Stable mannanase for blends

Abstract

This invention relates to variants of mannanase enzyme. The variants are useful in industrial applications wherein degradation or modification of mannan is desired, such as in laundry and cleaning applications, in feed, food, pulp and paper and oil industry. The invention also provides useful mannanases enzymes, polynucleotides encoding these enzymes, enzyme compositions and methods for their production and use.

Description

BASF SE 240828W0011 B19118WOStable mannanase for blendsField of the inventionThis invention relates to variants of a mannanase enzyme. The variants are useful in industrial applications wherein degradation or modification of mannan is desired, such as in laundry and cleaning applications, in feed, food, pulp and paper and oil industry. The invention also provides polynucleotides encoding the mannanase variants, compositions comprising these variants and methods for their production and use.Background of the inventionThe main role of hemicelluloses and galactomannans is to function as structural polysaccharide and / or as reserve energy. Besides amylose and amylopectin which are the most widespread storage polysaccharides in plants, there is a diverse group of mannan-based polysaccharides found in seeds, roots, bulbs and tubers of various plants. These include mannans, galactomannans and glucomannans.Mannans are polysaccharides with a backbone of B-1 ,4-linked D-mannopyranosyl residues. In most cases the mannans are highly insoluble in water but have high water binding capacity. In contrast to unsubstituted mannans, the galactomannans are water soluble. Due to the complex structural composition of the plant cell wall, microorganisms thriving on decaying plant material must possess a number of different enzymes that are able to hydrolyse these highly polymeric and mostly insoluble materials. The two major endoacting enzymes involved in degradation of hemicelluloses are beta-mannanase and beta-xylanase. In addition, the exoacting enzymes beta-mannosidase, alpha-galactosidase and beta-glucosidase are needed for complete degradation of galactoglucomannan.The main enzyme type participating in the degradation of mannan backbones are endo-1,4-beta-mannanases (EC 3.2.1 .78), which hydrolyze the internal glycoside bonds in the mannan backbone. Endo-1 ,4-B-mannanases (EC 3.2.1 .78) are mannan-degrading enzymes which may be called endo-B-1,4-D-mannanase, B-mannanase, or mannanase herein. Since endo-1,4-beta-mannanases (EC 3.2.1.78) degrade the mannan-backbone, mannan-degradation includes the degradation of mannans, galactomannans and / or glucomannans.The use of mannanase enzymes is widespread in food and feed applications, the detergent, and the pulp and paper industry:• The use of mannanase enzymes as feed additives has been shown to provide several beneficial effects since mannan is a contributing factor to viscosity of gut contents and it thereby adversely affects the feed digestibility and animal growth rate.• In the food industry mannanase enzymes are described for the use in the production of instant coffee where the enzyme reduces the viscosity of the coffee extracts due to hydrolysis of the coffee mannan. Further, mannanases are used to produce specific mannooligomers that are of interest as functional food ingredients such as mannooligomers with a prebiotic functionality. In such applications plant-derived mannopolymers are subjected to hydrolysis by mannanases.• It is common to use mannanases in the processing and manufacturing fruit juice because they lower viscosity and improve filtration rate, stability and help to extract fruit components.• Detergent use: mannanases facilitate the removal of food and cosmetic derived stains / soils that often comprise mannan containing additives like stabilizers, emulsifiers and thickeners. In a more specific cleaning application mannanases are applied to remove biofilms from surfaces or tubings that need to be free from microbials likeBASF SE 240828W0012 B19118WO pharmaceutical equipment. In this application mannanases are often used in combination with detergents and other enzymes like carbohydrases and proteases.• Pulp and paper: mannanases are used in the enzyme-aided bleaching of paper pulp. Mannanases are said to complement the action of xylanases.• Mannanases are applied in the process of oil and gas well stimulation by hydraulic fracturing. Mannanases reduce viscosity of a guar solution that is applied in the process.• Mannanases are used in the controlled release of drugs or other material from matrices that are composed of cross-linked galactomannans.Activity under application conditions is a critical parameter for many industrially applied enzymes, since these enzymes often tend to be insufficiently active under application conditions, for example in a blend with other enzymes such as proteases. Therefore, it was an objective of the present invention to find mannanase variants with improved performance especially after storage of the same over a certain period of time in combination with a protease.The mannanase variants of the invention are advantageous in having good stability and mannanase activity. Further, the mannanase variants of the invention may provide improved yield in production and better performance in use.Brief summary of the inventionThe present invention is directed to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1. The present invention further relates to a polynucleotide encoding said variant polypeptide and a composition comprising said variant polypeptide.Detailed description of the inventionThe 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.Although the present invention will be described with respect to particular embodiments, this description is not to be construed in a limiting sense.DefinitionsUnless otherwise noted, the terms used herein are to be understood according to conventional usage by those of ordinary skill in the relevant art.Before describing in detail exemplary embodiments of the present invention, definitions important for understanding the present invention are given. Unless stated otherwise or apparent from the nature of the definition, the definitions apply to all compounds, methods and uses described herein.As used in this specification and in the appended claims, the singular forms of "a" and "an" also include the respective plurals unless the context clearly dictates otherwise.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 indicatesBASF SE 240828W0013 B19118WO a deviation from the indicated numerical value of ±20 %, preferably ±15 %, more preferably ±10 %, and even more preferably ±5 %.Furthermore, the terms "first", "second", "third" or "(a)", "(b)", "(c)", "(d)" etc. and the like in the description and in the claims, are used for distinguishing between similar 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.Throughout this application, various publications are referenced. The disclosure of all of these publications and those references cited within those publications in their entireties are hereby incorporated by reference into this application in order to more fully describe the state of the art to which this invention pertains.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.“Amino acid substitutions” are described by providing the original amino acid followed by the number of the position within the amino acid sequence, followed by the substituted 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 in the variant without specifying the amino acid of the parent at this position, e.g., by using “X120A” or “120A” or “Xaa120Ala” or “120Ala”.Variants comprising multiple substitutions are separated by “+”, e.g., “Arg170Tyr+Gly195Glu”, “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 substitutions may be separated by space or a comma, e.g., “R170Y G195E” or “R170Y, G195E” respectively. Where different alternative substitutions can be introduced at a position, the different substitutions 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 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}”.The term “native” (or naturally or wild-type or endogenous) cell or organism or polynucleotide or polypeptide refers to the cell or organism or polynucleotide or polypeptide as found in nature (i.e., without there being any human intervention).The term "heterologous” (or exogenous or foreign or recombinant or non-native or non-natural) polypeptide is defined herein as a polypeptide that is not native to the host cell, a polypeptide native to the host cell in which structural modifications, e.g., deletions, substitutions, and / or insertions, have been made by recombinant DNA techniques to alter the native polypeptide, or a polypeptide native to the host cell whose expression is quantitatively altered or whose expression is directed from a genomic location different from the native host cell as a result of manipulation of the DNA of the host cell by recombinant DNA techniques, e.g., a stronger promoter. Similarly, the term “heterologous” (or exogenous or foreign or recombinant or non-native or non-natural) polynucleotide refers to a polynucleotide that is notBASF SE 240828W0014 B19118WO native to the host cell, a polynucleotide native to the host cell in which structural modifications, e.g., deletions, substitutions, and / or insertions, have been made by recombinant DNA techniques to alter the native polynucleotide, or a polynucleotide native to the host cell whose expression is quantitatively altered as a result of manipulation of the regulatory elements of the polynucleotide by recombinant DNA techniques, e.g., a stronger promoter, or a polynucleotide native to the host cell, but integrated not within its natural genetic environment as a result of genetic manipulation by recombinant DNA techniques. With respect to the relation between two or more polynucleotide sequences or the relation between two or more amino acid sequences, the term "heterologous” is used to characterize that the two or more polynucleotide sequences or two or more amino acid sequences are naturally not occurring in the specific combination with each other.For the purpose of the invention, "recombinant" (or transgenic) with regard to a cell or an organism means that the cell or organism contains a heterologous polynucleotide, which is introduced by man using gene technology. With regard to a polynucleotide “recombinant” includes all constructs produced by using gene technology / recombinant DNA techniques in which either(a) the sequence of the polynucleotide or a part thereof, or(b) one or more genetic control sequences, which are operably linked to the polynucleotide, including but not limited to a promoter, or(c) both a) and b) are not located in their wild-type genetic environment or have been modified by man.A "synthetic" compound is obtained by in vitro chemical and / or enzymatic synthesis.Variant polynucleotide and variant polypeptide sequences may be defined by their sequence identity when compared to a parent sequence. Sequence identity usually is 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, which 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, with 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 matrix=EBLOSUM62). After aligning two sequences, in a second step, an identity value is determined from the alignment produced. 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.A special aspect concerning amino acid substitutions are conservative mutations which often appear to have a minimal effect on protein folding resulting in substantially maintained enzyme properties of the respective enzyme variant compared to the enzyme properties of the parent enzyme. Conservative mutations are those where one amino acid is exchanged with a similar amino acid. Such an exchange most probably does not change enzyme properties. Herein the following conservative exchanges are considered:Amino acid A is similar to amino acids SBASF SE 240828W0015 B19118WOAmino acid D is similar to amino acids E; NAmino acid E is similar to amino acids D; K; QAmino acid F is similar to amino acids W; Y Amino acid H is similar to amino acids N; Y Amino acid I is similar to amino acids L; M; V Amino acid K is similar to amino acids E; Q; R Amino acid L is similar to amino acids I; M; V Amino acid M is similar to amino acids I; L; V Amino acid N is similar to amino acids D; H; S Amino acid Q is similar to amino acids E; K; R Amino acid R is similar to amino acids K; Q Amino acid S is similar to amino acids A; N; T Amino acid T is similar to amino acids S Amino acid V is similar to amino acids I; L; M Amino acid W is similar to amino acids F; Y Amino acid Y is similar to amino acids F; H; WConservative amino acid substitutions may occur over the full length of the sequence of a polypeptide sequence of a functional protein such as an enzyme. Preferably, such mutations are not pertaining the functional domains of an enzyme, more preferably conservative mutations are not pertaining the catalytic centers of an enzyme.The variant polypeptide of the present invention may comprise a deletion of one or more amino acids at the N terminus and / or the C terminus of the polypeptide and essentially retain mannanase activity. Preferably, the variant polypeptide of the present invention comprises 100 to 400 or 150 to 400 or 200 to 400 or 250 to 400 or 100 to 350 or 150 to 350 or 200 to 350 or 100 to 300 or 150 to 300 or 200 to 300 or 250 to 300 amino acids aligning with corresponding amino acids of the polypeptide as set forth in SEQ ID NO: 1. More preferably, the variant polypeptide of the present invention comprises amino acids aligning with corresponding amino acids 1 to 299 of the polypeptide as set forth in SEQ ID NO: 1 . Also preferably, the variant polypeptide of the present invention comprises 100 to 400 or 150 to 400 or 200 to 400 or 250 to 400 or 100 to 350 or 150 to 350 or 200 to 350 or 100 to 300 or 150 to 300 or 200 to 300 or 250 to 300 amino acids aligning with corresponding amino acids of the polypeptide as set forth in SEQ ID NO: 1. More preferably, the variant polypeptide of the present invention comprises consecutive amino acids aligning with corresponding amino acids 1 to 400 or 1 to 380 or 1 to 360 or 1 to 340 or 1 to 330 or 1 to 320 or 1 to 310 or 1 to 300 located at the N terminus of the polypeptide as set forth in SEQ ID NO: 1. Most preferably, the variant polypeptide of the present invention comprises consecutive amino acids aligning with amino acids 1 to 299 located at the N terminus of the polypeptide as set forth in SEQ ID NO: 1. Also preferably, the variant polypeptide of the present invention retains at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 98.5 %, at least 99%, at least 99.5% or at least 100% of the enzyme activity of the polypeptide as set forth in SEQ ID NO: 1 .BASF SE 240828W0016 B19118WOIn one embodiment, the polypeptide of the present invention does not comprise any internal deletions compared to the amino acid sequence according to SEQ ID NO: 1. However, as discussed above, the polypeptide of the present invention may comprise a deletion of one or more amino acids at the N terminus and / or the C terminus of the polypeptide.“Genetic construct” or “expression cassette” as used herein, is a nucleic acid molecule composed of at least one sequence of interest to be expressed, operably linked to one or more control sequences (at least to a promoter) as described herein.The term “vector” as used herein comprises any kind of construct suitable to carry foreign polynucleotide sequences for transfer to another cell, or for stable or transient expression within a given cell. The term “vector” as used herein encompasses any kind of cloning vehicles, such as but not limited to plasmids, phagemids, viral vectors (e.g., phages), bacteriophage, baculoviruses, cosmids, fosmids, artificial chromosomes, and any other vectors specific for specific hosts of interest. Foreign polynucleotide sequences usually comprise a coding sequence which may be referred to herein as “gene of interest”. The gene of interest may comprise introns and exons, depending on the kind of origin or destination of host cell.The term “introduction of a polynucleotide” or “transformation of a polynucleotide” as referred to herein encompasses the transfer of an exogenous polynucleotide into a host cell, irrespective of the method used for transfer. That is, the term “transformation of a polynucleotide” as used herein is independent from vector, shuttle system, or host cell, and it not only relates to the polynucleotide transfer method of transformation as known in the art (cf., for example, Sambrook, J. et al. (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY), but it encompasses any further kind of polynucleotide transfer methods such as, but not limited to, transduction or transfection.A polynucleotide encoding a polypeptide may be “expressed”. The term “expression” or “gene expression” means the transcription of a specific gene or specific genes or specific nucleic acid construct. The term “expression” or “gene expression” means the transcription of a gene or genes or genetic construct into structural RNA (e.g., rRNA, tRNA) or mRNA with or without subsequent translation of the latter into a protein. The process includes transcription of DNA and processing of the resulting mRNA product.The term “purification” or “purifying” refers to a process in which at least one component, e.g., a protein of interest, is separated from at least another component, e.g., a particulate matter of a fermentation broth, and transferred into a different compartment or phase, wherein the different compartments or phases do not necessarily need to be separated by a physical barrier. Examples of such different compartments are two compartments separated by a filtration membrane or cloth, i.e., filtrate and retentate; examples of such different phases are pellet and supernatant or cake and filtrate, respectively. The resulting solution after purifying the enzyme of interest from the fermentation broth is called herein “purified enzyme solution”.