Mannanases for sustainable cleaning

Abstract

In the present invention a liquid cleaning composition comprising a mannanase, at least one biodegradable surfactant and at least one biodegradable complexing agent is provided. Additionally, washing or cleaning methods using a liquid cleaning composition comprising a mannanase are provided. More specifically, the provided methods for washing or cleaning comprise a washing or cleaning step of 5-60 min.

Description

[0001] Mannanases for sustainable cleaning

[0002] Field of the invention

[0003] In the present invention a liquid cleaning composition comprising a mannanase, at least one biodegradable surfactant and at least one biodegradable complexing agent is provided. Additionally, washing or cleaning methods using a liquid cleaning composition comprising a mannanase are provided. More specifically, the provided methods for washing or cleaning comprise a washing or cleaning step of 5-60 min.

[0004] Background of the invention

[0005] Enzymes are biodegradable and therefore increasingly used in various applications as sustainable alternative to petrochemistry. In the cleaning industry, particularly in the detergent industry, enzymes are incorporated in cleaning compositions to improve cleaning efficiency and to reduce the use of harsh chemicals.

[0006] Endo-1 ,4-beta-mannanases (EC 3.2.1.78) are mannan-degrading enzymes. They are also called mannanases, endo-|3-1 ,4-D-mannanases, or p-mannanases herein.

[0007] Mannanases are enzymes capable of degrading mannans by hydrolysis of the internal glycoside bonds in the mannan backbone. Since mannanases degrade the mannan backbone, they are capable of degrading mannans, galactomannans and / or glucomannans.

[0008] Mannanases are therefore widely used in different industries. For example, in the detergent industry, they are deployed for the effective removal of mannan-comprising stains, e.g. containing guar or locust bean gums, glucomannans, and galactomannans.

[0009] An enzymes performance in removing stains depends on external conditions such as e.g. the presence of other detergent components such as surfactants and complexing agents, the washing temperature or the washing time. Generally, in the cleaning industry and especially in the detergent industry, there is a need to develop more sustainable washing and cleaning processes.

[0010] Ways to improve the sustainability profile of a washing process include the use of more sustainable detergent components, the use of less detergent overall, and the reduction of its energy consumption, which can be achieved by e.g. reducing the washing time or temperature.

[0011] Thus, the need exists to identify detergent components such as enzymes, e.g. mannanases, that perform well under more sustainable conditions such as in more sustainable cleaning compositions, in short wash cycles and at low temperature.

[0012] Brief summary of the invention

[0013] Thus, the present invention is directed to mannanases that show a superior performance under sustainable wash conditions and therewith promote a more sustainable washing process.

[0014] More specifically, a liquid cleaning composition comprising at least one mannanase, at least one biodegradable surfactant, and at least one biodegradable complexing agent is provided, wherein the mannanase is at least 65% but less than 100% identical to SEQ ID NO: 1 , or wherein the mannanase is at least 65% identical to SEQ ID NO: 2, or 3. Additionally, methods of washing or cleaning having an improved sustainability profile using a liquid cleaning composition comprising a mannanase, wherein the mannanase is at least 65% but less than 100% identical to SEQ ID NO: 1 , or wherein the mannanase is at least 65% identical to SEQ ID NO: 2, or 3, are provided. More specifically, the provided methods give superior cleaning results in short wash cycles, at low temperature, and / or when using low detergent dosage.

[0015] Detailed description of the invention

[0016] The present invention may be understood more readily by reference to the following detailed description of the embodiments of the invention and the examples included herein.

[0017] Although the present invention will be described with respect to particular embodiments, this description is not to be construed in a limiting sense.

[0018] Definitions

[0019] Unless otherwise noted, the terms used herein are to be understood according to conventional usage by those of ordinary skill in the relevant art.

[0020] Before describing exemplary embodiments of the present invention in detail, definitions important for understanding the present invention are provided. Unless stated otherwise or apparent from the nature of the definition, the definitions apply to all compounds, methods and uses described herein.

[0021] As used in this specification and in the appended claims, the singular forms of "a" and "an" also include the respective plurals and vice versa unless the context clearly dictates otherwise.

[0022] In the context of the present invention, the terms "about" and "approximately" denote an interval of accuracy that a person skilled in the art will understand to still ensure the technical effect of the feature in question. The term typically indicates a deviation from the indicated numerical value of ± 20%, preferably ± 15%, more preferably ± 10%, and even more preferably ± 5%.

[0023] Furthermore, the terms "first", "second", "third" or "(a)", "(b)", "(c)", "(d)" etc. in the description and in the claims, are used for distinguishing between elements and not necessarily for describing a sequential or chronological order. It is to be understood that the terms so used are interchangeable under appropriate circumstances and that the embodiments of the invention described herein are capable of operation in other sequences than described or illustrated herein. In case the terms "first", "second", "third" or "(a)", "(b)", "(c)", "(d)", "i", "ii" etc. relate to steps of a method or use or assay, there is no time or time interval coherence between the steps, i.e. the steps may be carried out simultaneously or there may be time intervals of seconds, minutes, hours, days, weeks, months or even years between such steps, unless otherwise indicated in the application as set forth herein above or below.

[0024] Throughout this application, various publications are referenced. The disclosures of all these publications and the references cited within those publications in their entireties are hereby incorporated by reference into this application to describe the state of the art to which this invention pertains more fully.

[0025] It is to be understood that the term "comprising" is not limiting. For the purposes of the present invention the term "consisting of" is considered to be a preferred embodiment of the term "comprising". If hereinafter a group is defined to comprise at least a certain number of members, this is meant to also encompass a group which consists of these members only.

[0026] “Variant” enzymes differ from “parent” enzymes by certain amino acid alterations, preferably amino acid substitutions at one or more amino acid positions.

[0027] In describing the polypeptides and variants of the present invention, the abbreviations for single amino acids used are according to the accepted IUPAC single letter or three letter amino acid abbreviation.

[0028] “Amino acid alteration” as used herein refers to amino acid substitution, deletion, or insertion.

[0029] “Substitutions” are described by providing the original amino acid followed by the number of the position within the amino acid sequence followed by the amino acid, which substitutes the original amino acid. For example, the substitution of histidine at position 120 with alanine is designated as “His120Ala” or “H120A”. Substitutions can also be described by merely naming the resulting amino acid without specifying the initial amino acid at this position, e.g., “X120A” or“120A” or“Xaa120Ala” or“120Ala”. Positions of substitutions can be described by merely providing the number of the position within the amino acid sequence.

[0030] “Deletions” are described by providing the original amino acid followed by the number of the position within the amino acid sequence followed by *. Accordingly, the deletion of glycine at position 150 is designated as “Gly150*” or “G150*”. Alternatively, deletions are indicated by, e.g., “deletion of D183 and G184”.

[0031] “Insertions” are described by providing the original amino acid followed by the number of the position within the amino acid sequence followed by the original amino acid and the additional amino acid. For example, an insertion at position 180 of lysine next to glycine is designated as “Gly180GlyLys” or “G180GK”. When more than one amino acid residue is inserted, such as, e.g., a Lys and an Ala after Gly 180 this may be indicated as: “Gly180GlyLysAla” or “G195GKA”.

[0032] In cases where a substitution and an insertion occur at the same position, this may be indicated as “S99A+S99SD” or in short “S99AD”. Sequences comprising multiple alterations are separated by “+”, e.g., “Arg170Tyr+Gly 195Glu” , “R170Y+G195E” or “X170Y+X195E” representing a substitution of arginine and glycine at positions 170 and 195 with tyrosine and glutamic acid, respectively. Alternatively, multiple alterations may be separated by space or a comma, e.g., “R170Y G195E” or “R170Y, G195E” respectively. Where different alternative alterations can be introduced at a position, the different alterations are separated by a comma, e.g., “Arg170Tyr, Glu” and “R170T, E”, respectively, represents a substitution of arginine at position 170 with tyrosine or glutamic acid. Alternative substitutions at a particular position can also be indicated as “X120A,G,H”, “120A,G,H”, “X120A / G / H”, or“120A / G / H”. Alternatively, different alterations or optional substitutions may be indicated in brackets, e.g., “Arg170 [Tyr, Gly]” or“Arg170 {Tyr, Gly}” or in short “R170 [Y, G]” or “R170 {Y, G}”. Ways of introducing amino acid alterations, e.g., substitutions, into protein sequence are well known in the art.

[0033] Variant polynucleotide and variant polypeptide sequences may be defined by their sequence identity when compared to another sequence. Sequence identity is usually provided as “% sequence identity” or“% identity”. For calculation of sequence identities, in a first step a sequence alignment is produced. According to this invention, a pairwise global alignment is produced, meaning that two sequences are aligned over their complete length. The alignment is usually produced by using a mathematical approach called alignment algorithm. According to the invention, the alignment is generated by using the algorithm of Needleman and Wunsch (J. Mol. Biol. (1970) 48, p. 443-453). Preferably, the program “NEEDLE” (The European Molecular Biology Open Software Suite (EMBOSS)) is used for the purposes of the current invention, using the programs default parameter (polynucleotides: gap open=10.0, gap extend=0.5 and matrix=EDNAFULL; polypeptides: gap open=10.0, gap extend=0.5 and ma- trix=EBLOSUM62). After aligning the two sequences, an identity value is determined from the produced alignment in a second step. For this purpose, the %-identity is calculated by dividing the number of identical residues by the length of the alignment region, which is showing the respective sequence of the present invention over its complete length multiplied with 100: %-identity = (identical residues / length of the alignment region, which is showing the respective sequence of the present invention over its complete length) *100. For calculating the percent identity of two polynucleotides the same applies as outlined above with some specifications. For polynucleotides encoding for a protein the pairwise alignment shall be made over the complete length of the coding region of the sequence of this invention from start to stop codon excluding introns. Introns present in the other sequence, to which the sequence of this invention is compared to shall also be removed for the pairwise alignment. After aligning the two polynucleotide sequences, an identity value is determined in a second step from the alignment produced. Percent identity is calculated by: %-identity = (identical residues / length of the alignment region, which is showing the sequence of the invention from start to stop codon excluding introns over its complete length) *100.

[0034] Herein, the exchange of one amino acid with a similar amino acid may be called “conservative amino acid substitution”.

[0035] Similar amino acids according to the invention are defined as follows:

[0036] Amino acid A is similar to amino acids S

[0037] Amino acid D is similar to amino acids E; N

[0038] Amino acid E is similar to amino acids D; K; Q

[0039] Amino acid F is similar to amino acids W; Y

[0040] Amino acid H is similar to amino acids N; Y

[0041] Amino acid I is similar to amino acids L; M; V

[0042] Amino acid K is similar to amino acids E; Q; R

[0043] Amino acid L is similar to amino acids I; M; V

[0044] Amino acid M is similar to amino acids I; L; V

[0045] Amino acid N is similar to amino acids D; H; S

[0046] Amino acid Q is similar to amino acids E; K; R

[0047] Amino acid R is similar to amino acids K; Q

[0048] Amino acid S is similar to amino acids A; N; T

[0049] Amino acid T is similar to amino acids S

[0050] Amino acid V is similar to amino acids I; L; M

[0051] Amino acid W is similar to amino acids F; Y

[0052] Amino acid Y is similar to amino acids F; H; W “Enzyme properties” include, but are not limited to catalytic activity, substrate / cofactor specificity, product specificity, stability in the course of time, thermostability, pH stability, and chemical stability. “Enzymatic activity” or “catalytic activity” means the catalytic effect exerted by an enzyme, expressed as units per milligram of enzyme (specific activity) or molecules of substrate transformed per minute per molecule of enzyme (molecular activity). Enzymatic activity can be specified by the enzymes actual function, e.g., proteases exerting proteolytic activity by catalyzing hydrolytic cleavage of peptide bonds, lipases exerting lipolytic activity by hydrolytic cleavage of ester bonds, amylases activity involves hydrolysis of glycosidic linkages in polysaccharides, mannanase activity involves hydrolysis of the internal glycoside bonds in the mannan backbone etc.

