317] The Netherlands. Specific test swatches indicated in each test prototcol.

[0318] The compositioin of a liquid model detergent is disclosed in the tables below.

[0319] Detergent A (w / w%) Detergent dose in Full Scale Wash (FSW) is 2.2 g / L.

[0320] Commercial raw materials are used and dosage of raw material is adjusted wilth the purity of the individual ingredients to achieve the listed active content.

[0321] Calculating the biopolymer effect is done by taking the measurements from washed swatches with biopolymer and subtract with the measurements from washed without biopolymer for each stain. The total biopolymer performance is calculated as the average of individual ARem.

[0322] Detergent H (w / w%)

[0323] Detergent I (w / w%)

[0324] Detergent J (w / w%)

[0325] Wash assays

[0326] Standard EU washing conditions (Full Scale Wash, FSW) Terq-O-tometer (TOM) wash assay

[0327] The Tergo-To-Meter (TOM) is a medium scale model wash system that can be applied to test 16 different wash conditions simultaneously. A TOM is basically a large temperature-controlled water bath with up to 16 open metal beakers submerged into it. Each beaker constitutes one small top loader style washing machine and during an experiment, each of them will contain a solution of a specific detergent / enzyme / polymer system and the soiled and unsoiled fabrics its performance is tested on. Mechanical stress is achieved by a rotating stirring arm, which stirs the liquid within each beaker.

[0328] The TOM model wash system is mainly used in medium scale testing of detergents, enzymes and polymers at Ell or AP wash conditions. In a TOM experiment, factors such as the ballast to soil ratio and the fabric to wash liquor ratio can be varied. Therefore, the TOM provides the link between small scale experiments, and the more time-consuming full-scale experiments.

[0329] Equipment: A water bath with 16 steel beakers and 1 rotating arm per beaker with capacity of 1 L detergent solution. Temperature ranges from 5°C to 80°C. The water bath has to be filled up with deionised water. Rotational speed can be set up to 70 to 120rpm / min.

[0330] Set temperature in the Terg-O-Tometer and start the rotation in the water bath. Wait for the temperature to adjust (tolerance is + / - 0,5°C). All beakers shall be clean and without traces of prior test material.

[0331] The wash solution with desired amount of detergent, temperature and water hardness is prepared in a bucket. The detergent is allowed to dissolve during magnet stirring for 10 min. Wash solution shall be used within 30 to 60 min after preparation.

[0332] 1 L wash solution is added into a TOM beaker. The wash solution is agitated at 120rpm and optionally one or more enzymes or polymers are added to the beaker. The swatches are sprinkled into the beaker and then the ballast load. Time measurement starts when the swatches and ballast are added to the beaker. The swatches are washed for 20 or 30 minutes after which agitation is terminated.

[0333] The wash load is subsequently transferred from the TOM beaker to a sieve and rinse with cold tap water. The soil swatches are separated from the ballast load. The soil swatches are transferred to a 5L beaker with cold tap water under running water for 5 minutes. The ballast load is kept separately for the coming inactivation. The water is gently pressed out of the swatches by hand and placed on a tray covered with a paper. The swatches are allowed to dry overnight before subjecting the swatches to analysis, such as measuring the delta REM.

[0334] Test 1 : Antiredeposition Carbon black, TOM.

[0335] TOM, 40°C, 120 rpm, 1 L, 15dH (4:1), 0.1 g / L Carbon Black, 60 minutes, 2 / 3 SBL 2004 sheet, 2 wash cycles. Measurement: Remission 460nm (Datacolor), Y, Wl (CIE), before and after wash.

[0336] Test 2: Stainremoval and Whiteness full scale wash (FSW), standard A.I.S.E. whiteness.

[0337] FSW whiteness test, min 6 cycles for whiteness, 1 cycle stainremoval. 40°C, 3kg ballast.

[0338] Soil: 4 SBL 2004 sheets. Stains in A.I.S.E v07 2020 stainset.

[0339] White tracers: cotton, polyester / cotton; polyester and polyamide.