“Protein formulation” (or “enzyme preparation” or “polypeptide formulation”), e.g., “mannanase formulation”, means any non-complex formulation comprising a small number of ingredients, preferably, 2 to 8 components, wherein the ingredients serve the purpose of stabilizing the proteins / polypeptides comprised in the protein / polypeptide formulation and / or the stabilization of the protein / polypeptide formulation itself. Preferably, the non-complex protein / polypeptide formulation comprises the protein / polypeptide in higher concentrations than the complex formulation, e.g., than a detergent formulation. Thus, preferably the non-complex protein formulation is a concentrated protein / polypeptide formulation. Preferably, non-complex protein / polypeptide formulations comprise 10 mg / g to 120 mg / g active enzyme,BASF SE 240828W0017 B19118WO whereas complex formulations, like cleaning compositions, comprise 0.001 mg / g to 10 mg / g active enzyme. In contrast to a non-complex formulation, a complex formulation means herein a formulation comprising a higher number of ingredients, preferably, 9 to 30 components, wherein the ingredients serve the purpose of stabilizing the proteins comprised in the protein formulation and / or the stabilization of the protein formulation itself, but additionally the complex formulation comprises components that serve the purpose of the complex formulation, e.g., a cleaning composition. An example for a non-complex protein formulation is a concentrated enzyme composition that is used as a stock-solution to prepare a complex formulation, e.g., a cleaning composition, wherein in the cleaning compositions other compounds are present that serve the cleaning purpose of the cleaning composition, e.g., surfactants and / or chelating agents.“Enzyme properties” include, but are not limited to, catalytic activity, substrate / cof actor 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 enzyme’s 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 glycosidic bonds between mannose units in polypeptides etc.The term “enzyme stability” according to the current invention relates to the retention of enzymatic activity as a function of time during storage or operation. Retention of enzymatic activity as a function of time during storage is called “storage stability” and is preferred within the context of the invention.To determine and quantify changes in catalytic activity of enzymes stored or used under certain conditions over time, the enzymatic activity is measured under defined conditions at an initial time point (100 %) and at a certain point in time later (x %). By comparison of the values measured, the residual activity of the enzyme can be determined in its extent. The extent of the residual activity of the enzyme determines an enzyme’s stability or non-stability.“Enzyme inhibitors” as used herein are compounds that slow down or halt enzymatic activity. Enzyme inhibitors frequently also stabilize the enzyme in its three-dimensional structure. Hence, enzyme inhibitors usually also act as “enzyme stabilizers”.“pH stability” refers to the ability of an enzyme to exert enzymatic activity after exposure to a certain pH value.The terms “detergent stability” (also called herein “residual activity in a detergent” or “storage stability in a cleaning composition”) refer to the ability of an enzyme to exert catalytic activity or wash performance after storage in a cleaning composition, preferably, at a temperature of 37 °C, 45 °C, or 50 °C for up to 28 days in a cleaning composition (preferably, in Model B detergent as described herein). Most preferably, “detergent stability” is determined by measuring residual activity of the mannanase after storage at a temperature of 45 °C for 14 days in a cleaning composition (preferably, in Model B detergent as described herein).The term “formulation stability” (also called herein “residual activity in an enzyme formulation” or “storage stability in an enzyme formulation”) refers to the ability of an enzyme to exert catalytic activity or wash performance after storage in an enzyme formulation, preferably, at a temperature of 37 °C to 50 °C for up to 28 days in an enzyme formulation (preferably, in the Model enzyme formulation solution as described herein). Most preferably, “formulation stability” is determined by measuring residual activity of the mannanase after storage at a temperature of 45 °C for 28 days in an enzyme formulation (preferably, in the Model enzyme formulation solution as described herein).BASF SE 240828W0018 B19118WOAs used herein, "wash performance" (also called herein “cleaning performance”) of an enzyme 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 herein similarly for laundry and hard surface cleaning. Wash performance is compared under relevant washing conditions. The term "relevant washing conditions" is used herein to indicate the conditions, particularly washing temperature, time, washing mechanics, sud concentration, type of detergent and water hardness, actually used in households in a detergent market segment. The term "improved wash performance" is used to indicate that a better end result is obtained in stain removal under relevant washing conditions, or that less enzyme, on weight basis, is needed to obtain the same end result relative to the corresponding control conditions. The term "comparable wash performance" is used to indicate that essentially the same end result is obtained in stain removal under relevant washing conditions, or that essentially the same amount of enzyme, on weight basis, is needed to obtain the same end result relative to the corresponding control conditions. “Essentially the same end result” as used herein means that the end result obtained using a specific enzyme variant differs by 30% or less from the end result obtained using corresponding control conditions, e.g. a corresponding wild-type enzyme. Within the present invention the wash performance is preferably determined on egg stains.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 guar gum or locust bean gum containing stains or soils, such as desserts, sweets (chocolates), sauces, cosmetics, etc.“Detergent composition” or “detergent” means compositions designated for cleaning soiled material. Detergent compositions are complex formulations as further defined herein. Detergent compositions include detergent compositions for different applications such as laundry and hard surface cleaning. Detergent compositions also include biodegradable detergent compositions. The term “detergent component” is defined herein to mean a type of chemical, which can be used in detergent compositions. A typical detergent component is a surfactant. "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, amphoteric or zwitter-ionic. 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). Detergent compositions typically have a mannanase concentration of 0.0001 g / L to 1 g / L, preferably of 0.0005 g / L to 0.5 g / L and more preferably of 0.001 g / L to 0.1 g / L active enzyme.The term “laundry” or “laundering” relates to both household laundering and industrial laundering and means the process of treating textiles and / or fabrics with a solution containing a detergent composition. The laundering process may be carried out by using technical devices such as a household or an industrial washing machine. Alternatively, the laundering process may be done by hand.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,BASF SE 240828W0019 B19118WO knitting or felting fibers) or “garment” (any article of clothing made of textile) as used herein, are intended to include the broader term textile as well.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, comprising proteins like collagen, keratin and fibroin (e.g. silk, sheep’s 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.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 detergent composition. Hard surfaces may include any hard surfaces in the household or industry, such as floors, furnishing, walls, sanitary ceramics, glass, metallic surfaces including cutlery or dishes and medical devices such as diagnostic instruments, trays, pans, holders, racks, forceps, scissors, shears, saws (e.g. bone saws and their blades), hemostats, knives, chisels, rongeurs, files, nippers, drills, drill bits, rasps, burrs, spreaders, breakers, elevators, clamps, needle holders, carriers, clips, hooks, gouges, curettes, retractors, straightener, punches, extractors, scoops, keratomes, spatulas, expressors, trocars, dilators, cages, glassware, tubing, catheters, cannulas, plugs, stents, endoscopes, arthoscopes and related equipment. A particular form of hard surface cleaning is dishwashing, particularly automatic dishwashing (ADW).The term “dish wash” refers to all forms of washing dishes, e.g. by hand or automatic dish wash. 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.Cleaning performance is evaluated under relevant cleaning conditions. The term "relevant cleaning conditions" herein refers to the conditions, particularly cleaning temperature, time, cleaning mechanics, suds concentration, type of detergent and water hardness, actually used in laundry machines, automatic dish washers or in manual cleaning processes.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.In the field of detergency, usually the term “stains” is used with reference to laundry, e.g., cleaning of 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” shall be used interchangeably.A “sequestering builder” as used herein is different from a precipitating builder in that no significant amount of precipitate is formed when the builder is used in an amount sufficient to combine with all of the calcium ions in an aqueous solution with 7 °dH hardness (German hardness) initially at neutral pH. A “strong builder” is classified as high efficiency chelators that can bind the divalent cations such as Ca2+strongly with a logarithmic stability constant (Log KCa) of the cation / chelator complex of above 4, particular above 5, above 6 or above 7. The stability constants are determined at an ionic strength of 0.1 M and at a temperature of 25 °C. A ..strong sequestering builder” combines both of the above- mentioned properties. Strong sequestering builders include, but are not limited to, Ethylenediaminetetraacetic acidBASF SE 240828W00110 B19118WO(EDTA), Ethylene diamine tetra(methylene phosphonic acid (EDTMP), Nitrilo trimethylene phosphonic acid (NTMP), Diethylenetriamine Penta(Methylene Phosphonic acid) (DTPMP), methylglycinediacetic acid (MGDA), Nitrilotriacetic acid (NTA), 1 -Hydroxy Ethylidene-1 ,1-Diphosphonic acid (HEDP), sodium tripolyphosphate (STPP), iminodisuccinic acid (IDS), N,N-diacetic acid tetra sodium salt (GLDA), pyrophosphate and ethylenediaminedisuccinic acid (EDDS), preferably MGDA and / or EDDS.An “antimicrobial agent’ is a chemical compound that kills microorganisms or inhibits their growth or reproduction. Microorganisms can be bacteria, yeasts or molds. 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.A composition “essentially devoid” of a compound shall mean herein that the respective compound is not added to the composition on purpose, meaning that at most non-effective amounts are present, most preferably 0 % of the compound are contained in the composition.A “composition” is a mixture of components (also called ingredients) prepared according to a specific formula. Compositions can be liquid or solid. Liquid compositions of the invention include solutions, emulsions and dispersions, gels etc. as long as the liquid is fluid and pourable. Liquid compositions according to the present invention preferably have a dynamic viscosity in the range of about 500 mPa*s to about 20,000 mPa*s (milli Pascal seconds), determined at 25 °C according to Brookfield, for example spindle 3 rpm at 20 rpm with a Brookfield viscosimeter LVT-II."Gel", as used herein, means a shear thinning, lamellar gel, with a pouring viscosity in the range of from 100 mPa*s to 5,000 mPa*s, more preferably less than 3,000 mPa*s, most preferably less than 1 ,500 mPa*s. Compositions include enzyme compositions, e.g. liquid enzyme compositions as described herein, and cleaning compositions, e.g. liquid cleaning compositions as described herein.The components of the composition can be separated by formulating them in different compartments, such as different compartments of multi-chamber-pouches or bottles having different chambers, from which the liquids are poured out at the same time in a predefined amount to assure the application of the right amount per individual point of use of each component from each chamber. Such multi-compartment-pouches and bottles etc. are known to a person of skill as well. The compositions of the invention may be delivered in dual- or multi-compartment containers, in single-phase or multiphase unit doses, in a spray or foam detergent, as premoistened wipes (i.e., the cleaning composition in combination with a nonwoven material such as that discussed in US 6,121 ,165, Mackey, et al.), and other homogeneous, non- homogeneous or single-phase or multiphase cleaning product forms.Detailed descriptionIn the present invention new mannanase enzymes are provided. More specifically, variants of a parent mannanase, methods of making the variant mannanases, compositions comprising the mannanase variants, and methods of using the variant mannanases or compositions comprising the variant mannanases are provided.Mannanase VariantThe present invention is directed to a variant polypeptide having mannanase activity, wherein the variant polypeptide: (i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 andBASF SE 240828W00111 B19118WO(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1. The present invention is directed to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 and(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the variant polypeptide of the present invention has a length of 200 to 350 amino acids or of 220 to 330 amino acids or of 240 to 320 amino acids or of 260 to 310 amino acids or of 280 to 300 amino acids, preferably the variant polypeptide of the present invention has a length of 299 amino acids.In one embodiment, the variant polypeptide of the present invention does not comprise amino acids 300 to 460 of SEQ ID NO: 1.The variant polypeptide having mannanase activity of the present invention is a non-naturally occurring mannanase. Preferably, the variant polypeptide having mannanase activity of the present invention is a purified, isolated, synthetic, and / or recombinant mannanase. Preferably, the variant polypeptide having mannanase activity of the present invention is a purified and recombinant mannanase.Mannanases according to the invention have “mannanase activity” or “mannan degrading activity”. “Mannanase activity” or “mannan degrading activity” describes the capability for the hydrolysis of glycosidic bonds between the mannose units in polysaccharides. In one embodiment, “mannan degrading activity” refers to the degradation of at least one galactomannan. Preferably, at least one galactomannan is characterized by the ratio mannose:galactose of about 1 :1 , about 2:1 , about 3:1 , about 4: 1 , and / or 5:1.The mannanase activity may be determined by assays for measurement of mannanase activity which are known to those skilled in the art.Preferably, a polypeptide having mannan degrading activity or mannanase activity may be tested for this activity according to standard test procedures known in the art, such as by applying a solution to be tested to 4 mm diameter holes punched out in agar plates containing 0.2% AZCL galactomannan (carob), i.e. substrate for the assay of endo-1 ,4- beta-D-mannanase available as CatNo. I-AZGMA from the company Megazyme (Megazyme's Internet address: http: / / www. megazyme. com / Purchase / index. html).Alternatively, mannan degrading activity of a mannanase may be tested in a liquid assay using carob galactomannan dyed with Remazol Brilliant Bue as described in McCleary, B. V. (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 gut - for reference see Miller, G. L. Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugars. Analytical Chemistry 1959; 31 : 426-428.In one embodiment, the variant polypeptide having mannanase activity of the present invention:(i) has a sequence identity of at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 90.5%, at least 91 %, at least 91 .5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.1 %, at least 95.2%, at least 95.3%, at least 95.4%, at least 95.5%, at least 95.6%, at least 95.7%, at least 95.8%, at least 95.9% at least 96%, at least 96.1 %,BASF SE 240828W00112 B19118WO at least 96.2%, at least 96.3%, at least 96.4%, at least 96.5%, at least 96.6%, at least 96.7%, at least 96.8%, at least 96.9%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 , and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 . In one embodiment, the variant polypeptide having mannanase activity of the present invention:(i) has a sequence identity of at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 90.5%, at least 91 %, at least 91 .5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.1 %, at least 95.2%, at least 95.3%, at least 95.4%, at least 95.5%, at least 95.6%, at least 95.7%, at least 95.8%, at least 95.9% at least 96%, at least 96.1 %, at least 96.2%, at least 96.3%, at least 96.4%, at least 96.5%, at least 96.6%, at least 96.7%, at least 96.8%, at least 96.9%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 , and(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the variant polypeptide having mannanase activity of the present invention:(i) has a sequence identity of 81 % to 91 %, 81.5% to 91 %, 82% to 91 %, 82.5% to 91 %, 83% to 91 %, 83.5% to 91 %, 84% to 91 %, 84.5% to 91 %, 85% to 91%, 85.5% to 91 %, 86% to 91 %, 86.5% to 91 %, 87% to 91 %, 87.5% to 91 %, 88% to 91 %, 88.5% to 91 %, 89% to 91 %, 89.5% to 91 % to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 . In one embodiment, the variant polypeptide having mannanase activity of the present invention:(i) has a sequence identity of 81 % to 91 %, 81.5% to 91 %, 82% to 91 %, 82.5% to 91 %, 83% to 91 %, 83.5% to 91 %, 84% to 91 %, 84.5% to 91 %, 85% to 91%, 85.5% to 91 %, 86% to 91 %, 86.5% to 91 %, 87% to 91 %, 87.5% to 91 %, 88% to 91 %, 88.5% to 91 %, 89% to 91 %, 89.5% to 91 % to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1, and(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises an amino acid substitution at amino acid residue 100.In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises the amino acid substitution X100R / K / Q.In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises the amino acid substitution X100R.BASF SE 240828W00113 B19118WOIn one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises an amino acid substitution at amino acid residue 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises the amino acid substitution X100R / K / Q, preferably the amino acid substitution X100R, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises an amino acid substitution at amino acid residue 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises the amino acid substitution X100R / K / Q, preferably the amino acid substitution X100R, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94 and 96 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .BASF SE 240828W00114 B19118WOIn one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q and X96E / D / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least one amino acid substitution selected from the group consisting of X79K, X92K, X94D / E and X96E compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises amino acid substitutions at at least two, at least three or all amino acid residues selected from the group consisting of 79, 92, 94 and 96 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least two, at least three, or all of the amino acid substitutions X79K / H / R, X92 K / E / Q / R / H, X94D / E / N / K / Q and X96E / D / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least two, at least three or all of the amino acid substitutions X79K, X92K, X94D / E and X96E compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94 and 96 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q and X96E / D / K / Q, preferably at least one amino acid substitution selected from the group consisting of X79K, X92K, X94D / E and X96E, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .BASF SE 240828W00115 B19118WOIn one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94 and 96 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q and X96E / D / K / Q, preferably at least one amino acid substitution selected from the group consisting of X79K, X92K, X94D / E and X96E, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , (Hi) comprises an amino acid substitution at amino acid residue 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94 and 96 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,BASF SE 240828W00116 B19118WO(iii) comprises an amino acid substitution at amino acid residue 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q and X96E / D / K / Q, preferably at least one amino acid substitution selected from the group consisting of X79K, X92K, X94D / E and X96E, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(iii) comprises an amino acid substitution at amino acid residue 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94 and 96 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(iii) comprises the amino acid substitution X100R / K / Q, preferably the amino acid substitution X100R, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94 and 96 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(iii) comprises the amino acid substitution X100R / K / Q, preferably the amino acid substitution X100R, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , andBASF SE 240828W00117 B19118WO(iv) the polypeptide comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q and X96E / D / K / Q, preferably at least one amino acid substitution selected from the group consisting of X79K, X92K, X94D / E and X96E, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.Table 1 :In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 80%, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .Table 2:BASF SE 240828W00118 B19118WOIn one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of 81 % to 91 %, 81.5% to 91 %, 82% to 91 %, 82.5% to 91 %, 83% to 91 %, 83.5% to 91 %, 84% to 91 %, 84.5% to 91 %, 85% to 91%, 85.5% to 91 %, 86% to 91 %, 86.5% to 91 %, 87% to 91 %, 87.5% to 91 %, 88% to 91 %, 88.5% to 91 %, 89% to 91 %, 89.5% to 91 %, to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1, and(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of 81 % to 91 %, 81.5% to 91 %, 82% to 91 %, 82.5% to 91 %, 83% to 91 %, 83.5% to 91 %, 84% to 91 %, 84.5% to 91 %, 85% to 91%, 85.5% to 91 %, 86% to 91 %, 86.5% to 91 %, 87% to 91 %, 87.5% to 91 %, 88% toBASF SE 240828W00119 B19118WO91 %, 88.5% to 91 %, 89% to 91 %, 89.5% to 91 % to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1, and(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) the polypeptide comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises an amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:BASF SE 240828W00120 B19118WO(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises an amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations shown in T able 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .BASF SE 240828W00121 B19118WOIn one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of 81 % to 91 %, 81.5% to 91 %, 82% to 91 %, 82.5% to 91 %, 83% to 91 %, 83.5% to 91 %, 84% to 91 %, 84.5% to 91 %, 85% to 91%, 85.5% to 91 %, 86% to 91 %, 86.5% to 91 %, 87% to 91 %, 87.5% to 91 %, 88% to 91 %, 88.5% to 91 %, 89% to 91 %, 89.5% to 91 %, to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations shown in T able 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of 81 % to 91 %, 81.5% to 91 %, 82% to 91 %, 82.5% to 91 %, 83% to 91 %, 83.5% to 91 %, 84% to 91 %, 84.5% to 91 %, 85% to 91%, 85.5% to 91 %, 86% to 91 %, 86.5% to 91 %, 87% to 91 %, 87.5% to 91 %, 88% to 91 %, 88.5% to 91 %, 89% to 91 %, 89.5% to 91 % to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of 81 % to 91 %, 81.5% to 91 %, 82% to 91 %, 82.5% to 91 %, 83% to 91 %, 83.5% to 91 %, 84% to 91 %, 84.5% to 91 %, 85% to 91%, 85.5% to 91 %, 86% to 91 %, 86.5% to 91 %, 87% to 91 %, 87.5% to 91 %, 88% to 91 %, 88.5% to 91 %, 89% to 91 %, 89.5% to 91 % to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of 81 % to 91 %, 81.5% to 91 %, 82% to 91 %, 82.5% to 91 %, 83% to 91 %, 83.5% to 91 %, 84% to 91 %, 84.5% to 91 %, 85% to 91%, 85.5% to 91 %, 86% to 91 %, 86.5% to 91 %, 87% to 91 %, 87.5% to 91 %, 88% to 91 %, 88.5% to 91 %, 89% to 91 %, 89.5% to 91 % to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , andBASF SE 240828W00122 B19118WO(iii) comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises an amino acid substitution at at least two, at least three, at least four, at least five, at least six, at least seven, at least eight, at least nine, at least ten, at least eleven, at least twelve, at least thirteen, at least fourteen, at least fifteen, at least sixteen, at least seventeen, at least eighteen, at least nineteen or all amino acid residues selected from the group consisting of 103, 107, 201 , 205, 225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least one amino acid substitution selected from the group consisting of X103N / D, X107E, X201 L, X205N, X225Y, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least two, at least three, at least four, at least five, at least six, at least seven, at least eight, at least nine, at least ten, at least eleven, at least twelve, at least thirteen, at least fourteen, at least fifteen, at least sixteen, at least seventeen, at least eighteen, at least nineteen or all of the amino acid substitutions X103N / D, X107E, X201 L, X205N, X225Y, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V, preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , andBASF SE 240828W00123 B19118WO(iii) comprises at least one amino acid substitution selected from the group consisting of X103N / D, X107E, X201 L, X205N, X225Y, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iii) comprises at least one amino acid substitution selected from the group consisting of X103N / D, X107E, X201 L, X205N, X225Y, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises an amino acid substitution at least two, at least three, at least four, at least five, at least six, at least seven, at least eight, at least nine, at least ten, at least eleven, at least twelve, at least thirteen, at least fourteen, at least fifteen, at least sixteen, at least seventeen, at least eighteen, at least nineteen, at least twenty, at least twenty-one, at least twenty-two, at least twenty-three, at least twenty-four, at least twenty-five, at least twenty-six, at least twenty-seven or all amino acid residues selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least one amino acid substitution selected from the group consisting of X2S, X5H, X7S, X29T / A, X31Y, X33S, X41 G, X44N, X59V, X66D, X71V, X97A, X99M, X108L, X110D, X111T, X118K, X134G, X135G, X138E, X158I, X160A,BASF SE 240828W00124 B19118WOX168K / Q, X175Q, X182T, X243T, X259M and X289E compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the variant polypeptide of the present invention having mannanase activity additionally comprises at least two, at least three, at least four, at least five, at least six, at least seven, at least eight, at least nine, at least ten, at least eleven, at least twelve, at least thirteen, at least fourteen, at least fifteen, at least sixteen, at least seventeen, at least eighteen, at least nineteen, at least twenty, at least twenty-one, at least twenty-two, at least twenty-three, at least twenty-four, at least twenty-five, at least twenty-six, at least twenty-seven or all of the amino acid substitutions X2S, X5H, X7S, X29T / A, X31Y, X33S, X41 G, X44N, X59V, X66D, X71V, X97A, X99M, X108L, X110D, X111T, X118K, X134G, X135G, X138E, X158I, X160A, X168K / Q, X175Q, X182T, X243T, X259M and X289E compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 ,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / MA / , preferably selected from the group consisting of X58G and X72L, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution selected from the group consisting of X2S, X5H, X7S, X29T / A, X31Y, X33S, X41 G, X44N, X59V, X66D, X71V, X97A, X99M, X108L, X110D, X111T, X118K, X134G, X135G, X138E, X158I, X160A, X168K / Q, X175Q, X182T, X243T, X259M and X289E compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , andBASF SE 240828W00125 B19118WO(iii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iii) comprises at least one amino acid substitution selected from the group consisting of X2S, X5H, X7S, X29T / A, X31Y, X33S, X41 G, X44N, X59V, X66D, X71V, X97A, X99M, X108L, X110D, X111T, X118K, X134G, X135G, X138E, X158I, X160A, X168K / Q, X175Q, X182T, X243T, X259M and X289E compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(iii) comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(iii) comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution selected from the group consisting of X103N / D, X107E, X201 L, X205N, X225Y, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:BASF SE 240828W00126 B19118WO(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(Hi) comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(Hi) comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution selected from the group consisting of X2S, X5H, X7S, X29T / A, X31Y, X33S, X41 G, X44N, X59V, X66D, X71V, X97A, X99M, X108L, X110D, X111T, X118K, X134G, X135G, X138E, X158I, X160A, X168K / Q, X175Q, X182T, X243T, X259M and X289E compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,BASF SE 240828W00127 B19118WO(iii) comprises at least one amino acid substitution selected from the group consisting of X103N / D, X107E, X201 L, X205N, X225Y, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution selected from the group consisting of X2S, X5H, X7S, X29T / A, X31Y, X33S, X41 G, X44N, X59V, X66D, X71V, X97A, X99M, X108L, X110D, X111T, X118K, X134G, X135G, X138E, X158I, X160A, X168K / Q, X175Q, X182T, X243T, X259M and X289E compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises amino acid substitutions at one of the combinations of positions shown in Table 1 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(iii) comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(v) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has a sequence identity of at least 81 %, but less than 100% to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 1 ,(ii) comprises one of the combinations of amino acid substitutions shown in T able 2 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(iii) comprises the amino acid substitution X234Q / T, preferably the amino acid substitution X234Q, compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 ,(iv) comprises at least one amino acid substitution selected from the group consisting of X103N / D, X107E, X201 L, X205N, X225Y, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(v) comprises at least one amino acid substitution selected from the group consisting of X2S, X5H, X7S, X29T / A, X31 Y, X33S, X41 G, X44N, X59V, X66D, X71V, X97A, X99M, X108L, X110D, X111T, X118K, X134G, X135G, X138E, X158I, X160A, X168K / Q, X175Q, X182T, X243T, X259M and X289E compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.BASF SE 240828W00128 B19118WOIn one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 90%, at least 90.5%, at least 91%, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to any one of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 90%, at least 90.5%, at least 91%, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 3.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 91 %, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 4.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 91 %, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 5.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 90%, at least 90.5%, at least 91%, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 6.BASF SE 240828W00129 B19118WOIn one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 91 %, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 7.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 90%, at least 90.5%, at least 91%, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 8.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 9.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 10.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 91 %, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 11.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 90%, at least 90.5%, at least 91%, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, atBASF SE 240828W00130 B19118WO least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 12.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 90%, at least 90.5%, at least 91%, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 13.In one embodiment, the variant mannanase has an amino acid sequence with a sequence identity of at least 91 %, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to SEQ ID NO: 14.