[0053] As used herein, "wash performance" (also called “cleaning performance” herein) refers to the cleaning result of a composition.

[0054] As used herein, "wash performance of an enzyme " (also called “cleaning performance of an enzyme” herein) refers to the contribution of the enzyme to the cleaning performance of a cleaning composition, i.e. the cleaning performance added to the cleaning composition by the performance of the enzyme. The term “wash performance” is used similarly herein for laundry and hard surface cleaning. The contribution of specific components to the wash performance is compared under relevant washing conditions. The term "relevant washing conditions" or “relevant cleaning conditions” is used herein to indicate the conditions, particularly washing or cleaning temperature, time, washing mechanics, concentration of detergent components in the wash liquor (i.e., suds concentration), type of detergent and water hardness. The term "improved wash performance" is used to indicate that a better cleaning result is obtained under relevant washing conditions, or that a reduced amount of a compound, e.g. less enzyme, on weight basis, is needed to obtain the same end result relative to the corresponding control conditions.

[0055] As used herein, the term "specific performance" refers to the cleaning and removal of specific stains or soils per unit of active enzyme. In some embodiments, the specific performance is determined using stains or soils such as egg, egg yolk, milk, grass, spinach, minced meat, blood, chocolate sauce, chocolate ice cream, baby food, salad dressing, guar gum, locust bean gum, etc.

[0056] “Detergent composition” or “detergent” or “cleaning composition” means compositions designated for cleaning soiled material. Cleaning compositions according to the invention include compositions for different applications such as laundry and hard surface cleaning. Cleaning compositions can be liquid or solid. The term “detergent component” is defined herein to mean a type of chemical, which can be used in detergent compositions. Typical detergent components are surfactants and complexing agents. "Surfactant" (synonymously used herein with “surface active agent”) means an organic chemical that, when added to a liquid, changes the properties of that liquid at an interface. According to its ionic charge, a surfactant is called non-ionic, anionic, cationic, or amphoteric.

[0057] A “complexing agent” (also called chelating agents (chelants) or builder herein) can bind metal ions in a stable chelator complex.

[0058] A “biodegradable” compound (such as a surfactant or complexing agent) is a compound that is readily biodegradable in an aerobic aqueous medium according to the OECD guideline 301. “Readily biodegradable” is defined according to the Detergents Regulation as the ability of a product to biodegrade more than 60% within 28 days according to OECD 301A-F / ASTM. The term “effective amount of a detergent component” includes amounts of certain components to provide effective stain removal and / or effective cleaning conditions (e. g. pH, temperature, water hardness, quantity of foaming), amounts of certain components to effectively provide optical benefits (e. g. optical brightening, dye transfer inhibition, color care), and amounts of certain components to effectively aid the processing (maintain physical characteristics during processing, storage and use; e.g. rheology modifiers, hydrotropes, desiccants).

[0059] A composition “devoid” of a compound shall mean herein that the respective compound is not added to the composition on purpose, preferably that at most non-effective amounts are present, most preferably 0% of the compound are contained in the composition.

[0060] The term “laundry” or “laundering” relates to both household cleaning and industrial cleaning and means the process of treating textiles and / or fabrics with a solution containing a cleaning composition of the present invention. The cleaning or washing process or method may be carried out by using technical devices such as a household or an industrial washing machine. Alternatively, the cleaning or washing process may be done by hand.

[0061] The term “textile” means any textile material including yarns (thread made of natural or synthetic fibers used for knitting or weaving), yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, as well as fabrics made of these materials such as garments, cloths, and other articles. The terms “fabric” (a textile made by weaving, knitting or felting fibers) or “garment” (any article of clothing made of textile) as used herein, mean to include the broader term textile as well.

[0062] The term “fibers” includes natural fibers, synthetic fibers, and mixtures thereof. Examples of natural fibers are of plant (such as flax, jute and cotton) or animal origin, the latter comprising proteins like collagen, keratin and fibroin (e. g. silk, sheep wool, angora, mohair, cashmere). Examples for fibers of synthetic origin are polyurethane fibers such as Spandex® or Lycra®, polyester fibers, polyolefins such as elastofin, or polyamide fibers such as nylon. Fibers may be single fibers or parts of textiles such as knitwear, woven or non-woven fabrics.

[0063] The term “hard surface cleaning” relates to both household hard surface cleaning and industrial hard surface cleaning and means the process of treating hard surfaces with a solution containing a cleaning composition of the present invention. Hard surfaces may include any hard surfaces in a household or industry, such as floors, furnishing, walls, sanitary ceramics, glass, metallic surfaces including medical devices, cutlery, and dishes (also called dishware). A particular form of hard surface cleaning is dishwashing, including manual dish washing (MDW) or automatic dishwashing (ADW).

[0064] The term “dish wash” refers to all forms of washing dishes, e. g. by hand or automatic dish washing. Washing dishes includes, but is not limited to, the cleaning of all forms of crockery such as plates, cups, glasses, bowls, all forms of cutlery such as spoons, knives, forks and serving utensils as well as ceramics, plastics such as melamine, metals, china, glass, and acrylics.

[0065] The term “medical device cleaning” refers to the cleaning step in reprocessing reusable medical devices. Medical device cleaning methods can be divided into two categories, manual and mechanical / automated cleaning methods. Manual cleaning is used when mechanical units are not available or medical devices to be cleaned are too fragile or difficult to clean with a mechanical unit. Mechanical / automated cleaning methods remove soiling and microorganisms through an automated cleaning and rinsing process, this includes ultrasonic cleaning and washing.

[0066] In the field of detergency, usually the term “stains” is used with reference to laundry, e.g., cleaning for textiles, fabric, or fibers, whereas the term “soils” is usually used with reference to hard surface cleaning, e.g., cleaning of dishes and cutlery. However, herein the terms “stain” and “soil” are used interchangeably. “Mannan-comprising stains” herein comprise at least one mannan, at least one galactomannan and / or at least one glucomannan and can further comprise constituents such as cellulose and / or hemicellulose. Further, such stains may comprise proteinaceous material, starch and / or sugars. Galactomannans usually consist of a mannose backbone with galactose side groups. Herein, galactomannans include galactomannans having the following mannose to galactose ratio: fenugreek gum about 1 : 1 , guar gum about 2: 1 , tara gum about 3: 1 , locust bean gum or carob gum about 4: 1 , cassia gum about 5: 1 , wherein the ratio is mannose:galactose. Galactomannans are often used in food and cosmetic products to increase the viscosity of a liquid product. Glucomannans usually consist of a mannose backbone with glucose side groups.

[0067] Detailed description

[0068] Mannanases

[0069] “Mannanases” as described herein are enzymes selected from the group of mannan degrading enzymes that according to the invention have “mannanase activity”. The mannan degrading enzyme according to the invention is selected from the group of endo-1 ,4-p-mannosidases (EC 3.2.1 .78), a group of enzymes which may be called endo - - 1 ,4-D- mannanase, p-mannanase, or mannanase herein. “Mannanase activity” describes the capability of p-mannanases to degrade mannans by hydrolysis of the internal glycoside bonds in the mannan backbone. Since Mannanases degrade the mannan backbone, they are capable of degrading mannans, galactomannans and / or glucomannans. Mannanase activity may be determined by assays for measurement of mannanase activity, which are known to those skilled in the art. For instance, a mannanase to be tested may be applied to 4 mm diameter holes punched out in agar plates comprising 0.2% AZCL galactomannan (carob), i.e. substrate for the assay of endo-1 ,4-beta-D-man- nanase. Carob is e.g. available as l-AZGMA from the company Megazyme. Mannan degrading activity may be tested in a liquid assay using carob galactomannan dyed with Remazol Brilliant Blue as described in McCleary, B. V.10 (1978). Carbohydrate Research, 67(1), 213-221. Another method for testing mannan degrading activity uses detection of reducing sugars when incubated with substrate such as guar gum or locust bean gum - for reference see Miller, G. L. Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugars. Analytical Chemistry 1959; 31 : 426-428.

[0070] The mannanase of the present invention is a mannanase that comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1 , or which is at least 65% identical to SEQ ID NO: 2 or 3.

[0071] In one embodiment, the mannanase is a variant of a parent mannanase, wherein the mannanase variant comprises one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, 282, 318, 319, and 322, according to the numbering of SEQ ID NO: 1, and an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical SEQ ID NO: 1.

[0072] In another embodiment, the mannanase is a variant of a parent mannanase that comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions se- lected from the group consisting of X59V, X66D, X89H, X234Q, X259M, X282Y, X318N, X319G, and X322G according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical SEQ ID NO: 1 . In another embodiment, the mannanase is a variant of a parent mannanase that comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, X282Y, X318N, X319G, and X322G according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 90%, preferably at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical SEQ ID NO: 1.

[0073] In another embodiment, the mannanase is a variant of a parent mannanase that comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical SEQ ID NO: 1.

[0074] The mannanase variant can additionally comprise one or more, preferably 1-10, more preferably 1 -5 conservative amino acid substitutions.

[0075] In another embodiment, the mannanase is a variant comprising or consisting of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 and optionally additionally comprises one or more, preferably 1 -10, more preferably 1-5 conservative amino acid substitutions.

[0076] In another embodiment, the mannanase consists of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 and optionally additionally comprises one or more, preferably 1 -10, more preferably 1-5 conservative amino acid substitutions.

[0077] In one embodiment, the mannanase is a variant of a parent mannanase, wherein the mannanase variant comprises one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, and 282, according to the numbering of SEQ ID NO: 1 , and an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical to amino acids 1-296 of SEQ ID NO: 1 .

[0078] In another embodiment, the mannanase is a variant of a parent mannanase that comprises at least one, at least two, at least three, at least four, at least five, or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, and X282Y according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical to amino acids 1-296 of SEQ ID NO: 1.

[0079] In another embodiment, the mannanase is a variant of a parent mannanase that comprises at least one, at least two, at least three, at least four, at least five, or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, and X282Y according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 90%, preferably at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical to amino acids 1 -296 of SEQ ID NO: 1. In another embodiment, the mannanase is a variant of a parent mannanase that comprises at least one, at least two, at least three, at least four, at least five, or all amino acid substitutions selected from the group consisting of Q59V, N66D, A89H, E234Q, W259M, and N282Y according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical to amino acids 1-296 of SEQ ID NO: 1 .

[0080] In another embodiment, the mannanase is a variant comprising or consisting of amino acids 1 -296 of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, and N282Y, according to the numbering of SEQ ID NO: 1 , and optionally additionally comprises one or more, preferably 1 -10, more preferably 1-5 conservative amino acid substitutions.

[0081] In another embodiment, the mannanase is a variant consisting of amino acids 1 -296 of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, according to the numbering of SEQ ID NO: 1 , and optionally additionally comprises one or more, preferably 1 -10, more preferably 1 -5 conservative amino acid substitutions.

[0082] In one embodiment, the mannanase comprises an amino acid sequence that is with increasing preference at least 70%, at least 72%, at least 74%, at least 75%, at least 76%, at least 78%, at least 80%, at least 82%, at least 84%, at least 85%, at least 86%, at least 88%, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 2.

[0083] In one embodiment, the mannanase comprises or consists of SEQ ID NO: 2 and optionally additionally comprises one or more, preferably 1-10, more preferably 1-5 conservative amino acid substitutions.