[0340] Evaluation: stain removal: he evaluation of the degree of stain removal can either be assessed via suitable instrumental measurements such as reflectance (Y-value, SRI) or image analysis, as long as these methods are fully validated. Basic whiteness: as Y-value and Visual whiteness simulated as Ganz-Griesser value on 4 standard fabrics (cotton, polyester / cotton, polyester and polyamide) after 6 (8) cumulative washes.

[0341] Test 3: Whiteness full scale wash (FSW), whiteness tracers, Clay and increased soil, multiwashes Standard Ell washing conditions (FSW), 40°C cotton short, 6 repetive cycles.

[0342] Soil: 8xSBL2004 sheets (W-SBL 2004, Soil Ballast Load Fabric purchased from CFT (Center for Testmaterials BV). and red clay powder (garden soil purchased from China horticultural market, 50 mesh sieve filtrated before use), 2g / L.

[0343] White tracer list used for Test 3 (table A)

[0344] CFT is abbreviation for “Center for Testmaterials BV”

[0345] Tracers are grouped in three categories for summarization of results:

[0346] Natural textile: W-10 A; W-12 A; W-80 A; C-N-11 ; C-N-42; T-266; T-266 with pre-aged treatment Semisynthetic textile: P-CN-01 ; W-20 A

[0347] Synthetic textile: T-720; P-N-01; W-30 A; W-40 A; T-340 Nylon / Lycra 81 / 19

[0348] Test 4: Full scale wash (FSW) assay for whiteness on real items (used items)

[0349] Standard Ell washing conditions (FSW), 40°C cotton short, 1 cycle followed by a “soil rinse” cycle as described in table B. Table B:

[0350] White tracer list: as in test 3, table A.

[0351] Real item list: table C The wash procedure instructions below are applied: a. same procedure as in Test 3 a. After the wash is completed, remove the ballast and leave the real item pieces in wash machine. b. Add 7.5g Detergent H and 7.5 g pigment soil into 1 L hard water (14dH as it is in main wash), and stir for 10 min. c. Select parameters for soil rinse: Program and Water level. d. Add in Model O- pigment soil solution through detergent tank after water is intaken automatically. Rinse the beaker with hard water for several times and add rinse water into washing machine. e. After the wash is completed, the test swatches are removed from the tea towels and placed on trays for drying. Test 5: Soil release, prewash and soiling

[0352] Fabric swatches (JoAnn’s Fabric Symphony Broadcloth: 65% polyester: 35% cotton) are scoured in 400 ppm nonionic surfactant prior to use. The fabric is cut to 4"X4" and 3 swatches are used per test. The swatches are dipped in 100 ppm of aqueous solution benzyl-carboxymethyl glucan, wrung to a consistent liquid mass, and laid flat to air dry. Vegetable oil dyed with solvent red 27 is used to soil each swatch (approximately 0.13 g of soil is applied to each swatch). The swatches are dried overnight before washing. Wash conditions: 1 L tap water, 60 ppm hardness. 80 rpm agitation, 38 °C wash temperature, 10 minute wash with 3 minute rinse. Detergent used: Arms & Hammer Clean Burst 0.68g / L; addition order: water, detergent, cloth. The swatches are wrung to consistent mass before and after rinse cycle and air dried. The reflectance readings (x, y, z color space) are taken in quadruplicate for each swatch using a Hunter colorimeter both after soiling and after washing. The y values are used to determine cleaning efficacy. The differences between the two values are reported (Delta R, the larger value indicates more soil removal)

[0353] Test 6: Dye transfer

[0354] According to the A. I. S. E. v.7 October 2020 testing guidelines for detergents, test execution Dye transfer: Equipment: linitester, Color donator (direct orange 39; direct black 22, Acid blue 113, Direct Red 83.1), tracer acceptor (cotton and polyamide), 60°C, 30minutes, 100ml watervolume. Evaluation of color difference delta E, as gray scale units (ISO 105 A 04).

[0355] Test 7: opacify (turbidity).

[0356] T urbidity is defined as the cloudiness or haziness of a fluid, such as a detergent. Turbidity or haze (or haziness) is scattering of light by a medium, which results into cloudy appearance, and poorer clarity of objects when viewing through that. Turbidity is measured in NTU (Nephelometric Turbidity Units) using a TB300-IR Turbidimeter (Orbeco-Hellige, Sarasota, Florida) calibrated between 0 and 800 NTU.