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, atBASF SE 240828W00131 B19118WO least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 3, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 4, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 5, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 6, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:BASF SE 240828W00132 B19118WO(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 8, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 9, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, atBASF SE 240828W00133 B19118WO least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 10, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 11 , and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 12, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 13, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein:BASF SE 240828W00134 B19118WO(i) the polypeptide has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 14, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, and(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 .In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7, and(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / MA / compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 .In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at leastBASF SE 240828W00135 B19118WO97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 3, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 4, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , andBASF SE 240828W00136 B19118WO(iii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 5, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(iii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 6, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(iii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, atBASF SE 240828W00137 B19118WO least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 8, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 9, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.BASF SE 240828W00138 B19118WOIn one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 10, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 11 , and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 12, andBASF SE 240828W00139 B19118WO(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 13, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 14, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:BASF SE 240828W00140 B19118WO(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / MA / compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQBASF SE 240828W00141 B19118WOID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(Hi) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , andBASF SE 240828W00142 B19118WO(iii) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , and(iii) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%,BASF SE 240828W00143 B19118WO at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 3, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 4, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 5, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 6, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:BASF SE 240828W00144 B19118WO(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 8, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 9, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%,BASF SE 240828W00145 B19118WO at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 10, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 11 , and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 12, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 13, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:BASF SE 240828W00146 B19118WO(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 14, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, and(ii) the polypeptide comprises the amino acid substitutions X58G / A / P, X72L / M / V, X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7, and(ii) the polypeptide comprises the amino acid substitutions X58G / A / P, X72L / M / V, X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%,BASF SE 240828W00147 B19118WO at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , (Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1, and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , (Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1, and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%,BASF SE 240828W00148 B19118WO at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , (Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1, and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / MA / compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , (Hi) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1, and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQBASF SE 240828W00149 B19118WOID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , (Hi) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7,(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , (Hi) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14,BASF SE 240828W00150 B19118WO(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / M / V compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , (Hi) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of X103N / D, X107E, X201 L, X205N, X225Y, X234Q / T, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7,(ii) comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / MA / compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , (Hi) comprises at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , and(iv) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of X103N / D, X107E, X201 L, X205N, X225Y, X234Q / T, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, andBASF SE 240828W00151 B19118WO(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, 100, 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7, and(ii) comprises amino acid substitutions at amino acid residues 58, 72, 79, 92, 94, 96, 100, 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, and(ii) comprises the amino acid substitutions X58G / A / P, X72L / M / V, X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, X100R / K / Q, X103N / D, X107E, X201 L, X205N, X225Y, X234Q / T, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7, andBASF SE 240828W00152 B19118WO(ii) comprises the amino acid substitutions X58G / A / P, X72L / M / V, X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, X100R / K / Q, X103N / D, X107E, X201 L, X205N, X225Y, X234Q / T, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, and(ii) comprises the amino acid substitutions X58G, X72L, X79K, X92K, X94D, X96E, X100R, X103N, X107E, X201 L, X205N, X225Y, X234Q, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y, X284E, X293L, X295G and X299S compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the present invention relates to a variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or 100% identical to amino acids 1 to 299 of the amino acid sequence according to SEQ ID NO: 7, and(ii) comprises the amino acid substitutions X58G, X72L, X79K, X92K, X94D, X96E, X100R, X103N, X107E, X201 L, X205N, X225Y, X234Q, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y, X284E, X293L, X295G and X299S compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.In one embodiment, the mannanase variant of the present invention exhibits one or more improved properties compared to the mannanase according to SEQ ID NO: 1 or 15, preferably compared to the mannanase according to SEQ ID NO: 15.Preferably, the variant polypeptide having mannanase activity of the present invention shows an increased stability, in particular storage stability, compared to the mannanase according to SEQ ID NO: 1 or 15, preferably compared to the mannanase according to SEQ ID NO: 15. The increased stability is preferably indicated as residual activity after stability challenge. Preferably, storage stability is indicated as residual activity after storage under the respective storageBASF SE 240828W00153 B19118WO conditions, preferably, after storage in a detergent composition (preferably in a laundry or dishwash detergent, preferably laundry detergent) or an enzyme formulation. Most preferably, storage stability of the variant polypeptide having mannanase activity is determined after storage in a composition comprising a protease and an enzyme stabilizer. Preferably, the residual activity of the mannanase variant is increased compared to the residual activity of the mannanase according to SEQ ID NO: 1 or 15, preferably the mannanase according to SEQ ID NO: 15, after storage. Preferably, the residual activity of the mannanase variant after storage is at least 0.5%, at least 1 %, at least 2%, at least 3%, at least 5%, at least 6%, at least 7%, at least 8%, at least 9%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 110%, at least 120%, at least 130%, at least 140%, at least 150%, at least 160%, at least 170%, at least 180%, at least 190%, or at least 200% increased compared to the residual activity of the parent mannanase, preferably compared to the mannanase SEQ ID NO: 1 or 15, preferably compared to the mannanase according to SEQ ID NO: 15. Preferably, the residual activity of the mannanase variant is increased compared to the residual activity of the mannanase according to SEQ ID NO: 1 or 15, preferably the mannanase according to SEQ ID NO: 15, after storage in a composition comprising a protease and an enzyme stabilizer. Preferably, the residual activity of the mannanase variant after storage is at least 0.5%, at least 1 %, at least 2%, at least 3%, at least 5%, at least 6%, at least 7%, at least 8%, at least 9%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%, at least 110%, at least 120%, at least 130%, at least 140%, at least 150%, at least 160%, at least 170%, at least 180%, at least 190%, or at least 200% increased compared to the residual activity of the parent mannanase, preferably compared to the mannanase SEQ ID NO: 1 or 15, preferably compared to the mannanase according to SEQ ID NO: 15 after storage in a composition comprising a protease and an enzyme stabilizer.Preferably, the improved property is one or more property selected from the group consisting of an increase in stability, thermostability, performance in a detergent, performance in a laundry detergent and performance in an ADW detergent. Preferably, the improved activity is improved wash performance, wash performance of a laundry detergent and / or wash performance of an ADW detergent.Preferably, the improved property is improved stability in a detergent composition, preferably a laundry detergent composition, preferably in a detergent composition comprising 1 % to 20%, more preferably 5% to 10% anionic surfactants, preferably linear alkylbenzene sulfonate (LAS), and / or greater than 50% water, preferably in a Model B type detergent as described herein. In one embodiment, the improved property is improved stability in a detergent composition, preferably a laundry detergent composition, preferably in a detergent composition comprising 0.1 % to 5%, preferably 0.3% to 3%, of a strong sequestering builder. In this embodiment, the detergent composition preferably comprises 1 % to 20%, more preferably 5% to 10% anionic surfactants, preferably LAS, and / or greater than 50% water. Preferably, the improved property is improved stability in an enzyme formulation, preferably in an enzyme formulation comprising 40% to 60%, preferably 45% to 55%, more preferably 50% stabilizers and formulation aids, more preferably in an enzyme formulation comprising neopentyl glycol (NPG), mono propylene glycol (MPG) and glycerol, and / or greater than 50% water, most preferably in the Model enzyme formulation solution as described herein. Also preferably, the improved property is improved stability in an enzyme formulation comprising protease, preferably comprising 0.1 % to 6% (v / v) protease, more preferably 1 % to 5% (v / v) protease and most preferably 2.5% to 4% (v / v) protease.BASF SE 240828W00154 B19118WONucleic acid constructThe present invention also refers to a polynucleotide encoding the polypeptide having mannanase activity of the present invention. Preferably, the polynucleotide is a codon-optimized polynucleotide for improving expression in a specific host cell, preferably a Bacillus cell.The present invention also refers to a nucleic acid construct, preferably an expression cassette, comprising the polynucleotide as described herein.Typically, the expression cassette comprises three elements: a promoter sequence, an open reading frame and a 3' untranslated region that, in eukaryotes, usually contains a polyadenylation site. Additional regulatory elements may include transcriptional as well as translational enhancers. An intron sequence may also be added to the 5' untranslated region (UTR) or in the coding sequence to increase the amount of the mature message that accumulates in the cytosol. The expression cassette may be part of a vector or may be integrated into the genome of a host cell and replicated together with the genome of its host cell. The expression cassette usually is capable of increasing or decreasing expression.The present invention also refers to an expression vector comprising the polynucleotide or the nucleic acid construct as described herein. The expression vector can be a low copy number vector or high copy number vector.A vector as used herein may provide segments for transcription and translation of a foreign polynucleotide upon transformation into a host cell or host cell organelles. Such additional segments may include regulatory nucleotide sequences, one or more origins of replication that is required for its maintenance and / or replication in a specific cell type, one or more selectable markers, a polyadenylation signal, a suitable site for the insertion of foreign coding sequences such as a multiple cloning site etc. One example is when a vector is required to be maintained in a bacterial cell as an episomal genetic element (e.g., plasmid or cosmid molecule). Non-limiting examples of suitable origins of replication include the f1-ori and colE1.A vector may replicate without integrating into the genome of a host cell, e.g., as a plasmid in a bacterial host cell, or it may integrate part or all of its DNA into the genome of the host cell and thus lead to replication and expression of its DNA.The polynucleotide encoding the polypeptide having mannanase activity of the present invention may be introduced into a vector by means of standard recombinant DNA techniques. Once introduced into the vector, the polynucleotide comprising a coding sequence may be suitable to be introduced (transformed, transduced, transfected, etc.) into a host cell or host cell organelles. A cloning vector may be chosen suitable for expression of the polynucleotide sequence in the host cell or host cell organelles.Host cellThe present invention also refers to a host cell comprising the polynucleotide encoding the polypeptide having mannanase activity of the present invention, the nucleic acid construct as described herein, or the expression vector as described herein. In one embodiment of the invention, a vector is used for transformation of a host cell. Preferably, the host cell is capable of expressing the polynucleotide encoding the polypeptide having mannanase activity of the present invention.BASF SE 240828W00155 B19118WOThe polynucleotide encoding the polypeptide having mannanase activity of the present invention herein may be transiently or stably introduced into a host cell. The polynucleotide may be maintained non-integrated, for example, as a plasmid. Usually, stable transformation is due to integration of nucleic acid comprising a foreign coding sequence into the host cell chromosomes or as an episome (separate piece of nuclear DNA). Usually, transient transformation is due to nucleic acid comprising a foreign nucleic acid sequence not being integrated into the host cell chromosomes or as an episome. Methods for introducing a nucleic acid into a host cell are well-known in the art.Various host cells can be used for expressing the nucleic acid construct described herein. The host cell of the present invention does not naturally express the polypeptide having mannanase activity of the present invention. Thus, the host cell is a recombinant host cell; the nucleic acid construct described herein is heterologous for the host cell.In one embodiment, the host cell is a prokaryote or a eukaryote. In another embodiment, the host cell is a bacterial cell, an archaea, a fungal cell, a yeast cell or a eukaryotic cell. In another embodiment, the host cell is a non-human host cell. In one embodiment, the host cell is a bacterial cell. The bacterial host cell may be any gram-positive bacterium or a gram-negative bacterium. Gram-positive bacteria include, but are not limited to, Bacillus, Brevibacterium, Corynebacterium, Streptococcus, Streptomyces, Staphylococcus, Enterococcus, Lactobacillus, Lactococcus, Clostridium, Geobacillus, and Oceanobacillus. Gram-negative bacteria include, but are not limited to, Escherichia, Pseudomonas, Salmonella, Campylobacter, Helicobacter, Acetobacter, Flavobacterium, Fusobacterium, Gluconobacter. In a specific embodiment, the bacterial host cell is a Echerichia coli cell. In one embodiment, the host cell is a bacterial cell. In a specific embodiment the host cell is of the genus Escherichia or Bacillus.In the methods of the present invention, the bacterial host cell may be any Bacillus cell. Bacillus cells useful in the practice of the present invention include, but are not limited to, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus stearothermophilus, Bacillus methylotrophicus, Bacillus cereus Bacillus paralicheniformis, Bacillus subtilis, and Bacillus thuringiensis cells. In one embodiment, the bacterial host cell is a Bacillus amyloliquefaciens, Bacillus pumilus, Bacillus lentus, Bacillus licheniformis, Bacillus stearothermophilus or Bacillus subtilis cell. In preferred embodiment, the bacterial host cell is a Bacillus licheniformis cell, a Bacillus pumilus, ora Bacillus subtilis cell. Preferably, the bacterial host cell is a Bacillus licheniformis cell.Methods of makingAnother embodiment of the present invention is a method of obtaining a mannanase variant of a parent mannanase comprising the steps of: a) introducing into the mannanase according to SEQ ID NO: 1 an amino acid substitution at the amino acid residues 79 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , thereby providing a variant polypeptide of said parent mannanase, wherein said variant has at least 80%, but less than 100%, sequence identity to the amino acid sequence according to SEQ ID NO: 1 , and wherein said variant polypeptide has mannanase activity and preferably wherein the variant polypeptide has an improved property relative to said parent mannanase; or b) introducing into a parent mannanase comprising amino acids 1 to 299 of SEQ ID NO: 1 , an amino acid substitution at the amino acid residues 79 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , thereby providing a variant polypeptide of said parent mannanase,BASF SE 240828W00156 B19118WO wherein said variant has at least 80%, but less than 100%, sequence identity to the amino acids 1 to 299 of SEQ ID NO: 1 , and wherein said variant polypeptide has mannanase activity and preferably wherein the variant polypeptide has an improved property relative to said parent mannanase.Ways of introducing amino acid substitutions into a protein sequence are well known in the art. The variants may be prepared using any mutagenesis procedure known in the art, such as site-directed mutagenesis, synthetic gene construction, semi-synthetic gene construction, random mutagenesis, shuffling, etc.The variant polypeptide having mannanase activity of the present invention can be produced in an industrial scale and subsequently purified. Industrial production of enzymes usually is done by cultivating a host cell (also called fermentation) which