[0084] In one embodiment, the mannanase comprises an amino acid sequence that is with increasing preference at least 70%, at least 72%, at least 74%, at least 75%, at least 76%, at least 78%, at least 80%, at least 82%, at least 84%, at least 85%, at least 86%, at least 88%, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 3.

[0085] In one embodiment, the mannanase comprises or consists of SEQ ID NO: 3 and optionally additionally comprises one or more, preferably 1-10, more preferably 1-5 conservative amino acid substitutions.

[0086] Preferably, the mannanase is a variant of a parent mannanase that comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, X282Y, X318N, X319G, and X322G according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 90%, preferably at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical to SEQ ID NO: 1 or the man- nanase is a mannanase that has an amino acid sequence which is with increasing preference, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 2 or SEQ ID NO: 3.

[0087] More preferably, the mannanase is a variant of a parent mannanase that comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, X282Y, X318N, X319G, and X322G according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 90%, preferably at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical to SEQ ID NO: 1 or the mannanase is a mannanase that has an amino acid sequence which is with increasing preference, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 3.

[0088] Most preferably, the mannanase is a variant of a parent mannanase that comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, X282Y, X318N, X319G, and X322G according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 90%, preferably at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical to SEQ ID NO: 1

[0089] In another preferred embodiment, the mannanase comprises or consists of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 or the mannanase is a mannanase that has an amino acid sequence which is with increasing preference, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 2 or SEQ ID NO: 3.

[0090] More preferably, the mannanase comprises or consists of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 or the mannanase is a mannanase that has an amino acid sequence which is with increasing preference, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to SEQ ID NO: 3.

[0091] Most preferably, the mannanase is a variant comprising or consisting of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1.

[0092] Compositions

[0093] In one embodiment, the present invention is directed to a liquid cleaning composition comprising a mannanase as described above.

[0094] The liquid cleaning composition may comprise further detergent components.

[0095] The one or more detergent component may be selected from the group consisting of additional enzymes (secondary enzymes) different from the mannanase described herein, enzyme stabilizing systems, surfactants, defoamers, complexing agents, polymers, bleaching systems (bleach), rheology modifiers, hydrotropes, softening agents, desiccants, whitening agents, buffers, preservatives, anti-corrosion additives, dyestuff, and fragrances. Preferably, at least one additional component of the composition is selected from the group consisting of surfactants, complexing agents, polymers, preservatives, and second enzymes different to the mannanase.

[0096] Detergent components may have more than one function in the final application of a liquid cleaning composition, therefore any detergent component mentioned in the context of a specific function herein, may also have another function in the final application of a liquid cleaning composition. The function of a specific detergent component in the final application of a cleaning composition usually depends on its amount within the cleaning composition, i.e. , the effective amount of a detergent component. Detergent components vary in type and / or amount in a cleaning composition depending on the desired application such as washing white textiles, colored textiles, and wool. Further selected component(s) depend on the physical form of a cleaning composition (liquid, solid, gel, provided in pouches or as a tablet, etc.). The component(s) chosen e. g. for cleaning compositions further depend on regional conventions, which themselves are related to aspects like washing temperatures used, mechanics of laundry machine (vertical vs. horizontal axis machines), water consumption per wash cycle etc. and geographical characteristics like average hardness of water.

[0097] In one embodiment, a cleaning composition comprises more than two detergent components, wherein at least one component is effective in stain-removal, at least one component is effective in providing the optimal cleaning conditions, and at least one component is effective in maintaining the physical characteristics of the detergent.

[0098] The cleaning composition preferably is a liquid cleaning composition or a combination of liquid and solid cleaning compositions. The liquid cleaning composition is preferably a gel cleaning composition.

[0099] The cleaning composition can be a unit dose or multi dose composition. The cleaning composition can be in the form of a pouch, including multi-compartment pouches. The cleaning composition can be a laundry or dish washing cleaning composition, suitable for home care and / or industrial and institutional (l&l) cleaning. Both laundry and dish wash composition can be in the form of a hand wash or automated wash composition. Preferably, the dish wash composition is an Automatic Dish Wash (ADW).

[0100] Detergent pouches can be of any form, shape, and material, which is suitable for containing the composition, e.g., without allowing the 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 blend compositions comprising hydrolytically degradable and water-soluble polymer blends such as polyactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by Chris Craft In. Prod. Of Gary, Ind., US) plus plasticizers like glycerol, ethylene glycol, propylene glycol, sorbitol and mixtures thereof. The pouches can comprise a solid laundry cleaning composition and / or a liquid cleaning composition. The compartment for liquid components can be different in composition from compartments containing solids (see e.g. US 2009 / 001 1970). Cleaning compositions may comprise total amounts of enzyme in the range of 0.00005% to 0. 1 %, preferably 0.0002- 0.05% by weight, all relative to the total weight of the cleaning composition. In one embodiment, the cleaning composition has a pH in the range of 5-12, preferably in the range of 6-1 1 , more preferably in a range selected from 6-10, 7- 9, and 7.5-8.5.

[0101] In one embodiment, the cleaning compositions according to the invention comprise one or more surfactant(s). According to its ionic charge, a surfactant is called non-ionic, anionic, cationic, or amphoteric.

[0102] The cleaning composition of the present invention 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 preferred embodiments, the cleaning compositions of the invention comprise at least one surfactant. In a particular embodiment, the cleaning composition of the present invention includes a mixture of one or more nonionic surfactants and one or more anionic surfactants. The surfactant(s) is / are typically present at a level of from about 0.1 to 60 wt.-%, such as 1 to 40 wt.-%, 3 to 20 wt.-% or 3 to 10 wt.-%. The surfactant(s) is / are chosen based on the desired cleaning application, and includes any conventional surfactant(s) known in the art.

[0103] In one embodiment, the cleaning composition of the present invention comprises a reduced amount of surfactant in comparison to a conventional detergent not containing a mannanase as described herein.

[0104] Any surfactant known in the art for use in detergents may be utilized. Non-limiting examples of surfactants are disclosed McCutcheon's 2016 Detergents and Emulsifiers, and McCutcheon's 2016 Functional Materials, both North American and International Edition, MC Publishing Co, 2016 edition. Further useful examples are disclosed in earlier editions of the same publications, which are known to those skilled in the art.

[0105] In a preferred embodiment, the cleaning compositions according to the invention comprise one or more biodegradable surfactant(s). A biodegradable surfactant is readily biodegradable in an aerobic aqueous medium according to the OECD guideline 301. Biodegradable surfactants include but are not limited to, sodium alkyl ether sulfates, preferably sodium laureth sulfate, preferably sodium laureth sulfate + 2 EO (Texapon N70), alkyl polyglucosides, preferably alkyl polyglucoside C10-C16 (Glucopon 600), and alcohol ethoxylates, preferably C12-C18 fatty alcohol + 7 EO (De- hydol LT 7).

[0106] “Sodium alkyl ether sulfates” include but are not limited to sodium laureth sulfate + 2 EO.

[0107] “Alkyl polyglucosides” (APGs) are nonionic surfactants that include compounds according to the general formula (I)

[0108] R1in general formula (I) is selected from C1-C17 alkyl and C2-C17 alkenyl, wherein alkyl and / or alkenyl are linear (straight-chain; n-) or branched; examples are n-C?Hi5, n-CgHw, n-CnFh, n-C Hg?, n-C Hsi, n-CizHss, i-CgH , I- C12H25.

[0109] R2in general formula (I) is selected from H, C1-C17 alkyl and C2-C17 alkenyl, wherein alkyl and / or alkenyl are linear (straight-chain; n-) or branched.

[0110] G1in general formula (I) is selected from monosaccharides with 4 to 6 carbon atoms, such as glucose and xylose. The integer w of the general formula (I) is in the range of from 1.1 to 4, w being an average number. “Alcohol ethoxylates” include but are not limited to C12-C18 fatty alcohol + 7 EO.

[0111] The cleaning compositions according to the invention may comprise one or more complexing agents (chelating agents (chelants), sequestering agents), which may form water-soluble complexes with calcium and magnesium. Such compounds may be called “builders” or “building agents” herein.

[0112] In one embodiment, the cleaning composition of the invention comprises at least one complexing agent or builder selected from non-phosphate-based builders such as sodium gluconate, citrate(s), silicate(s), carbonate(s), phospho- nate(s), amino carboxylate(s), polycarboxylate(s), polysulfonate(s), and polyphosphonate(s). Preferably, cleaning compositions of the current invention are free from phosphate, meaning essentially free from phosphate-based builders. Herein, “essentially free from phosphate” is to be understood as meaning that the content of phosphate and polyphosphate is in sum in the range of 10 ppm to 1 % by weight, determined by gravimetry and referring to the respective inventive cleaning composition.

[0113] Cleaning compositions of the invention may comprise one or more citrates. “Citrate(s)” include the mono- and the dialkali metal salts and in particular the mono- and preferably the trisodium salt of citric acid, ammonium or substituted ammonium salts of citric acid as well as citric acid as such.

[0114] Cleaning compositions of the invention may comprise one or more silicates. “Silicate(s)” in the context of the present invention include in particular sodium disilicate and sodium metasilicate, aluminosilicates such as sodium aluminosilicates like zeolith A (i.e. Nai2(AIO2)i2(SiO2)i2*27H2O), and sheet silicates, in particular those of the formula alpha- Na2Si2O5, beta-Na2Si2O5, and delta-Na2Si2O5.

[0115] Cleaning compositions of the invention may comprise one or more carbonates. The term “carbonate(s)” includes alkali metal carbonates and alkali metal hydrogen carbonates, preferred are the sodium salts. Particularly suitable is sodium carbonate (Na2CO3).

[0116] Cleaning compositions of the invention may comprise one or more phosphonates. “Phosphonates” include, but are not limited to 2-phosphinobutane-1 ,2,4-tricarboxylic acid (PBTC); ethylenediaminetetra(methylenephosphonic acid) (EDTMPA); 1 -hydroxyethane-1 , 1 -diphosphonic acid (HEDP), CH2C(OH)[PO(OH)2]2; aminotris(methylenephosphonic acid) (ATMP), N[CH2PO(OH)2]3; aminotris(methylenephosphonate), sodium salt (ATMP), N[CH2PO(ONa)2]3; 2-hy- droxyethyliminobis(methylenephosphonic acid), HOCH2CH2N[CH2PO(OH)2]2; diethylenetriaminepenta(meth- ylenephosphonic acid) (DTPMP), (HO)2POCH2N[CH2CH2N[CH2PO(OH)2]2]2; diethylenetriaminepenta(meth- ylenephosphonate), sodium salt, CgHps-xjNsNaxOisPs (x=7); hexamethylenediamine(tetramethylenephosphonate), potassium salt, CioH(28-X)N2KxOi2P4 (x=6); and bis(hexamethylene)triamine(pentamethylenephosphonic acid), (HO2)POCH2N[(CH2)2N[CH2PO(OH)2]2]2. Salts thereof may be suitable, too.