[0357] The biopolymer is added to a clear detergent on (less than 25 Nephelometric Turbidity Units (NTU) at room temperature) and after stirring for 1 hour at room temperature and allowing bubbles to settle for 3 hours, then turbidity is measured and if <25 NTU its considered clear.

Claims

CLAIMS1. A biopolymer characterised in that a. The biopolymer consists of carbohydrate monomers selected from the group consisting of glucose, mannose, rhamnose, galactose, fructose, xylose and arabinose; and b. The carbohydrate monomers of the biopolymer are linked via alpha-1 ,2, alpha-1 ,3, alpha-1 ,4, alpha-1 ,6, beta-1 ,2, beta-1 ,3, beta-1 ,4, beta-1,6, or beta-2,1 glycosidic linkage or a combination thereof; and c. The degree of polymerization (DP) of the biopolymer is in the range 5-100.

2. The biopolymer of claim 1 , wherein the biopolymer comprises a. at least two glucose monomers linked via alpha-1 ,2, beta-1 ,2, beta-1 ,3, beta-1 ,6, or beta-2,1 glycosidic linkage; b. at least two mannose monomers linked via alpha-1 ,3, alpha-1 ,4, alpha-1 ,6, beta-1 ,2, beta-1,6, or beta-2,1 glycosidic linkage; c. at least two rhamnose monomers linked via alpha-1 ,2, glycosidic linkage; and / or d. at least two galactose monomers linked via alpha-1 ,6, beta-1 ,3, beta-1 ,4, or beta-1 ,6 glycosidic linkage; and / or e. at least two fructose monomers linked via alpha-1 ,2, beta-1 ,2, or beta-2, 1 glycosidic linkage; and / or f. at least two xylose monomers linked via beta-1 ,3, or beta-1 ,4 glycosidic linkage; and / or g. at least two arabinose monomers linked via beta-1 ,3 glycosidic linkage; or a mixture or any of the glycosidic linkages of a. to g.

3. The biopolymer of claims 1 or 2, wherein the biopolymer is a homopolysaccharide.

4. The biopolymer of claims 1 or 2, wherein the biopolymer is a heteropolysaccharide comprising two or three different carbohydrate monomers.

5. The biopolymer of any of claims 1 to 4, wherein the biopolymer is branched or linear.

6. The biopolymer of any of claims 1 to 5, wherein the biopolymer is substituted.

7. The biopolymer of claim 6, wherein the biopolymer is an amphiphilic derivative.

8. The biopolymer of any of claims 6 or 7, wherein the degree of substitution is from about 0.1 to about 3.0.

9. The biopolymer of any of claims 6 to 8, wherein the substituent is selected from the group consisting of carboxymethyl, benzoylmethyl, acrylic / maleic acid copolymer, polyacrylate, PEG,PPG; sulfated PEG, polyvinylacetate, polyester, polyethylene terephthalate, styrene, methacrylate and styrene copolymers, or combinations of any of the substitutents.

10. A process for producing the biopolymer of any of claims 1 to 9, wherein the process comprises the steps a. Dissolving the one or more mono-, di- or oligosaccharides in a solvent; b. Adding an enzyme selected from the group consisting of inulinase, betagalactosidase, glycosyltransferase, fructosyltransferase to the solvent to obtain the unsubstituted biopolymer; c. Optionally reacting the unsubstituted biopolymer obtained in step b. above with a substituent to obtain the substituted biopolymer.11 . The process according to claim 10, wherein the solvent is essentially water-free.

12. A detergent composition comprising a biopolymer of claims 1-9 and one or more enzymes such as proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidases, haloperoxygenases, phosphodiesterases, dispersin, catalases or mannanases, or any mixture thereof13. Use of the composition of claim 12 for cleaning of an item, such as a hard surface or a textile.

14. Use of the biopolymer of any of claims 1 to 9 for the improvement of the sustainability profile of a detergent.

15. A method for laundering a textile comprising the steps of: a. Exposing a textile to a wash liquor comprising a detergent composition, wherein said detergent composition comprises the biopolymer of any of claims 1 to 9, b. Completing at least one wash cycle; and c. Optionally rinsing the item.

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