expresses the enzyme. Suitable host cells are described herein. A nucleic acid sequence encoding the variant polypeptide having mannanase activity of the present invention can be transformed into the host cell, which is subsequently cultivated under conditions suitable for the host cell to produce the variant polypeptide having mannanase activity of the present invention. In a preferred embodiment, the variant polypeptide having mannanase activity of the present invention is purified from the host cell.Hence, in yet another embodiment, the present invention is directed to a method of producing a variant polypeptide having mannanase activity, comprising the steps of(a) providing a host cell comprising a heterologous nucleic acid construct comprising a polynucleotide encoding the variant polypeptide having mannanase activity;(b) cultivating the recombinant host cell of step (a) under conditions conductive for the expression of the polynucleotide; and(c) optionally, recovering the variant polypeptide having mannanase activity encoded by the polynucleotide. Cultivation of the host cell normally takes place in a suitable nutrient medium allowing the recombinant cells to grow and express the desired protein. At the end of fermentation, the fermentation broth comprising a liquid fraction and a solid fraction is collected and may be further processed. The variant polypeptide having mannanase activity may be further purified from the fermentation broth.The variant polypeptide having mannanase activity described herein may be secreted (into the liquid fraction of the fermentation broth) or may not be secreted from the microbial cells (and therefore is comprised in the cells of the fermentation broth). Depending on this, the variant polypeptide having mannanase activity may be recovered from the liquid fraction of the fermentation broth or from cell lysates. Preferably, the variant polypeptide having mannanase activity is secreted from the cell into the fermentation broth, preferably by means of a secretion signal peptide added to the N- terminus of the amino acid sequence, forming a propeptide of the polypeptide. The polypeptide is folded upon cleavage of the propeptide and the mature mannanase is released as active variant. Recovery of the variant polypeptide having mannanase activity can be achieved by methods known to those skilled in the art. Suitable methods for recovery of proteins from fermentation broth include, but are not limited to, collection, centrifugation, filtration, extraction, and precipitation. If the protein of interest precipitates or crystallizes in the fermentation broth or binds at least in part to the particulate matter of the fermentation broth additional treatment steps might be needed to release the protein of interest from the biomass or to solubilize protein of interest crystals and precipitates. WO 00 / 43502 A1 , WO 2008 / 110498 A1 , and WO 2017 / 097869 A1 describe a method for recovering a protein of interest, which precipitates and / or crystallizes during fermentation, from the fermentation broth. In case the desired protein is comprised in the cells of the fermentation broth release of the protein of interest from the cells might be needed. Release from the cells can be achieved forBASF SE 240828W00157 B19118WO instance, but not being limited thereto, by cell lysis using techniques well known to the skilled person, e.g., lysozyme treatment, ultrasonic treatment, French press or combinations thereof.The variant polypeptide having mannanase activity may be purified from the fermentation broth by methods known in the art. For example, the variant polypeptide having mannanase activity may be isolated from the fermentation broth by conventional procedures including, but not limited to, centrifugation, filtration, extraction, spray-drying, evaporation, or precipitation. The isolated polypeptide may then be further purified by a variety of procedures known in the art including, but not limited to, chromatography (e.g., ion exchange, affinity, hydrophobic, chromatofocussing, and size exclusion), electrophoretic procedures (e.g., preparative isoelectric focusing (IEF), differential solubility (e.g., ammonium sulfate precipitation), or extraction (see, e.g., Protein Purification, J.-C. Janson and Lars Ryden, editors, VCH Publishers, New York, 1989). The purified polypeptide may then be concentrated by procedures known in the art including, but not limited to, ultrafiltration and evaporation, in particular, thin film evaporation.Mannanase CompositionsThe purified solution of the variant polypeptide having mannanase activity of the present invention may be further processed to form a mannanase containing composition. Hence, also claimed herein is a composition comprising the variant polypeptide having mannanase activity of the present invention and at least one additional component.Thus, the present invention therefore also refers to a method for making a composition comprising the steps of mixing i. a variant polypeptide having mannanase activity as described herein; and ii. one or more components described herein.Further, the present invention also refers to a method for improving mannanase stability in a composition comprising the steps of mixing(a) a variant polypeptide having mannanase activity as described herein; and(b) one or more components described herein.The composition can be a non-complex formulation, e.g., a mannanase formulation, or a complex formulation, e.g., a cleaning composition, as described herein.In one embodiment of the present invention, the variant polypeptide having mannanase activity is formulated as a mannanase formulation, preferably a concentrated mannanase formulation. The mannanase formulation can be either solid or liquid. Protein formulations can be obtained by using techniques known in the art. For instance, without being limited thereto, solid enzyme formulations can be obtained by extrusion or granulation. Suitable extrusion and granulation techniques are known in the art and are described for instance in WO 94 / 19444 A1 and WO 97 / 43482 A1 .Liquid mannanase formulations may comprise amounts of mannanase enzyme in the range of 0.5 % to 40 %, 0.5 % to 30 %, 0.5 % to 25 %, 0.5 % to 12 %, or preferably 0.5 % to 7.5 % by weight, all relative to the total weight of the enzyme formulation.In one embodiment, the mannanase formulation, in particular the liquid mannanase formulation, comprises in addition one or more additional compounds selected from the group consisting of solvent, salt, pH regulator, preservative, enzyme stabilizer, and thickening agent. Preferably, the mannanase formulation is essentially devoid of surfactants, i.e. the mannanase formulation comprises less than 1 % surfactant, preferably less than 0.5 % surfactant. The solvent may be water and / or an organic solvent. Aqueous mannanase formulations of the invention may comprise water in amounts of more than about 30 % by weight, more than about 40 % by weight, more than about 50 % by weight or more than aboutBASF SE 240828W00158 B19118WO60 % by weight, all relative to the total weight of the mannanase formulation. The mannanase-containing formulations of the invention may comprise an organic solvent in amounts of more than 30 %, more than 40 %, more than about 50 % by weight, more than about 60 % by weight, more than about 70 % by weight, or more than about 80 % by weight, all relative to the total weight of the mannanase formulation. The organic solvent may be a water-miscible solvent. The organic solvent may be one or more selected from the group consisting of glycerol, propanediol, polypropylene glycol, and polyethylene glycol.In one embodiment, the mannanase formulation comprises at least one preservative. Preferably, preservative means substances that are added to a liquid composition for the purpose of preservation, meaning more preferably that compounds known to have preserving features comprised in a liquid composition formed in the production process are excluded from the term preservatives. In one embodiment, the preservative is selected from the group consisting of 2- phenoxyethanol, glutaraldehyde, 2-bromo-2-nitropropane-1 ,3-diol, formic acid in acid form or as its salt, and 4, 4’ -dichloro 2-hydroxydiphenylether. Usually, the liquid compositions of the invention comprise at least one preservative in amounts below 10 ppm, such as in amounts ranging from 2 ppm to 5% by weight relative to the total weight of the liquid composition. Preferably, the mannanase formulation is free from preservatives, meaning that preservatives are comprised in amounts less than 1 ppm, preferably 0 ppm.An exemplary mannanase formulation comprises 20% to 80% glycerol and 1 to 10% citric acid with a pH of 5 to 7.In one embodiment, the composition comprising a variant polypeptide having mannanase activity of the present invention further comprises one or more additional enzymes different from the mannanase. Preferably, the additional enzyme is a protease, more preferably a serine protease (EC 3.4.21) and most preferably a subtilisin protease (EC 3.4.21.62). Subtilisin protease herein refers to a serine protease having the catalytic triad of subtilisin related proteases. Examples include the subtilisins as described in WO 89 / 06276 and EP 0283075, WO 89 / 06279, WO 89 / 09830, WO 89 / 09819, WO 91 / 06637 and WO 91 / 02722. For the purpose of the invention, at least one protease may be selected from the following: subtilisin from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J. Bacteriol. Volume 159, p. 811- 819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume 11 , p. 7911-7925); subtilisin from Bacillus licheniformis (subtilisin Carlsberg; disclosed in EL Smith et al. (1968) in J. Biol Chem, Volume 243, pp. 2184-2191 , and Jacobs et al. (1985) in Nucl. Acids Res, Vol 13, p. 8913-8926); subtilisin PB92 (original sequence of the alkaline protease PB92 is described in EP 283075 A2); subtilisin 147 and / or 309 (Esperase®, Savinase®, respectively) as disclosed in WO 89 / 06279; subtilisin from Bacillus lentus as disclosed in WO 91 / 02792, such as from Bacillus lentus DSM 5483 or the variants of Bacillus lentus DSM 5483 as described in WO 95 / 23221 ; subtilisin from Bacillus alcalophilus (DSM 11233) disclosed in DE 10064983; subtilisin from Bacillus gibsonii (DSM 14391) as disclosed in WO 2003 / 054184; subtilisin from Bacillus sp. (DSM 14390) disclosed in WO 2003 / 056017; subtilisin from Bacillus sp. (DSM 14392) disclosed in WO 2003 / 055974; subtilisin from Bacillus gibsonii (DSM 14393) disclosed in WO 2003 / 054184; subtilisin having SEQ ID NO: 4 as described in WO 2005 / 063974; subtilisin having SEQ ID NO: 4 as described in WO 2005 / 103244; subtilisin having SEQ ID NO: 7 as described in WO 2005 / 103244; and subtilisin having SEQ ID NO: 2 as described in application DE 102005028295.4. Further proteases are described in WO 2024 / 094735, WO 2024 / 094733, WO 2024 / 094732, EP 24 166 826.8, EP 24 166 833.4, EP 24 166 822.7, EP 24 166 830.0 and EP 24 166 835.9.Preferably, the mannanase formulation further comprising a protease also comprises an enzyme stabilizing system. In a mannanase formulation comprising a protease as an additional enzyme, the enzyme stabilizing system comprises preferably at least one compound selected from the group consisting of polyols (preferably, 1 ,3-propanediol, ethyleneBASF SE 240828W00159 B19118WO glycol, glycerol, 1 ,2-propanediol, or sorbitol), inorganic salts (preferably, CaCl2, MgCh, or NaCI), short chain (preferably, CrCs) carboxylic acids or salts thereof (preferably, formic acid, formate (preferably, sodium formate), acetic acid, acetate, or lactate), borate, boric acid, boronic acids (preferably, 4-formyl phenylboronic acid (4-FPBA)), peptide aldehydes (preferably, Benzyloxycarbony-VAL-H (Z-VAL-H or Cbz-VAL-H) or Benzyloxycarbony-GAY-H (Z-GAY-H or Cbz-GAY- H), peptide acetals, and peptide aldehyde hydrosulfite adducts. Preferably, the enzyme stabilizing system comprises a combination of at least two of the compounds selected from the group consisting of salts, polyols, and short chain carboxylic acids and preferably one or more of the compounds selected from the group consisting of borate, boric acid, boronic acids (preferably, 4-formyl phenylboronic acid (4-FPBA)), peptide aldehydes, peptide acetals, and peptide aldehyde hydrosulfite adducts. In a particularly preferred embodiment, the stabilizing system comprises a protease inhibitor, preferably selected from borate, boric acid, boronic acids (preferably, 4-FPBA), peptide aldehydes (preferably, peptide aldehydes like Z-VAL-H or Z-GAY-H), peptide acetals, and peptide aldehyde hydrosulfite adducts, preferably the protease inhibitor is a peptide aldehyde, preferably Z-VAL-H or Z-GAY-H. In one embodiment, the stabilizing system does not comprise a protease inhibitor. Preferably, the composition is boron-free. Preferably, the mannanase formulation comprises a calcium salt, preferably calcium chloride.In one embodiment, the mannanase formulation comprises a protease inhibitor, preferably a peptide aldehyde, in amounts in the range of about 0.04 % to 0.8 %, 0.04 % to 0.7 %, 0.04 % to 0.6 %, 0.04 % to 0.5%, 0.04 % to 0.4 % or 0.04 % to 0.3 % by weight relative to the total weight of the liquid mannanase variant formulation. Preferably, the peptide aldehyde is comprised in amounts in the range of about 0.1 % to 0.6 % by weight, of about 0.1 % to 0.5 % by weight, of about 0.1 % to 0.4 %, or of about 0.1 % to 0.35 % by weight, all relative to the total weight of the liquid mannanase formulation.Preferably, the liquid mannanase formulation comprises or consists of the variant polypeptide having mannanase activity of the present invention, a solvent, an enzyme stabilizing system, and optionally a preservative and optionally an additional enzyme different from the mannanase variant. Preferably, the formulation of the variant polypeptide having mannanase activity of the present invention is essentially devoid of surfactants, i.e. the mannanase formulation comprises less than 1 % surfactant, preferably less than 0.5 % surfactant.The present invention therefore also relates to a method for making a mannanase formulation, preferably a concentrated mannanase formulation, comprising the steps of mixing a) a variant polypeptide having mannanase activity of the present invention; and b) one or more components selected from the group consisting of solvent, enzyme stabilizing system, preservative, and an additional enzyme different from the mannanase.Further, the present invention relates to a method for improving mannanase stability in a composition with comprising the steps of mixing a) a variant polypeptide having mannanase activity of the present invention; and b) one or more components selected from the group consisting of solvent, enzyme stabilizing system, preservative, and an additional enzyme different from the mannanase.In one embodiment, the variant polypeptide having mannanase activity of the present invention is part of a microorganism (alive, attenuated or inactivated), probiotic, or prebiotic.BASF SE 240828W00160 B19118WOAdditional enzymesIn another embodiment, the composition comprising a variant polypeptide having mannanase activity of the present invention further comprises one or more additional enzymes different from the mannanase. Preferably, the additional enzyme is selected from the group consisting of amylases, lipases, proteases, mannanases other than the polypeptide having mannanase activity of the present invention, cellulases, hemicellulases, phospholipases, esterases, pectinases, lactases, peroxidases, xylanases, cutinases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, beta-glucanases, arabinosidases, hyaluronidases, chondroitinases, laccases, nucleases, ribonucleases (RNAses), deoxyribonucleases (DNAses), phosphodiesterases, phytases, carbohydrases, galactanases, xanthanases, xyloglucanases, oxidoreductases, perhydrolases, aminopeptidases, asparaginases, carbohydrases, carboxypeptidases, catalases, chitinases, cyclodextrin glycosyltransferases, alpha-galactosidases, beta-galactosidases, glucoamylases, alpha-glucosidases, betaglucosidases, invertases, transglutaminases and dispersins, and combinations of at least two of the foregoing types. More preferably, the additional enzyme is selected from the group consisting of amylases, lipases, proteases, mannanase other than the polypeptide having mannanase activity of the present invention, cellulases, esterases, xylanases, DNAses, dispersins, pectinases, oxidoreductases, and cutinases, and combinations of at least two of the foregoing types. Further preferred, the additional enzyme is selected from the group consisting of amylases, lipases, proteases, mannanases other than the polypeptide having mannanase activity of the present invention, cellulases, and combinations of at least two of the foregoing types. Most preferably, the additional enzyme is a protease.The composition of the present invention can comprise more than one enzyme of different types, e.g., a protease and a mannanase, or more than one enzyme of the same type, e.g., two or more different mannanases, or mixtures thereof, e.g., a protease and two different mannanases of which one is the variant polypeptide having mannanase activity of the present invention.Cleaning compositionsIn one embodiment, the present invention is directed to the use of the variant polypeptide having mannanase activity of the present invention in a cleaning composition. Thus, the present invention is also directed to a cleaning composition comprising the variant polypeptide having mannanase activity of the present invention and one or more adjunct cleaning additive.The publication IPCCM000274489D published on www.IP.com is regarded as Reference RF1 , which is incorporated herein by reference in its entirety. The publication Prior Art Disclosure; Issue 684; paragraphs