[0117] Cleaning compositions of the invention may comprise one or more amino carboxylates. Non-limiting examples of suitable “amino carboxylates” include, but are not limited to: diethanol glycine (DEG), dimethylglycine (DMG), nitrilitri- acetic acid (NTA), N-hydroxyethylaminodiacetic acid, ethylenediaminetetraacetic acid (EDTA), N-(2hydroxyethyl)imi- nodiacetic acid (HEIDA), hydroxyethylenediaminetriacetic acid, N-hydroxyethyl-ethylenediaminetriacetic acid (HEDTA), hydroxyethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid (DTPA), and methylglycinediacetic acid (MGDA), glutamic acid-diacetic acid (GLDA), iminodisuccinic acid (IDS), hydroxyiminodisuccinic acid, ethylenediaminedisuccinic acid (EDDS), aspartic acid-diacetic acid, and alkali metal salts or ammonium salts thereof. The above cited abbreviations, in particular MGDA, GLDA, and EDDS, always include the acid as such and the salt thereof. Further suitable are aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N, N-diacetic acid (ASDA), aspar- tic acid-N-monopropionic acid (ASMP), N-(2-sulfomethyl) aspartic acid (SMAS), N-(2-sulfoethyl) aspartic acid (SEAS), N-(2-sulfomethyl) glutamic acid (SMGL), N-(2-sulfoethyl) glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), alpha-alanine-N, N-diacetic acid (alpha-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N, N-diacetic acid (PHDA), anthranilic acid-N, N-diacetic acid (ANDA), sulfanilic acid-N, N-diace- tic acid (SLDA), taurine-N, N-diacetic acid (TUDA) and sulfomethyl-N, N-diacetic acid (SMDA) and alkali metal salts or ammonium salts thereof. The term “ammonium salts” as used in in this context refers to salts with at least one cation that bears a nitrogen atom that is permanently or temporarily quaternized. Examples of cations that bear at least one nitrogen atom that is permanently quaternized include tetramethylammonium, tetraethylammonium, dimethyldiethyl ammonium, and n-Cio-C2o-alky I trimethyl ammonium. Examples of cations that bear at least one nitrogen atom that is temporarily quaternized include protonated amines and ammonia, such as monomethyl ammonium, dimethyl ammonium, trimethyl ammonium, monoethyl ammonium, diethyl ammonium, triethyl ammonium, n-Cio-C2o-alkyl dimethyl ammonium 2-hydroxyethylammonium, bis(2-hydroxyethyl) ammonium, tris(2-hydroxyethyl)ammonium, N-methyl 2- hydroxyethyl ammonium, N,N-dimethyl-2-hydroxyethylammonium, and especially NH4+.

[0118] In one embodiment, cleaning compositions of the invention comprise more than one complexing agent. Preferably, inventive cleaning compositions contain less than 0.2% by weight of nitrilotriacetic acid (NTA), or 0.01 to 0.1 % NTA by weight relative to the total weight of the cleaning composition.

[0119] In one embodiment, the cleaning composition of the invention comprises at least one of aminocarboxylates selected from methylglycine diacetate (MGDA), glutamic acid diacetate (GLDA), ethylenediaminedisuccinic acid (EDDS) and the respective salts thereof, e.g., alkali (such as sodium) salts thereof in amounts in the range of 0.1 % to 25.0% by weight, in the range of 0.1 % to 18% by weight, in the range of 1 .0% to 18.0% by weight, in the range of 3.0% to 15.0% by weight, in the range of 3.0% to 10.0% by weight, or in the range of 5.0% to 8.0% by weight relative to the total weight of the cleaning composition.

[0120] In a preferred embodiment, the cleaning compositions according to the invention comprise one or more biodegradable complexing agent(s). A biodegradable complexing agent is readily biodegradable in an aerobic aqueous medium according to the OECD guideline 301 . Biodegradable complexing agents include but are not limited to, EDDS, MGDA, GLDA, and citrate.

[0121] The cleaning compositions of the invention may comprise one or more hydrotropes. One or more hydrotropes may be selected from organic solvents such as ethanol, isopropanol, ethylene glycol, 1 ,2-propylene glycol, and further organic solvents known in the art that are water-miscible under normal conditions without limitation. In one embodiment, the cleaning composition of the invention comprises 1 ,2-propylene glycol in a total amount in the range of 5- 10% by weight, preferably of about 6% by weight, all relative to the total weight of the cleaning composition. Further non-limiting examples of hydrotropes include sodium benzene sulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycol ethers, sodium hydroxy naphthoate, sodium hydroxy naphthalene sulfonate, sodium ethyl hexyl sulfate, and combinations thereof.

[0122] In one embodiment, the cleaning composition comprises at least one preservative. A preservative is an antimicrobial agent which may be added to aqueous products and compositions to maintain the original performance, characteristics and integrity of the products and compositions by killing contaminating microorganisms or inhibiting their growth. An antimicrobial agent is a chemical compound that kills microorganisms or inhibits their growth or reproduction. Microorganisms can be bacteria, yeasts or molds.

[0123] The composition may contain one or more antimicrobial agents and / or preservatives as listed in patent WO2021 / 115912 A1 (“Formulations comprising a hydrophobically modified polyethyleneimine and one or more enzymes”) on pages 35 to 39.

[0124] Especially of interest for the cleaning compositions and fabric and home care products and specifically in the laundry formulations are any of the following antimicrobial agents and / or preservatives:

[0125] 4,4’-dichloro 2-hydroxydiphenyl ether (further names: 5-chloro-2-(4-chlorophenoxy) phenol, Diclosan, DCPP), Tino- san® HP 100 (30wt.% of DCPP in in 1 ,2-propylene glycol); 2-Phenoxyethanol (further names: Phenoxyethanol, Methylphenylglycol, Phenoxetol, ethylene glycol phenyl ether, Ethylene glycol monophenyl ether, 2-(phenoxy) ethanol, 2-phenoxy-1 -ethanol); 2-bromo-2-nitropropane-1,3-diol (further names: 2-bromo-2-nitro-1 ,3-propanediol, Bronopol); Glutaraldehyde (further names: 1 -5-pentandial, pentane-1 ,5-dial, glutaral, glutardialdehyde); Glyoxal (further names: ethandial, oxylaldehyde, 1 ,2-ethandial); 5-bromo-5-nitro-1,3-dioxane (further names: 5-bromo-5-nitro-m-dioxane, Bronidox ®); Phenoxypropanol (further names: propylene glycol phenyl ether, phenoxyisopropanol 1 -phenoxy-2-pro- panol, 2-phenoxy-1 -propanol); Glucoprotamine (chemical description: reaction product of glutamic acid and alkylpropylenediamine, further names: Glucoprotamine 50); Cyclohexyl hydroxyl diazenium-1 -oxide, potassium salt (further names: N-cyclohexyl-diazenium dioxide, Potassium HDO, Xyligene,);Formic acid (further names: methanoic acid, Pro- tectol® FM, Protectol® FM 75, Protectol® FM 85, Protectol® FM 99, Lutensol® FM) and its salts, e.g. sodium form late); Tetrahydro-3, 5-d imethy 1-1 ,3,5-thiadia-zine-2-th lone (further names: 3,5-dimethyl-1 ,3-5-thiad iazi nane-2-th I- one, Dazomet; 2,4-dichlorobenzyl alcohol (further names: dichlorobenzyl alcohol, 2,4-dichloro-benzenemethanol, (2,4- dichloro-phenyl)-methanol, DCBA); 1 -propanol (further names: n-propanol, propan-1 -ol, n-propyl alcohol; 1 ,3,5-Tris- (2-hydroxyethyl)-hexahydro-1 ,3,5-triazin (further names: hexyhydrotriazine, tris(hydroethyl)-hexyhydrotriazin, hexyhy- dro-1 ,3-5-tris(2-hydroxyethyl)-s-triazine, 2,2',2"-(hexahydro-1 ,3,5-triazine-1 ,3,5- triyl)triethanol; 2-buty I -benzo[d] isoth I- azol-3-one (“BBIT”); 2-methyl-2H-isothiazol-3-one (“MIT””); 2-octyl-2H-isothiazol-3-one (“OIT”); 5-Chloro-2-methyl-2H- isothiazol-3-one (“CIT” or“CMIT”); Mixture of 5-chloro-2-methyl-2H- isothiazol-3-one (“CMIT”) and 2-methyl-2H-isothi- azol-3-one (“MIT”) (Mixture of CMIT / MIT); 1 ,2-benzisothiazol-3(2H)-one (“BIT”); Hexa-2,4-dienoic acid (trivial name “sorbic acid”) and its salts, e.g., calcium sorbate, sodium sorbate; potassium (E,E)-hexa-2,4-dienoate (Potassium Sorbate); Lactic acid and its salts; L-(+)-lactic acid; especially sodium lactate; Benzoic acid and salts of benzoic acid, e.g., sodium benzoate, ammonium benzo-ate, calcium benzoate, magnesium benzoate, MEA-benzoate, potassium benzoate; Salicylic acid and its salts, e.g., calcium salicylate, magnesium salicylate, MEA salicylate, sodium salicylate, potassium salicylate, TEA salicylate; Benzalkonium chloride, benzalkonium bromide, benzalkonium saccharinate; Didecyldimethylammonium chloride (“DDAC”); N-(3-aminopropyl)-N-dodecylpropane-1 ,3-diamine ("Diamine"); Peracetic acid; Hydrogen peroxide.

[0126] At least one antimicrobial agent or preservative may be added to the inventive composition in a concentration of 0.001 to 10% relative to the total weight of the composition. Preferably, the composition contains 2-phenoxyethanol in a concentration of 0.1 to 2% or 4, 4’ -dichloro 2-hydroxydi- phenyl ether (DCPP) in a concentration of 0.005 to 0.6%.

[0127] The invention also encompasses a method of preserving an aqueous composition according to the invention against microbial contamination or growth, which method comprises addition of at least one antimicrobial agent or preservative, preferably 2-phenoxyethanol.

[0128] The invention also encompasses a method of providing an antimicrobial effect on textiles after treatment with a solid laundry detergent (e.g. powders, granulates, capsules, tablets, bars etc.), a liquid laundry detergent, a softener or an after-rinse containing 4,4’-dichloro 2-hydroxydiphenyl ether (DCPP).

[0129] In one embodiment, the cleaning composition comprising a mannanase as described herein further comprises one or more second enzyme different from the mannanase. Preferably, the second enzyme is selected from the group consisting of proteases, amylases, lipases, cellulases, second mannanases, hemicellulases, phospholipases, esterases, cutinases, pectinases, lactases, peroxidases, xylanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, beta-glucanases, arabi- nosidases, hyaluronidases, chondroitinases, laccases, nucleases, DNase, phosphodiesterases, phytases, carbohydrases, galactanases, xanthanases, xyloglucanases, oxidoreductase, perhydrolases, aminopeptidases, asparaginases, carbohydrases, carboxypeptidases, catalases, chitinases, cyclodextrin glycosyltransferases, alpha-galacto- sidases, beta-galactosidases, glucoamylases, alpha-glucosidases, beta-glucosidases, invertases, ribonucleases, transglutaminases, and dispersins, and combinations of at least two of the foregoing types. More preferably, the second enzyme is selected from the group consisting of proteases, amylases, lipases, cellulases, mannanases, xylanases, DNases, dispersins, pectinases, pectate lyases, glycosidases, and oxidoreductases, and combinations of at least two of the foregoing types. Most preferably, the second enzyme is an amylase or protease, preferably amylase. Particularly preferred additional enzymes are disclosed elsewhere herein, and that description is incorporated by reference also to this part of the description.

[0130] The composition of the present invention can comprise one type of enzyme or more than one enzyme of different types, e.g., a mannanase and an amylase, or more than one enzyme of the same type, e.g., two or more different mannanases, or mixtures thereof, e.g., a mannanase and two different amylases.

[0131] In case, the composition comprises a protease, preferably a protease inhibitor is present, preferably selected from phenylboronic acid (preferably 4-FPBA) or a peptide aldehyde or a bisulfite adduct or acetal thereof (preferably a tripeptide aldehyde, preferably, Z-GAY or Z-VAL).

[0132] The cleaning compositions may comprise water-soluble sources of calcium and / or magnesium ions. In one embodiment, the cleaning composition comprises an enzyme stabilizing system as described herein.

[0133] All compounds can be bio-based or fossil-based, preferably bio-based.

[0134] Preferred compositions

[0135] In a preferred embodiment, the present invention is directed to a liquid cleaning composition comprising a mannanase as described herein, at least one biodegradable surfactant and at least one biodegradable complexing agent. In one embodiment, the present invention is directed to a detergent composition comprising a) a mannanase as described herein; b) one or more surfactant, preferably a biodegradable surfactant, preferably, in a concentration of 0.2-65%, preferably

[0136] 0.2-40%, c) one or more complexing agent, preferably a biodegradable complexing agent, in a concentration of 0.01 -25%, and d) optionally one or more additional compound selected from the group consisting of additional enzyme different from the mannanase under a), defoamer, polymer, bleaching system (bleach), rheology modifier, hydrotrope, softening agent, desiccant, whitening agent, buffer, preservative, anti-corrosion additive, dyestuff and fragrance; preferably wherein the cleaning composition, is a liquid, pouch, or capsule cleaning composition.

[0137] Preferably, the cleaning composition of the present invention comprises in addition to the mannanase as described herein a) one or more surfactant selected from the group consisting of sodium alkyl ether sulfates, preferably sodium lau- reth sulfate, more preferably sodium laureth sulfate +2 EO, alkyl polyglucosides, preferably alkyl polyglucoside C10-C16, and alcohol ethoxylates, preferably C12-C18 fatty alcohol +7 EO, and b) one or more complexing agent selected from the group consisting of EDDS, MGDA, GLDA, and citrate, preferably wherein the complexing agent is EDDS and / or citrate.

[0138] Preferably, the cleaning composition of the present invention comprises in addition to the mannanase as described herein a) one or more surfactant selected from the group consisting of sodium alkyl ether sulfates, preferably sodium laureth sulfate, preferably sodium laureth sulfate +2 EO, alkyl polyglucosides, preferably alkyl polyglucoside C10-C16, and alcohol ethoxylates, preferably C12-C18 fatty alcohol +7 EO, b) one or more complexing agent selected from the group consisting of EDDS, MGDA, GLDA, and citrate, preferably wherein the complexing agent is EDDS, and c) one or more compound selected from the group consisting of sulphonic acid, 1,2 propane diol, triethanolamine, monoethanolamine, NaOH, glycerol, ethanol, and polymer.

[0139] Preferably, the cleaning composition of the present invention comprises a) a mannanase as described herein, preferably in a concentration of 0.00005-0.001 % (w / w), preferably 0.0001 -0.0005% (w / w) (w / w), b) sodium laureth sulfate +2 EO, preferably in a concentration of 1 -5%, more preferably 2-3% (w / w), c) alkyl polyglucoside C10-C16, preferably in a concentration of 1-5%, more preferably 1 .5-3% (w / w), d) C12-C18-fatty alcohol + 7 EO, preferably in a concentration of 10-15%, more preferably 12-13% (w / w), e) EDDS, preferably in a concentration of 0.01 -5%, more preferably 0.1 -2% (w / w) f) Coco fatty acid K12-18, preferably in a concentration of 1-10%, more preferably 4.5-5.5% (w / w), g) Na citrate 2H2O, preferably in a concentration of 1 -10%, more preferably 2-4% (w / w), h) Glycerol, preferably in a concentration of 1 -10%, more preferably 4-6% (w / w), i) Ethanol, preferably in a concentration of 1 -10%, more preferably 4-6% (w / w) j) NaOH, preferably in a concentration of 1 -5%, more preferably 0.1 -2% (w / w), k) Grafted maltodextrin (Bverde GP 790 L), preferably in a concentration of 1 -5%, more preferably 0.1 -2% (w / w) l) Water up to 95%. Methods of making a composition

[0140] In one embodiment, the present invention also refers to a method of making a composition comprising the steps of mixing a) a mannanase as described herein, b) a biodegradable surfactant, c) a biodegradable complexing agent, and d) optionally one or more additional components described herein.

[0141] Methods of washing or cleaning

[0142] The present invention also refers to a method of washing or cleaning, preferably laundry or hard surface cleaning, comprising the steps of contacting an object or the surface of an object, preferably a textile or a hard surface, with a composition comprising a mannanase as described herein, preferably wherein the composition comprises at least one additional detergent component, preferably a surfactant and / or a complexing agent. Preferably, the hard surfaces are selected from floors, furnishing, walls, sanitary ceramics, glass, metallic surfaces including medical devices, cutlery, and dishes. Preferably, the method for hard surface cleaning, comprises the step of contacting a medical device, cutlery, or dish with a composition comprising a mannanase as described herein, preferably wherein the composition comprises at least one additional detergent component, preferably a surfactant and / or a complexing agent. A particular preferred form of hard surface cleaning is dishwashing, preferably manual dish washing (MDW) or automatic dishwashing (ADW), most preferably automatic dishwashing (ADW). Preferably, the method of laundry cleaning or washing, comprises the step of contacting a textile with a composition comprising a mannanase as described herein, preferably wherein the composition comprises at least one additional detergent component, preferably a surfactant and / or a complexing agent.

[0143] Thus, the present invention is also directed to a method of washing or cleaning comprising the steps of a) providing a liquid cleaning composition containing a mannanase, as described herein, and b) contacting an object having a mannan-comprising stain with the liquid cleaning composition of a) under conditions wherein the mannanase shows mannanase activity, wherein step b) is performed for 5-60 min, preferably 10-45 min, more preferably 15-40 min, more preferably for 15- 30 min, most preferably for 15-25 min. Thus, step b) may be performed for 5 min, 6 min, 7 min, 8 min, 9 min, 10 min, 11 min, 12 min, 13 min, 14 min, 15 min, 16 min, 17 min, 18 min, 19 min, 20 min, 21 min, 22 min, 23 min, 24 min, 25 min, 26 min, 27 min, 28 min, 29 min, 30 min, 31 min, 32 min, 33 min, 34 min, 35 min, 36 min, 37 min, 38 min, 39 min,

[0144] 40 min, 41 min, 42 min, 43 min, 44 min, 45 min, 46 min, 47 min, 48 min, 49 min, 50 min, 51 min, 52 min, 53 min, 54 min, 55 min, 56 min, 57 min, 58 min, 59 min or 60 min. Preferably, step b) is performed for 10 min, 11 min, 12 min, 13 min, 14 min, 15 min, 16 min, 17 min, 18 min, 19 min, 20 min, 21 min, 22 min, 23 min, 24 min, 25 min, 26 min, 27 min, 28 min, 29 min, 30 min, 31 min, 32 min, 33 min, 34 min, 35 min, 36 min, 37 min, 38 min, 39 min, 40 min, 41 min,

[0145] 42 min, 43 min, 44 min, or 45 min. More preferably step b) is performed for 15 min, 16 min, 17 min, 18 min, 19 min,

[0146] 20 min, 21 min, 22 min, 23 min, 24 min, 25 min, 26 min, 27 min, 28 min, 29 min, 30 min, 31 min, 32 min, 33 min, 34 min, 35 min, 36 min, 37 min, 38 min, 39 min, or 40 min. More preferably step b) is performed for 15 min, 16 min, 17 min, 18 min, 19 min, 20 min, 21 min, 22 min, 23 min, 24 min, 25 min, 26 min, 27 min, 28 min, 29 min, or 30 min. Most preferably for 15 min, 16 min, 17 min, 18 min, 19 min, 20 min, 21 min, 22 min, 23 min, 24 min, or 25 min. Such short wash programs or cycles are often called express wash, high-speed wash, quick wash, short wash, or 1- hour wash.

[0147] In one embodiment, step b) is performed at a temperature in the range of 5-40°C, preferably in the range of 10-35 °C, most preferably in the range of 20-30 °C. Thus, step b) may be performed at 5°C, 6°C, 7°C, 8°C, 9°C, 10°C, 11 °C, 12°C, 13°C, 14°C, 15°C, 16°C, 17°C, 18°C, 19°C, 20°C, 21 °C, 22°C, 23°C, 24°C, 25°C, 26°C, 27°C, 28°C,

[0148] 29°C, 30°C, 31 °C, 32°C, 33°C, 34°C, 35°C, 36°C, 37°C, 38°C, 39°C or 40 °C. Preferably, step b) is performed at

[0149] 10°C, 11 °C, 12°C, 13°C, 14°C, 15°C, 16°C, 17°C, 18°C, 19°C, 20°C, 21 °C, 22°C, 23°C, 24°C, 25°C, 26°C, 27°C,

[0150] 28°C, 29°C, 30°C, 31 °C, 32°C, 33°C, 34°C, or 35°C. More preferably, step b) is performed at 20°C, 21 °C, 22°C,

[0151] 23°C, 24°C, 25°C, 26°C, 27°C, 28°C, 29°C, 30°C. Most preferably step b) is performed at 20°C.

[0152] In a preferred embodiment, step b) is performed for 15-25 min at 20°C or 40°C. In an even more preferred embodiment, step b) is performed for 15-25 min at 20°C.

[0153] In one embodiment, the liquid cleaning composition under a) is a liquid cleaning composition comprising at least one mannanase, wherein the mannanase comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1 , or which is at least 65% identical to SEQ ID NO: 2 or 3, as described herein, at least one biodegradable surfactant as described herein, and at least one biodegradable complexing agent as described herein. In a preferred embodiment, the liquid cleaning composition is dosed to obtain a concentration of the at least one mannanase in the range of 0.0000001 to 0.001 g / l, preferably 0.000001 to 0.0001 g / l, of the at least one biodegradable surfactant in the range of 0.015 to 1.5 g / l, preferably 0.015-0.75 g / l, and at least one biodegradable complexing agent in the range of 0.0015 to 0.45 g / l, preferably 0.0015 to 0.225 g / l.

[0154] The present invention is also directed to a method of removing mannan-comprising stains, preferably containing guar or locust bean gums, glucomannans, and galactomannans, preferably containing guar or locust bean gums, comprising the step of contacting an object comprising a mannan-comprising stain, preferably containing guar or locust bean gums, with a composition comprising a mannanase comprising an amino acid sequence, which is at least 65% but less than 100% identical to SEQ ID NO: 1 , or which is at least 65% identical to SEQ ID NO: 2 or 3, as described herein.

[0155] Further, the present invention also refers to a method for improving wash performance of a cleaning composition on mannan-comprising stains, preferably containing guar or locust bean gums, glucomannan, and galactomannans, preferably containing guar or locust bean gums, comprising the step of formulating a mannanase as described herein in a cleaning composition.

[0156] Methods of use

[0157] The present invention is also directed to the use of at least one mannanase to increase the wash performance of a liquid cleaning composition towards a mannan-comprising stain in a washing or cleaning method, wherein the mannanase comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1 , or which is at least 65% identical to SEQ ID NO: 2 or 3, and wherein the washing or cleaning method comprises the step of contacting an object having a mannan-comprising stain with a liquid cleaning composition comprising the mannanase for 5-60 min, preferably 10-45 min, more preferably 15-40 min, more preferably for 15-30 min, most preferably for 15-25 min under conditions wherein the mannanase shows mannanase activity, preferably at a temperature in the range of 5-40°C, more preferably in the range of 10-40 °C, most preferably in the range of 20-30 °C. In one embodiment, the liquid cleaning composition under a) is a liquid cleaning composition comprising at least one mannanase, wherein the mannanase comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1, or which is at least 65% identical to SEQ ID NO: 2 or 3, as described herein, at least one biodegradable surfactant as described herein, and at least one biodegradable complexing agent as described herein.

[0158] Preferred embodiments

[0159] Particularly, preferred herein is:

[0160] 1 . A liquid cleaning composition comprising: a) at least one mannanase, wherein the mannanase

[0161] 1) comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1, or

[0162] 2) comprises an amino acid sequence which is at least 65% identical to SEQ ID NO: 2, or 3, b) at least one biodegradable surfactant, and c) at least one biodegradable complexing agent.