[3000] to

[3061] ; ISSN: 2198-4786; published: February 12, 2024 will be regarded as Reference RF2, which is incorporated herein by reference in its entirety.The phrase "cleaning composition" (also called “cleaning formulation”, “detergent composition”, “detergent formulation” or “detergent” herein), as used herein, includes compositions and formulations designed for cleaning soiled material. Such compositions and formulations include those designed for cleaning soiled material or surfaces of any kind, more preferably compositions for Fabric and Home Care. “Cleaning compositions” are defined in more detail in paragraphs

[0001] ,

[0002] ,

[0004] and

[0006] of Reference RF1.“Compositions for Fabric and Home Care” include cleaning compositions and formulations including but not limited to laundry cleaning compositions and detergents and hard surface cleaning compositions including dish washing compositions, more preferably liquid laundry formulations, solid laundry compositions, liquid manual dish washBASF SE 240828W00161 B19118WO formulations, automatic dish wash (ADW) gels and automatic dish wash (ADW) solid compositions. “Compositions for Fabric and Home Care” are defined in more detail in paragraph

[0003] of Reference RF1.The cleaning compositions of the invention including the inventive enzyme(s) may - and preferably do - contain adjunct cleaning additives (also abbreviated herein as “adjuncts”), such adjuncts being preferably in addition to a surfactant system as defined before.Suitable adjunct cleaning additives include polymers, surfactants or surfactant systems, builders, cobuilders, further enzymes, enzyme stabilizing systems, structurants or thickeners, clay soil removal / anti-redeposition agents, solubilizing agents, chelating agents, bleaching compounds, bleaching agents, bleach activators, bleach catalysts, brighteners, malodor control agents, pigments, dyes, opacifiers, hueing agents, dye transfer inhibiting agents, chelating agents, suds boosters, suds suppressors (antifoams), color speckles, silver care, anti-tarnish and / or anti-corrosion agents, alkalinity sources, pH adjusters, pH-buffer agents, hydrotropes, scrubbing particles, antibacterial agents, anti-oxidants, softeners, carriers, processing aids, pro-perfumes, dye fixation agent and perfumes.Thus, the present invention also relates to a method for making a cleaning composition comprising the steps of mixing a) a variant polypeptide having mannanase activity of the present invention; and b) one or more adjunct cleaning additives described herein.The present invention also refers to a method for making a cleaning composition with improved mannanase stability and / or for providing a cleaning composition with improved wash performance comprising the steps of mixing a) a variant polypeptide having mannanase activity of the present invention; and b) one or more adjunct cleaning additives described herein.The addition of the liquid mannanase formulation to a cleaning composition, preferably liquid cleaning composition, usually occurs in a weight ratio liquid mannanase formulation:cleaning composition of about 1 :1000, 1 :500, 1 :100, 1 :50, 1 :30, 1 :25, 1 :20, or 1 :10.In preferred embodiments, the cleaning compositions comprise the inventive enzyme(s) and a polymer, preferably cleaning polymers and / or soil release polymers. “Cleaning polymers and soil release polymers” are defined in more detail in paragraphs

[0032] to

[0034] of Reference RF1. These polymers include polycarboxylates, alkoxylated polyalkylenamines, alkoxylated polyalkylenimines, polyether-based polymers, rheology-modifying polymers, dye inhibition polymers and soil release polymers as defined in more detail in paragraphs

[3035] to

[3044] of Reference RF2. Polymers may include, without limitation, “multifunctional alkoxylated polyethylene imines”, “multifunctional alkoxylated diamines” and also terephthalic acid-based polyesters like Clariant’s TexCare®, such as TexCare® SRN 170, TexCare® SRN 172, TexCare® SRN 260, TexCare® SRN 260 SG Terra and TexCare® SRA 300 as well as distinct combinations of all of the before mentioned polymers. Also included are graft polymers comprising a polyalkylene oxide based backbone with grafted side chains of vinyl ester monomer and optionally N-vinylpyrrolidone monomers.In preferred embodiments, the cleaning compositions comprise the inventive enzyme(s) and a surfactant or surfactant system. “Surfactants” are anionic, non-ionic, cationic, amphoteric and zwitter-ionic surfactants defined in more detail in paragraphs

[3008] to

[3034] of Reference RF2. In addition, these surfactants are also described in more detail in paragraphs

[0007] to

[0013] of Reference RF1 .Anionic surfactants for inventive cleaning compositions include linear alkylbenzenesulfonates (LAS), alkyl sulfates (AS), alkyl alkoxy sulfates (AES), alkyl alkoxy carboxylates, modified alkylbenzene sulfonate (MLAS), methyl ester sulfonate (MES), alkyl sulfosuccinates, alpha-olefin sulfonate (AOS), alkyl polyglycosides (APG) and biosurfactants, such asBASF SE 240828W00162 B19118WO rhamnolipids and sophorolipids. Non-ionic surfactants for inventive cleaning compositions include alkoxylates, alkoxylated alcohols, alkoxylated fatty acids and alkoxylated (poly-)saccharides. Cationic surfactants for inventive cleaning compositions include surfactants comprising a quaternary ammonium. Amphoteric surfactants for inventive cleaning compositions include amine oxides. Zwitter-ionic surfactants for inventive cleaning compositions include betaines.In preferred embodiments, the cleaning compositions comprise the inventive enzyme(s) and a builder. “Builders” are defined in more detail in paragraphs

[0014] to

[0018] of Reference RF1. These builders include non-phosphate based builders (NPB) and phosphonates (CoP) described in more detail in paragraphs

[3001] to

[3005] of Reference RF2.Builders may include, without limitation, methylglycinediaceticacid (MGDA), ethylenediaminedisuccinic acid (EDDS), glutamic acid diacetate (GLDA), citric acid and salts thereof.In preferred embodiments, the cleaning compositions comprise the inventive enzyme(s) and an additional enzyme. “(Additional) enzymes” are defined in more detail in paragraphs

[0020] to

[0027] of Reference RF1.These additional enzymes may include hydrolases, such as (additional) mannanases, amylases, lipases, DNases, cellulases, hemicellulases, phospholipases, esterases, proteases, xylanases, dispersins, oxidoreductases, cutinases, pectate lyases, pectinases, lactases and peroxidases. In more preferred embodiments, the cleaning composition comprises, in addition to the inventive compound(s), an enzyme stabilizing system as described herein or in the chapter “Enzyme stabilizing system” of Reference RF1 , preferably comprising a protease inhibitor, preferably selected from borate, boric acid, boronic acids (preferably, 4-FPBA), peptide aldehydes (preferably, peptide aldehydes like Z-VAL-H or Z-GAY-H), peptide acetals, and peptide aldehyde hydrosulfite adducts, preferably the protease inhibitor is a peptide aldehyde, preferably Z-VAL-H and / or Z-GAY-H. Preferably, the protease inhibitor is Z-VAL-H and / or Z-GAY-H.In preferred embodiments, the cleaning compositions comprise the inventive enzyme(s) and a biocide. “Biocides” are defined in more detail in paragraphs

[0035] and

[0036] of Reference RF1. These biocides also include compounds as defined in more detail in paragraphs

[3006] and

[3007] of Reference RF2.Biocides may include, without limitation, 2-phenoxyethanol and 4,4’-dichoro 2-hydroxydiphenylether.Further adjunct cleaning additives are included and described in more detail in paragraphs

[0005] ,

[0019] ,

[0028] to

[0031] and

[0037] to

[0039] of Reference RF1 .Liquid laundry formulations, solid laundry compositions, liquid manual dish wash formulations, automatic dish wash (ADW) gels and automatic dish wash (ADW) solid compositions comprising inventive enzyme(s) are defined in more detail in paragraph