[0163] 2. A liquid cleaning composition according to embodiment 1 , comprising a) 0.00005-0.001 % (w / w), preferably 0.0001 -0.0005% (w / w) of the at least one mannanase, b) of 1-50% (w / w), preferably 5-25% (w / w) of the at least one biodegradable surfactant, and c) 0.1 -15% (w / w), preferably 0.05-5% (w / w), of the at least one biodegradable complexing agent.

[0164] 3. A composition according to any of embodiment 1 or 2, wherein the mannanase is a variant of a parent mannanase, wherein the mannanase variant comprises one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, 282, 318, 319, and 322, according to the numbering of SEQ ID NO: 1 , and an amino acid sequence which is at least 65%, but less than 100% identical to SEQ ID NO: 1.

[0165] 4. A composition according to embodiment 3, wherein the mannanase variant comprises an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical SEQ ID NO: 1.

[0166] 5. A composition according to embodiment 3 or 4, wherein the mannanase variant comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, X282Y, X318N, X319G, and X322G according to the numbering of SEQ ID NO: 1 .

[0167] 6. A composition according to any of embodiments 3 or 4, wherein the mannanase variant comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1.

[0168] 7. A composition according to embodiment 6, wherein the mannanase variant comprises or consists of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 and optionally additionally comprises 1-10, preferably 1-5 conservative amino acid substitutions. 8. A composition according to embodiment 7, wherein the mannanase consists of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 and optionally additionally comprises 1-10, preferably 1 -5 conservative amino acid substitutions.

[0169] 9. A composition according to embodiment 1 or 2, wherein the mannanase is a variant of a parent mannanase, wherein the mannanase variant comprises one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, and 282, according to the numbering of SEQ ID NO: 1 , and an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical to amino acids 1 -296 of SEQ ID NO: 1 .

[0170] 10. A composition according to embodiment 9, wherein the mannanase variant comprises at least one, at least two, at least three, at least four, at least five, or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, and X282Y according to the numbering of SEQ ID NO: 1.

[0171] 11. A composition according to any of embodiments 9 or 10, wherein the mannanase variant comprises at least one, at least two, at least three, at least four, at least five, or all amino acid substitutions selected from the group consisting of Q59V, N66D, A89H, E234Q, W259M, and N282Y according to the numbering of SEQ ID NO: 1.

[0172] 12. A composition according to embodiment 11 , wherein the mannanase variant comprises or consists of amino acids 1-296 of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, and N282Y, according to the numbering of SEQ ID NO: 1 and optionally additionally comprises 1 -10, preferably 1 -5 conservative amino acid substitutions.

[0173] 13. A composition according to embodiment 12, wherein the mannanase variant consists of amino acids 1 -296 of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, and N282Y, according to the numbering of SEQ ID NO: 1 and optionally additionally comprises 1-10, preferably 1-5 conservative amino acid substitutions.

[0174] 14. A composition according to any of embodiments 1 or 2, wherein the mannanase has an amino acid sequence which is at least 70%, preferably at least 72%, at least 74%, at least 75%, at least 76%, at least 78%, at least 80%, at least 82%, at least 84%, at least 85%, at least 86%, at least 88%, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or most preferably 100% identical to SEQ ID NO: 2.

[0175] 15. A composition according to any of embodiments 1 or 2, wherein the mannanase has an amino acid sequence which is at least 70%, preferably at least 72%, at least 74%, at least 75%, at least 76%, at least 78%, at least 80%, at least 82%, at least 84%, at least 85%, at least 86%, at least 88%, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or most preferably 100% identical to SEQ ID NO: 3.

[0176] 16. A composition according to any of embodiments 1 to 15, wherein the at least one biodegradable surfactant is selected from the group consisting of sodium alkyl ether sulfates, preferably sodium laureth sulfate, preferably sodium laureth sulfate +2 EO, alkyl polyglucosides, preferably alkyl polyglucoside C10-C16, and alcohol ethoxylates, preferably C12-C18 fatty alcohol + 7 EO.

[0177] 17. A composition according to embodiment 16, wherein the liquid composition comprises at least two of the biodegradable surfactants.

[0178] 18. A composition according to any of embodiments 16 or 17, wherein the liquid composition comprises at least three of the biodegradable surfactants.

[0179] 19. A composition according to any of embodiments 1 to 18, wherein the liquid composition comprises three biodegradable surfactants, wherein the surfactants are sodium laureth sulfate +2 EO, alkyl polyglucoside C10-C16, and C12-C18 fatty alcohol +7 EO.

[0180] 20. A composition according to any of embodiments 1 to 19, wherein the complexing agent is selected from the group consisting of EDDS, MGDA, GLDA, and citrate, preferably wherein the complexing agent is EDDS or citrate, more preferably wherein the complexing agent is EDDS.

[0181] 21. A composition according to embodiment 20, wherein the liquid composition comprises at least two of the complexing agents.

[0182] 22. A composition according to embodiment 21 , wherein the liquid composition comprises two complexing agents, wherein the complexing agents are EDDS and sodium citrate.

[0183] 23. The composition according to any of embodiments 1 to 22, wherein the composition comprises one or more further detergent components selected from the group consisting of secondary enzymes, enzyme stabilizing systems, defoamers, polymers, bleaching systems (bleach), rheology modifiers, hydrotropes, softening agents, desiccants, whitening agents, buffers, preservatives, anti-corrosion additives, dyestuff, and fragrances.

[0184] 24. The composition according to embodiment 23, wherein the one or more further detergent component is selected from the group consisting of polymers, preservatives, and secondary enzymes.

[0185] 25. The composition according to any of embodiments 23 or 24, wherein the secondary enzyme is selected from the group consisting of proteases, amylases, lipases, cellulases, mannanases, hemicellulases, phospholipases, esterases, cutinases, pectinases, lactases, peroxidases, xylanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, beta-glucanases, arabinosidases, hyaluronidases, chondroitinases, laccases, nucleases, DNase, phosphodiesterases, phytases, carbohydrases, galactanases, xanthanases, xyloglucanases, oxidoreductase, perhydrolases, aminopeptidase, asparaginases, carbohydrases, carboxypeptidases, catalases, chitinases, cyclodextrin glycosyltransferases, alpha-galactosidases, beta-galactosidases, glucoamylases, alpha-gluco- sidases, beta-glucosidases, invertases, ribonucleases, transglutaminases, and dispersins, preferably, the second enzyme is selected from the group consisting of proteases, amylases, lipases, cellulases, mannanases, xylanases, DNases, dispersins, pectinases, pectate lyases, glycosidases, and oxidoreductases, more preferably, the second enzyme is an amylase or protease, most preferably an amylase.

[0186] 26. The composition according to any of embodiments 1 to 25, wherein the composition comprises a) a mannanase as described herein, preferably in a concentration 0.00005-0.001 % (w / w), b) sodium laureth sulfate +2 EO, preferably in a concentration of 1 -5%, more preferably 2,8% (w / w), c) alkyl polyglucoside C10-C16, preferably in a concentration of 1-5%, more preferably 2% (w / w), d) C12-C18-fatty alcohol + 7 EO, preferably in a concentration of 10-15%, more preferably 12.5% (w / w), e) EDDS, preferably in a concentration of 0.01 -5%, more preferably 0.1 -2% (w / w) f) Coco fatty acid K12-18, preferably in a concentration of 1-10%, more preferably 5% (w / w), g) Na citrate 2H2O, preferably in a concentration of 1 -10%, more preferably 2-4% (w / w), h) Glycerol, preferably in a concentration of 1 -10%, more preferably 4-6% (w / w),

[0187] I) Ethanol, preferably in a concentration of 1 -10%, more preferably 4-6% (w / w) j) NaOH, preferably in a concentration of 1 -5%, more preferably 0.1-2% (w / w), k) Grafted maltodextrin (Bverde GP 790 L), preferably in a concentration of 1 -5%, more preferably 0.1 -2% (w / w) l) Water up to 95%. The composition according to any of embodiments 1 to 26, wherein the composition is devoid of non-biode- gradable surfactants and / or non-biodegradable complexing agents. The composition according to any of embodiments 1 to 27, wherein the composition is devoid of linear alkyl benzene sulfonates (LAS). A method of washing or cleaning comprising the steps of: a) providing a liquid cleaning composition containing a mannanase, wherein the mannanase

[0188] 1) comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1 , or

[0189] 2) comprises an amino acid sequence which is at least 65% identical to SEQ ID NO: 2, or 3, and b) contacting an object having a mannan-comprising stain with the liquid cleaning composition of (a) for 5-60 min, preferably 10-45 min, more preferably 15-40 min, more preferably for 15-30 min, most preferably for 15-25 min, under conditions wherein the mannanase shows mannanase activity. Use of at least one mannanase to increase wash performance of a liquid cleaning composition towards man- nan-comprising stains in a washing or cleaning method, wherein the washing or cleaning method comprises the steps of: a) providing a liquid cleaning composition containing a mannanase, wherein the mannanase

[0190] 1) comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1 , or

[0191] 2) comprises an amino acid sequence which is at least 65% identical to SEQ ID NO: 2, or 3, and b) contacting an object having a mannan-comprising stain with the liquid cleaning composition of (a) for 5-60 min, preferably 10-45 min, more preferably 15-40 min, more preferably for 15-30 min, most preferably for 15-25 min, under conditions wherein the mannanase shows mannanase activity. A method according to embodiment 29 or use according to embodiment 30, wherein the mannanase is a variant of a parent mannanase, wherein the mannanase variant comprises one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, 282, 318, 319, and 322, according to the numbering of SEQ ID NO: 1 , and an amino acid sequence which is at least 65%, but less than 100% identical to SEQ ID NO: 1. 32. A method or use according to embodiment 31 , wherein the mannanase variant comprises an amino acid se- quence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical SEQ ID NO: 1.

[0192] 33. A method or use according to any of embodiments 31 or 32, wherein the mannanase comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, X282Y, X318N, X319G, and X322G according to the numbering of SEQ ID NO: 1 .

[0193] 34. A method or use according to any of embodiments 31 to 33, wherein the mannanase variant comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1.

[0194] 35. A method or use according to embodiment 34, wherein the mannanase variant comprises or consists of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 and optionally additionally comprises 1-10, preferably 1-5 conservative amino acid substitutions.

[0195] 36. A method or use according to embodiment 35, wherein the mannanase variant consists of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 and optionally additionally comprises 1-10, preferably 1 -5 conservative amino acid substitutions.

[0196] 37. A method according to embodiment 29 or use according to embodiment 30, wherein the mannanase is a variant of a parent mannanase, wherein the mannanase variant comprises one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, and 282, according to the numbering of SEQ ID NO: 1 , and an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, or even more preferably at least 98% but less than 100% identical to amino acids 1 - 296 of SEQ ID NO: 1.

[0197] 38. A method or use according to embodiment 37, wherein the mannanase variant comprises at least one, at least two, at least three, at least four, at least five, or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, and X282Y according to the numbering of SEQ ID NO: 1.

[0198] 39. A method or use according to embodiment 38, wherein the mannanase variant comprises at least one, at least two, at least three, at least four, at least five, or all amino acid substitutions selected from the group consisting of Q59V, N66D, A89H, E234Q, W259M, and N282Y according to the numbering of SEQ ID NO: 1 .

[0199] 40. A method or use according to embodiment 39, wherein the mannanase variant comprises or consists of amino acids 1-296 of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, and N282Y, according to the numbering of SEQ ID NO: 1 and optionally additionally comprises 1-10, preferably 1 -5 conservative amino acid substitutions. 41. A method or use according to embodiment 40, wherein the mannanase variant consists of amino acids 1 -296 of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, and N282Y, accord- ing to the numbering of SEQ ID NO: 1 and optionally additionally comprises 1 -10, preferably 1 -5 conservative amino acid substitutions.

[0200] 42. A method according to embodiment 29 or use according to embodiment 30, wherein the mannanase has an amino acid sequence which is at least 70%, preferably at least 72%, at least 74%, at least 75%, at least 76%, at least 78%, at least 80%, at least 82%, at least 84%, at least 85%, at least 86%, at least 88%, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or most preferably 100% identical to SEQ ID NO: 2.

[0201] 43. A method according to embodiment 29 or use according to embodiment 30, wherein the mannanase has an amino acid sequence which is at least 70%, preferably at least 72%, at least 74%, at least 75%, at least 76%, at least 78%, at least 80%, at least 82%, at least 84%, at least 85%, at least 86%, at least 88%, at least 90%, at least 92%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or most preferably 100% identical to SEQ ID NO: 3.

[0202] 44. A method according to any of embodiments 29, and 31 to 43 or use according to any of embodiments 30 to 43, wherein step b) is performed for 5 min, 6 min, 7 min, 8 min, 9 min, 10 min, 1 1 min, 12 min, 13 min, 14 min, 15 min, 16 min, 17 min, 18 min, 19 min, 20 min, 21 min, 22 min, 23 min, 24 min, 25 min, 26 min, 27 min, 28 min,

[0203] 29 min, 30 min, 31 min, 32 min, 33 min, 34 min, 35 min, 36 min, 37 min, 38 min, 39 min, 40 min, 41 min, 42 min, 43 min, 44 min, 45 min, 46 min, 47 min, 48 min, 49 min, 50 min, 51 min, 52 min, 53 min, 54 min, 55 min,

[0204] 56 min, 57 min, 58 min, 59 min or 60 min, preferably, step b) is performed for 10 min, 1 1 min, 12 min, 13 min, 14 min, 15 min, 16 min, 17 min, 18 min, 19 min, 20 min, 21 min, 22 min, 23 min, 24 min, 25 min, 26 min, 27 min, 28 min, 29 min, 30 min, 31 min, 32 min, 33 min, 34 min, 35 min, 36 min, 37 min, 38 min, 39 min, 40 min,

[0205] 41 min, 42 min, 43 min, 44 min, or 45 min, more preferably step b) is performed for 15 min, 16 min, 17 min, 18 min, 19 min, 20 min, 21 min, 22 min, 23 min, 24 min, 25 min, 26 min, 27 min, 28 min, 29 min, 30 min, 31 min, 32 min, 33 min, 34 min, 35 min, 36 min, 37 min, 38 min, 39 min, or 40 min, more preferably step b) is performed for 15 min, 16 min, 17 min, 18 min, 19 min, 20 min, 21 min, 22 min, 23 min, 24 min, 25 min, 26 min, 27 min, 28 min, 29 min or 30 min, most preferably step b) is performed for 15 min, 16 min, 17 min, 18 min, 19 min, 20 min, 21 min, 22 min, 23 min, 24 min, or 25 min.

[0206] 45. A method according to any of embodiments 29, and 31 to 44 or use according to any of embodiments 30 to 44, wherein step b) is performed at a temperature in the range of 5-40°C, preferably in the range of 10-40 °C, most preferably in the range of 20-30 °C.

[0207] 46. A method according to any of embodiments 29, and 31 to 45 or use according to any of embodiments 30 to 45, wherein step b) is performed at 5°C, 6°C, 7°C, 8°C, 9°C, 10°C, 1 1 °C, 12°C, 13°C, 14°C, 15°C, 16°C, 17°C, 18°C, 19°C, 20°C, 21 °C, 22°C, 23°C, 24°C, 25°C, 26°C, 27°C, 28°C, 29°C, 30°C, 31 °C, 32°C, 33°C, 34°C, 35°C, 36°C, 37°C, 38°C, 39°C or 40 °C, preferably, step b) is performed at 10°C, 1 1 °C, 12°C, 13°C, 14°C, 15°C, 16°C, 17°C, 18°C, 19°C, 20°C, 21 °C, 22°C, 23°C, 24°C, 25°C, 26°C, 27°C, 28°C, 29°C, 30°C, 31 °C, 32°C, 33°C, 34°C, 35°C, 36°C, 37°C, 38°C, 39°C or 40 °C, more preferably, step b) is performed at 20°C, 21 °C, 22°C, 23°C, 24°C, 25°C, 26°C, 27°C, 28°C, 29°C, or 30°C, most preferably step b) is performed at 20°C.

[0208] 47. A method according to any of embodiments 29, and 31 to 46 or use according to any of embodiments 30 to 46, wherein step b) is performed for 20-25 min at 20°C or 40°C, preferably, wherein step b) is performed for 20-25 min at 20°C.

[0209] 48. A method according to any of embodiments 29, or 31 to 47, or use according to any of embodiments 30 to 47, wherein the liquid cleaning composition further comprises at least one additional detergent component selected from the group consisting of surfactants, builders, polymers, preservatives, and second enzymes different to the mannanase.

[0210] 49. A method according to any of embodiments 29, or 44 to 48, or use according to any of embodiments 30, or 44 to 48, wherein the liquid cleaning composition of a) is the liquid cleaning composition according to any of embodiments 1 to 28.

[0211] 50. A method according to embodiment 49, or use according to embodiment 49, wherein the liquid cleaning composition is dosed to obtain a concentration of the a) at least one mannanase in the range of 0.0000001 to 0.001 g / l wash sud, preferably 0.000001 to 0.0001 g / i b) at least one biodegradable surfactant in the range of 0.015 to 1 .5 g / l, preferably 0.015-0.75 g / l and c) at least one biodegradable complexing agent in the range of 0.0015 to 0.45 g / l, preferably 0.0015-0.225 g / l.

[0212] 51 . A method according to any of embodiments 29, or 31 to 49, or use according to any of embodiments 30 to 49, wherein the object is a textile or a dishware, preferably a textile.

[0213] Examples

[0214] Example 1 : Wash performance in Launder-o-meter (LOM) at 25 °C and 40 °C

[0215] Several solid swatches including relevant mannanase responsive stains were washed together with cotton ballast fabric and 20 steel balls at 25 and 40 °C in a liquid laundry formulation (see Table 1). Different selected mannanases (SEQ ID NO: 1 comprising the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 (Mani ), SEQ ID NO: 2 (Man2), SEQ ID NO: 3 (Man3), SEQ ID NO: 4 (Man4), and SEQ ID NO: 5 (Man5)) were supplemented into the wash liquor. Each stain was washed in duplicates.

[0216] Table 1: Washing conditions in Launder-o-meter (LOM)

[0217] 1> Producer: Center for Testmaterials BV, NL-3130 AC Vlaardingen

[0218] After the wash, the fabrics were rinsed, spin-, and air-dried. The washing performance was determined by measuring the CIELab values of the soiled fabrics before and after wash using the MACH5 multi area color measurement. For data evaluation, AE was calculated between unwashed and washed stains and AAE was calculated between detergent with enzymes and detergent without enzymes (see Table 2). The data represent average values of two external and two internal replicates.

[0219] Table 2: Wash performance in AAE of different mannanases in the LOM at 25 and 40 °C shown as sum over both stains CS-43 and CS-73

[0220] Over a range of different enzyme concentrations but especially also in the lower concentration ranges, Mani , Man2 and Man3, show superior wash performance in the LOM over Man4 and Man5. This advantageous effect is lost, meaning all tested mannanases achieve comparable results, in a full-length wash cycle (data not shown).

[0221] Example 2: Full-scale wash performance in express wash cycle at 40 °C

[0222] Several multi soil monitors including different technical stains as well as complex food-based stains responsive to mannanases, were washed using a short wash cycle program in a full-scale washing machine in presence of cotton ballast fabric. A short wash cycle program of approximately 20 mins was selected and the temperature selection was adjusted to 40 °C. The wash liquor was supplemented with liquid laundry formulation and different mannanase enzymes (SEQ ID NO: 1 comprising the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 (Mani), SEQ ID NO: 2 (Man2), SEQ ID NO: 3 (Man3), SEQ ID NO: 4 (Man4), SEQ ID NO: 5 (Man5)) as displayed in Table 3. Two identical machine loadings were set up and each washing machine was loaded with two copies of each stain. Table 3: Washing conditions in full scale washing machines

[0223] 1) Producer: Center for Testmaterials BV, NL-3130 AC Vlaardingen

[0224] After the wash, the fabrics were air-dried. The washing performance was quantified by measuring CIE Lab values of the soiled fabrics before and after wash using the MACH5 multi area color measurement. For data evaluation, mean values were determined over all four copies of each stain, AE was calculated as difference between unwashed and washed stains and AAE was calculated as difference between detergent with enzymes to detergent without enzymes. Table 4 displays the wash performance of Man2, 3, 4 and 5 in comparison to Mani (ManX minus Mani). This means that the more negative the value, the greater the difference to Mani .

[0225] Table 4: Wash performance of different mannanases in comparison to Mani in express wash cycle at 40 °C.

[0226] Mani , Man2 and Man3 show superior wash performance over Man4 and Man5 in a short wash cycle (20 mins) at 40 °C. Mani overall shows the best wash performance under test conditions. Example 3: Wash performance in express wash cycle at 20 °C

[0227] Several multi soil monitors including different technical stains as well as complex food-based stains responsive to mannanase, were washed in a full-scale washing machine in presence of cotton ballast fabric. A short wash cycle program of approximately 20 mins was selected and the temperature selection was adjusted to 20 °C. The wash liq- uor was supplemented with liquid laundry formulation and different mannanase enzymes (SEQ ID NO: 1 comprising the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 (Mani ), SEQ ID NO: 2 (Man2), SEQ ID NO: 3 (Man3), SEQ ID NO: 4 (Man4), SEQ ID NO: 5 (Man5)) as displayed in Table 5. Two identical machine loadings were set up and each washing machine was loaded with two copies of each stain. Table 5: Washing conditions in full scale washing machines

[0228] After the wash, the fabrics were air-dried. The washing performance was quantified by measuring CIE Lab values of the soiled fabrics before and after wash using the MACH5 multi area color measurement. For data evaluation mean values were determined over all four copies of each stain, AE was calculated as difference between unwashed and washed stains and AAE was calculated as difference between detergent with enzymes and detergent without enzymes. Table 6 displays the wash performance of Man2, 3, 4 and 5 in comparison to Mani (ManX minus Mani). This means that the more negative the value, the greater the difference to Mani . Table 6: Wash performance of different mannanases in express wash cycle at 20 °C, indicated as difference of Man2, Man3, Man4 and Man5 versus Mani.

[0229] Mani , Man2 and Man3 also show superior wash performance over Man4 and Man5 in a short wash cycle (20 mins) at 20 °C. Mani overall shows the best wash performance under test conditions.

[0230] From Example 1 , 2 and 3 it can be concluded that Mani , Man2 and Man3 overall show superior wash performance when using shorter wash cycles even at lower temperatures (20 °C).

[0231] Example 4: Wash performance in express wash cycle at 40 °C and 20 °C over comprehensive stain set Several multi soil monitors including 19 different stains responsive to mannanase, were washed in a full-scale washing machine in presence of cotton ballast fabric. A short wash cycle program of approximately 20 mins was selected and the temperature selection was adjusted to 40 °C or 20 °C. The wash liquor was supplemented with liquid laundry formulation and different mannanase enzymes (SEQ ID NO: 1 comprising the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 (Mani), SEQ ID NO: 2 (Man2), SEQ ID NO: 3 (Man3), SEQ ID NO: 4 (Man4), SEQ ID NO: 5 (Man5)) as displayed in Table 7. Two identical machine loadings were set up and each washing machine was loaded with two copies of each stain.