[0044] of Reference RF1.Method of useThe variant polypeptide having mannanase activity of the present invention can be used in various applications.The variant polypeptide having mannanase activity of the present invention or a composition comprising said variant polypeptide having mannanase activity of the present invention may be used in cleaning, food processing, animal feed, pulp and paper processing, baking, mining and oil well service, textile processing, leather processing, water treatment, brewery, ethanol production, circular economy, waste treatment, or recycling.The present invention is also directed to the use of a variant polypeptide having mannanase activity of the present invention in a cleaning process such as laundry or hard surface cleaning, preferably for home care or l&l cleaning. The variant polypeptide having mannanase activity of the present invention or a composition comprising said polypeptideBASF SE 240828W00163 B19118WO may be used in various industrial and institutional cleaning applications, including commercial laundry such as on premise laundry or tunnelwashing, mechanical ware wash such as in a hood machine or in a tunnelwasher, manual dish wash cleaning, carpet cleaning, open plant cleaning (outside pipe cleaning), cleaning in place (inside pipe cleaning), membrane cleaning such as in dairy, food, beverage or water treatment, vehicle care such as pad cleaning, microorganism removal, virus removal, insect removal or malodor removal or veterinary cleaning. The variant polypeptide having mannanase activity of the present invention or a composition comprising said polypeptide may also be used in textile processing, leather processing or water treatment.The variant polypeptide having mannanase activity of the present invention or a composition comprising said polypeptide may be used in the bioenergy industry, in particular in bioethanol production, oil and gas recovery, in particular liquefaction for improved oil recovery and food processing, in particular beverage production and / or processing.The present invention also refers to the use of a variant polypeptide having mannanase activity of the present invention for providing a cleaning composition with improved mannanase stability and / or for providing a cleaning composition with improved wash performance, preferably on mannanase sensitive stains.Thus, the present invention therefore also refers to a method for cleaning, preferably laundry or hard surface cleaning, comprising the step of contacting a subject, preferably a textile or a hard surface, with a composition comprising a variant polypeptide having mannanase activity of the present invention, preferably wherein the composition comprises at least one additional adjunct cleaning additive, preferably a surfactant and / or a builder.Further, the present invention also refers to a method for improving mannanase stability in a cleaning composition and / or for improving wash performance of a cleaning composition, preferably on mannanase-sensitive stains comprising the step of formulating a variant polypeptide having mannanase activity of the present invention in a cleaning composition. The present invention also refers to a method of laundering fabric or of cleaning hard surfaces, which method comprises treating a fabric or a hard surface with a composition comprising the variant polypeptide having mannanase activity of the present invention and further comprising 4, 4’ -dichloro 2-hydroxydiphenylether.In one embodiment, the variant polypeptide having mannanase activity of the present invention is used to improve the sustainability profile of a composition or a method and / or are used in circular economy. With respect to the use in circular economy, the variant polypeptide having mannanase activity of the present invention can be used in waste treatment or recycling.In one embodiment the present invention is directed to a process for waste treatment, preferably for solubilizing waste, comprising the step of contacting waste with a variant polypeptide having mannanase activity of the present invention and preferably with one or more enzymes selected from the group consisting of lipase, glucanase, amylase, pectate lyase, and mannanase, under conditions supporting enzymatic solubilizations of the waste. In one embodiment, the waste is municipal solid waste. In one embodiment, the liquified waste can be used as substrate for microbial fermentation.While the invention has been illustrated and described in detail in the drawings and foregoing description, such illustration and description are to be considered illustrative or exemplary and not restrictive. The invention is not limited to the disclosed embodiments. Other variations to the disclosed embodiments can be understood and effected by those skilled in the art in practicing a claimed invention, from a study of the drawings, the disclosure, and the dependent claims. The detailed description is merely exemplary in nature and is not intended to limit application and uses. The following examples further illustrate the present invention without, however, limiting the scope of the invention thereto. VariousBASF SE 240828W001B19118WO changes and modifications can be made by those skilled in the art on the basis of the description of the invention, and such changes and modifications are also included in the present invention.BASF SE 240828W00165 B19118WOSome preferred embodiments of the present invention include:1 . A variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 , and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.2. The variant polypeptide of embodiment 1 , wherein the variant polypeptide has an amino acid sequence which is 87.0% to 91 .0% identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 .3. The variant polypeptide of any one of the preceding embodiments, wherein the at least one amino acid substitution is selected from the group consisting of X58G / A / P and X72L / MA / .4. The variant polypeptide of any one of the preceding embodiments, wherein the variant polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.5. The variant polypeptide of embodiment 4, wherein:(a) the amino acid substitution at amino acid residue 79 is X79K / H / R; and / or(b) the amino acid substitution at amino acid residue 92 is X92 K / E / Q / R / H; and / or(c) the amino acid substitution at amino acid residue 94 is X94D / E / N / K / Q; and / or(d) the amino acid substitution at amino acid residue 96 is X96E / D / K / Q; and / or(e) the amino acid substitution at amino acid residue 100 is X100R / K / Q.6. The variant polypeptide of any one of the preceding embodiments, wherein the variant polypeptide additionally comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.7. The variant polypeptide of embodiment 6, wherein the amino acid substitution at amino acid residue 234 is X234Q / T.8. The variant polypeptide of any one of the preceding embodiments, wherein the polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.9. The variant polypeptide of embodiment 8, wherein:(a) the amino acid substitution at amino acid residue 103 is X103N / D; and / or(b) the amino acid substitution at amino acid residue 107 is X107E; and / or(c) the amino acid substitution at amino acid residue 201 is X201 L; and / or(d) the amino acid substitution at amino acid residue 205 is X205N; and / or(e) the amino acid substitution at amino acid residue 225 is X225Y; and / or(f) the amino acid substitution at amino acid residue 251 is X251 L; and / or(g) the amino acid substitution at amino acid residue 256 is X256S; and / or(h) the amino acid substitution at amino acid residue 257 is X257T; and / orBASF SE 240828W00166 B19118WO(i) the amino acid substitution at amino acid residue 258 is X258D; and / or(j) the amino acid substitution at amino acid residue 260 is X260A; and / or(k) the amino acid substitution at amino acid residue 269 is X269S; and / or(l) the amino acid substitution at amino acid residue 271 is X271 N; and / or(m) the amino acid substitution at amino acid residue 272 is X272S; and / or(n) the amino acid substitution at amino acid residue 275 is X275D; and / or(o) the amino acid substitution at amino acid residue 280 is X280V; and / or(p) the amino acid substitution at amino acid residue 282 is X282Y / F; and / or(q) the amino acid substitution at amino acid residue 284 is X284E; and / or(r) the amino acid substitution at amino acid residue 293 is X293L; and / or(s) the amino acid substitution at amino acid residue 295 is X295G; and / or(t) the amino acid substitution at amino acid residue 299 is X299S / L.10. The variant polypeptide of any one of the preceding embodiments, wherein said variant polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .11. The variant polypeptide of embodiment 10, wherein:(a) the amino acid substitution at amino acid residue 2 is X2S; and / or(b) the amino acid substitution at amino acid residue 5 is X5H; and / or(c) the amino acid substitution at amino acid residue 7 is X7S; and / or(d) the amino acid substitution at amino acid residue 29 is X29T / A; and / or(e) the amino acid substitution at amino acid residue 31 is X31 Y; and / or(f) the amino acid substitution at amino acid residue 33 is X33S; and / or(g) the amino acid substitution at amino acid residue 41 is X41 G; and / or(h) the amino acid substitution at amino acid residue 44 is X44N; and / or(i) the amino acid substitution at amino acid residue 59 is X59V; and / or(j) the amino acid substitution at amino acid residue 66 is X66D; and / or(k) the amino acid substitution at amino acid residue 71 is X71V; and / or(l) the amino acid substitution at amino acid residue 97 is X97A; and / or(m) the amino acid substitution at amino acid residue 99 is X99M; and / or(n) the amino acid substitution at amino acid residue 108 is X108L; and / or(o) the amino acid substitution at amino acid residue 110 is X110D; and / or(p) the amino acid substitution at amino acid residue 111 is X111 T; and / or(q) the amino acid substitution at amino acid residue 118 is X118K; and / or(r) the amino acid substitution at amino acid residue 134 is X134G; and / or(s) the amino acid substitution at amino acid residue 135 is X135G; and / or(t) the amino acid substitution at amino acid residue 138 is X138E; and / or(u) the amino acid substitution at amino acid residue 158 is X158I; and / or(v) the amino acid substitution at amino acid residue 160 is X160A; and / orBASF SE 240828W00167 B19118WO(w) the amino acid substitution at amino acid residue 168 is X168K / Q; and / or(x) the amino acid substitution at amino acid residue 175 is X175Q; and / or(y) the amino acid substitution at amino acid residue 182 is X182T; and / or(z) the amino acid substitution at amino acid residue 243 is X243T; and / or(aa) the amino acid substitution at amino acid residue 259 is X259M; and / or(bb) the amino acid substitution at amino acid residue 289 is X289E.12. The variant polypeptide of any one of the preceding embodiments, wherein said variant polypeptide has a length of 200 to 350 amino acids, preferably of 299 amino acids.13. The variant polypeptide of any one of the preceding embodiments, wherein said variant polypeptide does not comprise amino acids 300 to 460 of SEQ ID NO: 1 .14. The variant polypeptide of any one of the preceding embodiments, wherein said variant polypeptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14.15. A variant polypeptide having mannanase activity, wherein:(i) the polypeptide has an amino acid sequence which is at least 85% identical to an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.16. The variant polypeptide of embodiment 15, wherein the at least one amino acid substitution is selected from the group consisting of X58G / A / P and X72L7M / V.17. The variant polypeptide of embodiment 15 or 16, wherein the variant polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .18. The variant polypeptide of embodiment 17, wherein:(a) the amino acid substitution at amino acid residue 79 is X79K / H / R; and / or(b) the amino acid substitution at amino acid residue 92 is X92 K / E / Q / R / H; and / or(c) the amino acid substitution at amino acid residue 94 is X94D / E / N / K / Q; and / or(d) the amino acid substitution at amino acid residue 96 is X96E / D / K / Q; and / or(e) the amino acid substitution at amino acid residue 100 is X100R / K / Q.19. The variant polypeptide of any one of embodiments 15 to 18, wherein the variant polypeptide additionally comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.20. The variant polypeptide of embodiment 19, wherein the amino acid substitution at amino acid residue 234 is X234Q / T.21 . The variant polypeptide of any one of embodiments 15 to 20, wherein the polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205,BASF SE 240828W00168 B19118WO225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .22. The variant polypeptide of embodiment 21 , wherein:(a) the amino acid substitution at amino acid residue 103 is X103N / D; and / or(b) the amino acid substitution at amino acid residue 107 is X107E; and / or(c) the amino acid substitution at amino acid residue 201 is X201 L; and / or(d) the amino acid substitution at amino acid residue 205 is X205N; and / or(e) the amino acid substitution at amino acid residue 225 is X225Y; and / or(f) the amino acid substitution at amino acid residue 251 is X251 L; and / or(g) the amino acid substitution at amino acid residue 256 is X256S; and / or(h) the amino acid substitution at amino acid residue 257 is X257T; and / or(i) the amino acid substitution at amino acid residue 258 is X258D; and / or(j) the amino acid substitution at amino acid residue 260 is X260A; and / or(k) the amino acid substitution at amino acid residue 269 is X269S; and / or(l) the amino acid substitution at amino acid residue 271 is X271 N; and / or(m) the amino acid substitution at amino acid residue 272 is X272S; and / or(n) the amino acid substitution at amino acid residue 275 is X275D; and / or(o) the amino acid substitution at amino acid residue 280 is X280V; and / or(p) the amino acid substitution at amino acid residue 282 is X282Y / F; and / or(q) the amino acid substitution at amino acid residue 284 is X284E; and / or(r) the amino acid substitution at amino acid residue 293 is X293L; and / or(s) the amino acid substitution at amino acid residue 295 is X295G; and / or(t) the amino acid substitution at amino acid residue 299 is X299S / L.23. The variant polypeptide of any one of embodiments 15 to 22, wherein said polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .24. The variant polypeptide of embodiment 23, wherein:(a) the amino acid substitution at amino acid residue 2 is X2S; and / or(b) the amino acid substitution at amino acid residue 5 is X5H; and / or(c) the amino acid substitution at amino acid residue 7 is X7S; and / or(d) the amino acid substitution at amino acid residue 29 is X29T / A; and / or(e) the amino acid substitution at amino acid residue 31 is X31 Y; and / or(f) the amino acid substitution at amino acid residue 33 is X33S; and / or(g) the amino acid substitution at amino acid residue 41 is X41 G; and / or(h) the amino acid substitution at amino acid residue 44 is X44N; and / or(i) the amino acid substitution at amino acid residue 59 is X59V; and / or(j) the amino acid substitution at amino acid residue 66 is X66D; and / or(k) the amino acid substitution at amino acid residue 71 is X71V; and / orBASF SE 240828W00169 B19118WO(l) the amino acid substitution at amino acid residue 97 is X97A; and / or(m) the amino acid substitution at amino acid residue 99 is X99M; and / or(n) the amino acid substitution at amino acid residue 108 is X108L; and / or(o) the amino acid substitution at amino acid residue 110 is X110D; and / or(p) the amino acid substitution at amino acid residue 111 is X111 T; and / or(q) the amino acid substitution at amino acid residue 118 is X118K; and / or(r) the amino acid substitution at amino acid residue 134 is X134G; and / or(s) the amino acid substitution at amino acid residue 135 is X135G; and / or(t) the amino acid substitution at amino acid residue 138 is X138E; and / or(u) the amino acid substitution at amino acid residue 158 is X158I; and / or(v) the amino acid substitution at amino acid residue 160 is X160A; and / or(w) the amino acid substitution at amino acid residue 168 is X168K / Q; and / or(x) the amino acid substitution at amino acid residue 175 is X175Q; and / or(y) the amino acid substitution at amino acid residue 182 is X182T; and / or(z) the amino acid substitution at amino acid residue 243 is X243T; and / or(aa) the amino acid substitution at amino acid residue 259 is X259M; and / or(bb) the amino acid substitution at amino acid residue 289 is X289E.25. A variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 85% identical to the amino acid sequence according to SEQ ID NO: 7, and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.26. The variant polypeptide of embodiment 25, wherein the at least one amino acid substitution is selected from the group consisting of X58G / A / P and X72L7M / V.27. The variant polypeptide of embodiment 25 or 26, wherein the variant polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .28. The variant polypeptide of embodiment 27, wherein:(a) the amino acid substitution at amino acid residue 79 is X79K / H / R; and / or(b) the amino acid substitution at amino acid residue 92 is X92 K / E / Q / R / H; and / or(c) the amino acid substitution at amino acid residue 94 is X94D / E / N / K / Q; and / or(d) the amino acid substitution at amino acid residue 96 is X96E / D / K / Q; and / or(e) the amino acid substitution at amino acid residue 100 is X100R / K / Q.29. The variant polypeptide of any one of embodiments 25 to 28, wherein the variant polypeptide additionally comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.30. The variant polypeptide of embodiment 29, wherein the amino acid substitution at amino acid residue 234 is X234Q / T.BASF SE 240828W00170 B19118WO31 . The variant polypeptide of any one of embodiments 25 to 30, wherein the polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 282 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .32. The variant polypeptide of embodiment 31 , wherein:(a) the amino acid substitution at amino acid residue 282 is X282Y / F; and / or(b) the amino acid substitution at amino acid residue 299 is X299S / L.33. The variant polypeptide of any one of embodiments 25 to 32, wherein the polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 225 and 251 .34. The variant polypeptide of embodiment 33, wherein:(a) the amino acid substitution at amino acid residue 103 is X103N / D; and / or(b) the amino acid substitution at amino acid residue 