[0232] Table 7: Washing conditions in full scale washing machines

[0233] After the wash, the fabrics were air-dried. The washing performance was quantified by measuring CIE Lab values of the soiled fabrics before and after wash using the MACH5 multi area color measurement. For data evaluation mean values were determined over all four copies of each stain, AE was calculated as difference between unwashed and washed stains and AAE was calculated as difference between detergent with enzymes and detergent without enzymes. Table 8 displays the wash performance of Man2, 3, 4 and 5 in comparison to Mani (ManX minus Mani). This means that the more negative the value, the greater the difference to Mani .

[0234] Table 8: Wash performance of different mannanases in express wash cycle at 40 °C and 20 °C over a broad variety of stains. Data indicated as difference of Man2, Man3, Man4 and Man5 versus Mani.

[0235] Mani , Man2 and Man3 show superior wash performance over Man4 and Man5 in a short wash cycle (20 mins) at 20 °C and 40 °C over a broad stain set.

[0236] Example 5: Wash performance in sustainable cleaning composition with conventional dosage

[0237] Several multi soil monitors including different technical stains as well as complex food-based stains responsive to mannanase, were washed with a sustainable detergent in a full-scale washing machine in presence of cotton ballast fabric. A short was cycle program of approximately 20 min was selected and temperature selection adjusted to either 40 °C or 20°C. The wash liquor was supplemented with a sustainable liquid laundry formulation with conventional dosage (3.3 g / l) and different mannanase enzymes (SEQ ID NO: 1 comprising the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 (Mani), SEQ ID NO: 2 (Man2), SEQ ID NO: 3 (Man3), SEQ ID NO: 4 (Man4), SEQ ID NO: 5 (Man5)) as displayed in Table 9. Two identical machine loadings were set up and each washing machine was loaded with two copies of each stain. Table 9: Washing conditions for tests at conventional detergent dosage

[0238] After the wash, the fabrics were air-dried. The washing performance was quantified by measuring CIE Lab values of the soiled fabrics before and after wash using the MACH5 multi area color measurement. For data evaluation mean values were determined over all four copies of each stain, AE was calculated as difference of unwashed to washed stains and AAE was calculated as difference of detergent with enzymes to detergent without enzymes.

[0239] Table 10 displays the wash performance of Man2, 3, 4 and 5 in comparison to Mani (ManX minus Mani). This means that the more negative the value, the greater the difference to Mani .

[0240] Table 10: Wash performance in a short wash cycle at 40 °C and 20°C using a sustainable detergent dosed at 3.3 g / l. Data represent the performance difference of Man2, Man3, Man4 and Man5 versus Mani over the whole stain set.

[0241] Mani , Man2 and Man3 show superior wash performance over Man4 and Man5 in a short wash cycle using a sustainable detergent. Mani overall shows the best wash performance under test conditions.

[0242] Example 6: Wash performance in sustainable cleaning composition with reduced dosage Several multi soil monitors including different technical stains as well as complex food-based stains responsive to mannanase, were washed with a sustainable detergent in a full-scale washing machine in presence of cotton ballast fabric. A short was cycle program of approximately 20 min was selected and temperature selection adjusted to either 40 °C or 20°C. In this example, the wash liquor was supplemented with a sustainable liquid laundry formulation with reduced dosage (1.7 g / l) and different mannanase enzymes (SEQ ID NO: 1 comprising the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID

[0243] NO: 1 (Mani ), SEQ ID NO: 2 (Man2), SEQ ID NO: 3 (Man3), SEQ ID NO: 4 (Man4), SEQ ID NO: 5 (Man5)) as displayed in Table 1 1 . Each washing machine was loaded with two copies of each stain and two identical machine loadings were set up.

[0244] Table 11 : Washing conditions for tests at reduced detergent dosage After the wash, the fabrics were air-dried. The washing performance was quantified by measuring CIE Lab values of the soiled fabrics before and after wash using the MACH5 multi area color measurement. For data evaluation mean values were determined over all four copies of each stain, AE was calculated as difference of unwashed to washed stains and AAE was calculated as difference of detergent with enzymes to detergent without enzymes.

[0245] Table 12 displays the wash performance of Man2, 3, 4 and 5 in comparison to Mani (ManX minus Mani). This means that the more negative the value, the greater the difference to Mani .

[0246] Table 12: Wash performance in short wash cycle at 40 °C and 20°C using a sustainable detergent dosed at

[0247] 1.7 g / l. Data represent the performance difference of Man2, Man3, Man4 and Man5 versus Mani over the whole stain set.

[0248] Mani , Man2 and Man3 show superior wash performance over Man4 and Man5 in a short wash cycle using a sustainable detergent, even at low dose.

Claims

CLAIMS1 . A liquid cleaning composition comprising: a) at least one mannanase, wherein the mannanase1) comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1, or2) comprises an amino acid sequence which is at least 65% identical to SEQ ID NO: 2, or 3, b) at least one biodegradable surfactant, and c) at least one biodegradable complexing agent.

2. The composition according to claim 1, wherein the mannanase a) is a variant of a parent mannanase, wherein the mannanase variant comprises1) one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, 282, 318, 319, and 322, according to the numbering of SEQ ID NO: 1 , and an amino acid sequence which is at least 65%, but less than 100% identical to SEQ ID NO: 1 , or2) one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, and 282, according to the numbering of SEQ ID NO: 1 , and an amino acid sequence which is at least 65%, but less than 100% identical to amino acids 1 - 296 of SEQ ID NO: 1 , or wherein the mannanase b) has an amino acid sequence which is at least 70%, preferably at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or even more preferably 100% identical to SEQ ID NO: 2 or SEQ ID NO: 3.

3. The composition according to claim 2, wherein the mannanase variant under option a) 1) comprises at least one, at least two, at least three, at least four, at least five, at least six, at least seven, at least eight or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, X282Y, X318N, X319G, and X322G according to the numbering of SEQ ID NO: 1 and an amino acid sequence which is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or even more preferably at least 98% but less than 100% identical SEQ ID NO: 1 or wherein the mannanase variant under option a) 2) comprises at least one, at least two, at least three, at least four, at least five, or all amino acid substitutions selected from the group consisting of X59V, X66D, X89H, X234Q, X259M, and X282Y according to the numbering of SEQ ID NO: 1 and an amino acid sequencewhich is at least 65%, preferably at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or even more preferably at least 98% but less than 100% identical to amino acids 1 -296 of SEQ ID NO: 1.

4. The composition according to any of the previous claims, wherein the mannanase is a variant comprising or consisting of SEQ ID NO: 1 with the amino acid substitutions Q59V, N66D, A89H, E234Q, W259M, N282Y, T318N, E319G, and S322G according to the numbering of SEQ ID NO: 1 or wherein the mannanase comprises or consists of the amino acid sequence of SEQ ID NO: 2 or wherein the mannanase comprises or consists of the amino acid sequence of SEQ ID NO: 3.

5. The composition according to any of the preceding claims, wherein the surfactant is selected from the group consisting of sodium alkyl ether sulfates, preferably sodium laureth sulfate +2 EQ, alkyl polyglucosides, preferably alkyl polyglucoside C10-C16, and alcohol ethoxylates, preferably C12-C18 fatty alcohol +7 EQ.

6. The composition according to any of the preceding claims, wherein the liquid composition comprises at least two biodegradable surfactants, wherein the surfactants are selected from the group consisting of sodium alkyl ether sulfates, preferably sodium laureth sulfate +2 EQ, alkyl polyglucosides, preferably alkyl polyglucoside C10-C16, and alcohol ethoxylates, preferably C12-C18 fatty alcohol +7 EQ.

7. The composition according to any of the preceding claims, wherein the complexing agent is selected from the group consisting of EDDS, MGDA, GLDA, and citrate, preferably wherein the complexing agent is EDDS or citrate, more preferably EDDS.

8. The composition according to any of the preceding claims, wherein the composition is devoid of linear al kyl benzene sulfonates (LAS).

9. The composition according to any of the preceding claims, wherein the composition further comprises an antimicrobial agent selected from the group consisting of 2-phenoxyethanol and 4,4’-dichloro 2-hydroxydiphe- nylether, preferably comprising phenoxyethanol in an amount ranging from 2 ppm to 5% by weight of the composition, more preferably comprising 0.1 to 2% of phenoxyethanol by weight of the composition and / or preferably comprising 4, 4’ -dichloro 2-hydroxydiphenylether in a concentration from 0.001 to 3%, preferably 0.002 to 1 %, more preferably 0.01 to 0.6%, each by weight of the composition.

10. A method of washing or cleaning comprising the steps of: a) providing a liquid cleaning composition containing a mannanase, wherein the mannanase1) comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1 , or2) comprises an amino acid sequence which is at least 65% identical to SEQ ID NO: 2, or 3, andb) contacting of an object having a mannan-comprising stain with the liquid cleaning composition of a) for 5-60 min, preferably 10-45 min, more preferably 15-40 min, more preferably for 15-30 min, most preferably for 15-25 min under conditions wherein the mannanase shows mannanase activity.

11. The method according to claim 10, a) wherein the mannanase is a variant of a parent mannanase, wherein the mannanase variant comprises1) one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, 282, 318, 319, and 322, according to the numbering of SEQ ID NO: 1 , and an amino acid sequence which is at least 65%, but less than 100% identical to SEQ ID NO: 1 , or2) one or more amino acid substitutions at positions selected from the group consisting of 59, 66, 89, 234, 259, and 282, according to the numbering of SEQ ID NO: 1 , and an amino acid sequence which is at least 65%, but less than 100% identical to amino acids 1 - 296 of SEQ ID NO: 1 , or b) wherein the mannanase has an amino acid sequence which is at least 70%, preferably at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or even more preferably 100% identical to SEQ ID NO: 2 or SEQ ID NO: 3.

12. The method according to any of claims 10 or 11 , wherein step (b) is performed at a temperature in the range of 5-40°C, preferably in the range of 10-35 °C, most preferably in the range of 20-30 °C.

13. The method according to any of claims 10 to 12, wherein the liquid cleaning composition of a) is according to any of claims 1 to 8, and wherein the liquid cleaning composition is dosed to obtain a concentration of the a) at least one mannanase in the range of 0.0000001 to 0.001 g / l wash sud, preferably 0.000001 to 0.0001 g / l b) at least one biodegradable surfactant in the range of 0.015 to 1 .5 g / l, preferably 0.015-0.75 g / l and c) at least one biodegradable complexing agent in the range of 0.0015 to 0.45 g / l, preferably 0.0015- 0.225 g / l.

14. The method according to any of claims 10 to 13, wherein the object is a textile or a dishware, preferably a textile.

15. Use of at least one mannanase to increase wash performance of a liquid cleaning composition towards a mannan-comprising stain in a washing or cleaning method, wherein the washing or cleaning method comprises the steps of: a) providing a liquid cleaning composition containing a mannanase, wherein the mannanase1) comprises an amino acid sequence which is at least 65% but less than 100% identical to SEQ ID NO: 1, or2) comprises an amino acid sequence which is at least 65% identical to SEQ ID NO: 2, or 3, and b) contacting an object having a mannan-comprising stain with the liquid cleaning composition of a) for 5-60 min, preferably 10-45 min, more preferably 15-40 min, more preferably for 15-30 min, most preferably for 15-25 min under conditions wherein the mannanase shows mannanase activity, preferably at a temperature in the range of 5-40°C, more preferably in the range of 10-40 °C, most preferably in the range of 20-30 °C.

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