225 is X225Y; and / or(c) the amino acid substitution at amino acid residue 251 is X251 L.35. The variant polypeptide of any one of embodiments 25 to 34, wherein the polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 256, 257, 258, 269, 271 , 272, 275, 280, 284, 293 and 295.36. The variant polypeptide of embodiment 35, wherein:(a) the amino acid substitution at amino acid residue 256 is X256S; and / or(b) the amino acid substitution at amino acid residue 257 is X257T; and / or(c) the amino acid substitution at amino acid residue 258 is X258D; and / or(d) the amino acid substitution at amino acid residue 269 is X269S; and / or(e) the amino acid substitution at amino acid residue 271 is X271 N; and / or(f) the amino acid substitution at amino acid residue 272 is X272S; and / or(g) the amino acid substitution at amino acid residue 275 is X275D; and / or(h) the amino acid substitution at amino acid residue 280 is X280V; and / or(i) the amino acid substitution at amino acid residue 284 is X284E; and / or(j) the amino acid substitution at amino acid residue 293 is X293L; and / or(k) the amino acid substitution at amino acid residue 295 is X295G.37. The variant polypeptide of any one of embodiments 25 to 36, wherein the polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 107, 201 , 205 and 260.38. The variant polypeptide of embodiment 37, wherein:(a) the amino acid substitution at amino acid residue 107 is X107E; and / or(b) the amino acid substitution at amino acid residue 201 is X201 L; and / or(c) the amino acid substitution at amino acid residue 205 is X205N; and / or(d) the amino acid substitution at amino acid residue 260 is X260A.39. A variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 90%, identical to the amino acid sequence according to SEQ ID NO: 7, andBASF SE 240828W00171 B19118WO(ii) comprises an amino acid substitution at amino acid residues 58, 72, 79, 92, 94, 96, 100, 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.40. The variant polypeptide of embodiment 39, wherein the polypeptide comprises the amino acid substitutions S58G, I72L, N79K, N92K, A94D, S96E, D100R, S103N, S107E, S201 L, S205N, K225Y, E234Q, S251 L, G256S, P257T, E258D, S260A, A269S, D271 N, N272S, S275D, I280V, N282Y, A284E, I293L, P295G and G299S.41 . A variant polypeptide having mannanase activity, wherein the variant polypeptide has an amino acid sequence with a sequence identity of at least 91 %, at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.1 %, at least 97.2%, at least 97.3%, at least 97.4%, at least 97.5%, at least 97.6%, at least 97.7%, at least 97.8%, at least 97.9%, at least 98%, at least 98.1 %, at least 98.2%, at least 98.3%, at least 98.4%, at least 98.5%, at least 98.6%, at least 98.7%, at least 98.8%, at least 98.9%, at least 99%, at least 99.1 %, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, at least 99.9% or of 100% to the amino acid sequence according to any one of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14, preferably to the amino acid sequence according to SEQ ID NO: 7.42. The variant polypeptide of any one of the preceding embodiments, wherein the polypeptide exhibits one or more improved properties compared to the mannanase according to SEQ ID NO: 15, preferably wherein the improved properties are selected from:(i) increase in stability,(ii) increase in storage stability,(iii) increase in storage stability in an enzyme formulation, and(iv) increase in storage stability in a detergent composition.43. A polynucleotide encoding the variant polypeptide of any one of the preceding embodiments.44. A composition comprising the variant polypeptide of any one of embodiments 1 to 42and at least one additional component.45. The composition of embodiment 44, wherein the composition comprises one or more additional enzymes different from the variant polypeptide referred to in any of embodiments 1 to 42.46. The composition of embodiment 45, wherein the one or more additional enzymes are selected from the group consisting of protease, amylase, cellulase, oxidoreductase, transferase, hydrolase, lyase, isomerase, ligase, aminopeptidase, asparaginase, carbohydrase, carboxypeptidase, catalase, chitinase, cutinase, cyclodextrin glycosyltransferase, deoxyribonuclease, endo-beta 1 ,3 glucanase, endo- beta 1 ,4 glucanase, xanthan endoglucanase, esterase, alpha-galactosidase, betagalactosidase, glucoamylase, alpha-glucosidase, beta-glucosidase, glycosyl hydrolase, hyaluronic acid synthase, invertase, laccase, lipase, mannosidase, mutanase, oxidase, a pectinolytic enzyme, peroxidase, phytase, polyphenoloxidase, pullulanase, ribonuclease, transglutaminase, dispersin, and xylanase, preferably protease, amylase or cellulase, most preferably protease.47. The composition of embodiment 45 or 46, wherein the additional enzyme is a protease.48. A detergent composition comprising the variant polypeptide of any one of embodiments 1 to 42, preferably a laundry detergent composition or a hard surface cleaning detergent composition.BASF SE 240828W00172 B19118WO49. The detergent composition of embodiment 48, wherein the composition comprises one or more surfactants and / or one or more builders, preferably a strong sequestering builder.50. The detergent composition of embodiment 48 or 49, wherein the composition comprises a builder, wherein the builder is selected from MDGA, GLDA, DTPMP, HEDP, and EDDS, preferably MDGA or EDDS.51 . The detergent composition of embodiment 49, wherein the composition comprises a surfactant, wherein the surfactant is selected from non-ionic surfactant, anionic surfactant, cationic surfactant, amphoteric surfactant, and combinations thereof.52. The detergent composition of any one of embodiments 48 to 50, wherein the detergent composition is devoid of anionic surfactants.53. The detergent composition of any one of embodiments 49 to 52 wherein the surfactant and / or the builder is bio-degradable and / or bio-based.54. The detergent composition of any one of embodiments 48 to 53, wherein the detergent composition is liquid or solid.55. The detergent composition of any one of embodiments 48 to 53, wherein the detergent composition is in the form of a pouch.56. The detergent composition of any one of embodiments 48 to 55, wherein the detergent composition is a liquid laundry detergent composition.57. The detergent composition of any one of embodiments 48 to 56, wherein the detergent composition does not comprise a preservative.58. The detergent composition of any one of embodiments 48 to 57, wherein the composition further comprises 2-phenoxyethanol, 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.59. The detergent composition of any one of embodiments 48 to 58, wherein the composition further comprises 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.60. The detergent composition of any one of embodiments 48 to 51 and 53 to 59, wherein the composition comprises 5% to 10% LAS and / or greater than 50% water.61 . A detergent composition comprising the variant polypeptide of any one of embodiments 1 to 42 and a protease, preferably a laundry detergent composition or a hard surface cleaning detergent composition.62. The detergent composition of embodiment 61 , wherein the composition comprises one or more surfactants and / or one or more builders, preferably a strong sequestering builder.63. The detergent composition of embodiment 62, wherein the composition comprises a builder, wherein the builder is selected from MDGA, GLDA, DTPMP, HEDP, and EDDS, preferably MDGA or EDDS.64. The detergent composition of embodiment 62, wherein the composition comprises a surfactant, wherein the surfactant is selected from non-ionic surfactant, anionic surfactant, cationic surfactant, amphoteric surfactant, and combinations thereof.65. The detergent composition of any one of embodiments 61 to 63, wherein the detergent composition is devoid of anionic surfactants.BASF SE 240828W00173 B19118WO66. The detergent composition of any one of embodiments 62 to 65, wherein the surfactant and / or the builder is bio-degradable and / or bio-based.67. The detergent composition of any one of embodiments 61 to 66, wherein the detergent composition is liquid or solid.68. The detergent composition of any one of embodiments 61 to 66, wherein the detergent composition is in the form of a pouch.69. The detergent composition of any one of embodiments 61 to 67, wherein the detergent composition is a liquid laundry detergent composition.70. The detergent composition of any one of embodiments 61 to 69, wherein the detergent composition does not comprise a preservative.71 . The detergent composition of any one of embodiments 61 to 70, wherein the composition further comprises 2-phenoxyethanol, 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.72. The detergent composition of any one of embodiments 61 to 71 , wherein the composition further comprises 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.73. The detergent composition of any one of embodiments 61 to 64 and 66 to 72, wherein the composition comprises 5 to 10% LAS and / or greater than 50% water.74. The detergent composition of any one of embodiments 61 to 73, wherein the composition further comprises a protease inhibitor as enzyme stabilizer, preferably a peptide aldehyde, more preferably Z-VAL-H or Z-GAY-H.ExamplesMaterial and Methods1. Library GenerationGenes encoding mannanases were cloned by restriction-ligation based standard protocols into a gram-positive expression vector comprising a promoter sequence, a sequence coding for a secretion signal peptide, and a ribosome binding site. Post reaction, the plasmid assembly mixtures were transformed into B. subtilis PY79 by established naturalcompetency transformation methods. Successful transformations were selected by plating on LB agar plates supplemented with 20 pg / ml kanamycin sulfate and incubating overnight at 37°C. After overnight selection, colonies were isolated by plate washing with LB media and pelleted by centrifugation, and plasmid DNA was isolated by alkaline lysis method with a Qiagen QIAprep Spin Miniprep Kit. The isolated DNA was transformed into electrocompetent Bacillus licheniformis cells. The cells were electroporated with a Bio-Rad Gene Pulser Xcell per manufacturer’s instructions. Cells were immediately rescued after the shock by addition of 1 ml of the osmolyte-dense rich medium. After two hours of recovering at 37°C, the successful transformants, i.e. cells containing the genes encoding mannanases, were then selected by plating on LB agar plates supplemented with 20 pg / ml kanamycin sulfate and incubating overnight at 37°C.2. Preparation and expression of variantsSingle colonies of the mannanase expression strains were picked into 600 pL of rich medium (TB broth) supplemented with 20 pg / mL kanamycin sulfate in a 96-well plate. The cultures were grown at 37°C with shaking at 1000 rpm for 16BASF SE 240828W00174 B19118WO hours to 18 hours, then 6 pL of culture was used to inoculate 600 pL of defined glucose-mineral media as defined in Tables 3 and 4 below with 20 pg / mL kanamycin sulfate in a 96 well plate.Table 3: Composition of initial fermentation medium.Table 4: Trace element composition of the trace element solution comprising 40 g / L citric acidThe cultures were grown at 37 °C with shaking at 1000 rpm with a throw of 3 mm for 48 hours, after which the supernatant was harvested by pelleting the cells by centrifugation and removing the residual culture liquid. The harvested supernatant is referred to as the enzyme solution and had a mannanase concentration in the range of 0.3 g / L to 3.0 g / L as determined using LabChip.3. Mannanase Activity AssaysMannanase activity was determined by using a commercial assay available from the company Megazyme using an Azo- Carob Galactomannan substrate (Azo-CGM). Azo-CGM is an abbreviation for Azo-Carob Galactomannan, a decorated starch which can be cleaved by endo-beta (1-4)-mannanases. Following mannanase cleavage of the substrate for a specific time (1 hour for this assay) the reaction is stopped by quenching with ethanol. The product is separated from the un-hydrolyzed remaining substrate by centrifugation. The supernatant (hydrolyzed product) is transferred to a fresh plate followed by absorbance spectrophotometry at 590 nm. Mannanase samples were diluted in assay buffer (50 mM HEPES,BASF SE 240828W00175 B19118WO pH 8.0) after each stability challenge (detergent or formulation) prior to activity assessment, for example reaching a preassay dilution between 4 to 240 fold, depending on their expression levels, from the stability solution. The assay was conducted by transferring 100 pi L of diluted enzyme samples to a 96 well microtiter plate containing 100 pi L substrate working solution. The solution was mixed at room temperature, incubated for 1 hour, then activity was stopped by transfer of 100 pi L of the solution into 150 pi L of 95 % ethanol and mixing. The solution was separated by centrifugation at 4000 x g for 10 minutes. 125 pi I of supernatant was transferred to a fresh plate and absorbance was read at 590 nm using a standard plate reader (BioTek Synergy Neo® or Neo2®). The change in absorbance was calculated for each sample by subtracting the no enzyme control absorbance and the residual activity was calculated by dividing the activity after storage time with the activity of the sample at the initial time point.Example 1 : Storage stability assessment of mannanase variants from combinatorial librariesNovel mannanase variants were expressed in 96 deep well plates (DWP) as described in Materials and Methods. To assess the detergent stability, the supernatants containing the expressed mannanase variants were diluted into model B liquid detergent (see T able 6) under the conditions described in T able 5 and subjected to thorough mixing. The solution was equilibrated for 1 hour and then measured for activity with the azo galactomannan assay as described in the Materials and Methods section. This was considered the initial time point (unstressed sample). The sample-containing plate was sealed and placed at elevated temperatures (45°C) for a duration of 14 days. At designated time points during incubation, the mannanase activity of the stressed sample was measured and compared to the unstressed control to compute the residual activity, which is defined as the activity after storage at 45°C divided by the activity at the initial time point. The residual activity of the novel mannanase variants according to SEQ ID NOs: 3 to 14 in detergent is given in Table 7.Table 5. Challenge conditions for stability studiesTable 6. Model B detergent for stability studiesAEO: C13 / C15Oxo-alcohol (7EO) Lutensol® AO7 (BASF SE)BASF SE 240828W00176 B19118WOLAS: Linear alkylbenzene sulfonic acid Maranil® DBS / LC (BASF SE)SLES: sodium lauryl ether sulfate Texapon N 70 (BASF SE) 1 ,2-propyleneglycol.In the table above the concentrations of the surfactant trade products are given.Table 7: Stability of variants in detergent"Defined here as the activity after storage at 45°C for 14 days divided by the activity at the initial time pointT able 7 demonstrates that a mutation at position 58 and / or 72 of the mannanase sequence leads to a significant increase in stability compared to mannanases without this mutation. The residual activity of the mannanase variant according to SEQ ID NO: 1 in detergent was also tested, but did not show any measurable result under the tested conditions. In parallel, the residual activity of the mannanase variant according to SEQ ID NO: 15 in detergent was tested as reference,BASF SE 240828W00177 B19118WO wherein the residual activity was defined as the activity after storage at 37°C for 14 days divided by the activity at the initial time point. Under said conditions, the mannanase variant according to SEQ ID NO: 15 in detergent showed a residual activity of 0.74, i.e. a lower stability compared to the novel mannanase variants in detergent as shown in Table 7.Example 2: Formulation stability assessment of mannanase variants from combinatorial librariesThe mannanase variants were subjected to stability studies in a possible enzyme formulation (see Table 9) including protease and under the conditions described in Table 8 and stability was monitored at 45°C over time.Table 8. Challenge conditions for stability studiesTable 9. Model enzyme formulation solution for stability studiesThe solution was equilibrated for 1 hour and then measured for activity with the azo galactomannan assay as described in the Materials and Methods section. This was considered the initial time point (unstressed sample). The samplecontaining enzyme formulation plate was then sealed and placed at elevated temperatures (45 °C) for a duration of one to 28 days. At designated time points during incubation, the mannanase activity of the stressed sample was measured and compared to the unstressed control to compute the residual activity, which is defined as the activity after storage at 45°C divided by the activity at the initial time point. The residual activity of the novel mannanase variants according to SEQ ID NOs: 3 to 14 given in Table 10 is the residual activity in formulated enzyme product.BASF SE 240828W00178 B19118WOTable 10: Stability of variants in enzyme formulation"Defined here as the activity after storage at 45°C for 28 days divided by the activity at the initial time pointTable 10 demonstrates that a mutation at position 58 and / or 72 of the mannanase sequence leads to a significant increase in stability compared to mannanases without a mutation at this position. The residual activity of the mannanase variant according to SEQ ID NO: 1 in formulated enzyme product was also tested, but did not show any measurable result under the tested conditions. In parallel, the residual activity of the mannanase variant according to SEQ ID NO: 15 in formulated enzyme product was tested as reference, wherein the residual activity was defined as the activity after storage at 37°C for 28 days divided by the activity at the initial time point. Under said conditions, the mannanase variant according to SEQ ID NO: 15 in formulated enzyme product showed a residual activity of 0.58, hence a lower stability compared to the novel mannanase variants in formulated enzyme product as shown in Table

Claims

1. BASF SE 240828W00179 B19118WOCLAIMS1 . A variant polypeptide having mannanase activity, wherein the variant polypeptide:(i) has an amino acid sequence which is at least 81 %, but less than 100%, identical to amino acids 1 to 299 of the amino acid sequence as set forth in SEQ ID NO: 1 , and(ii) comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.

2. The variant polypeptide of claim 1 , wherein:(a) the amino acid substitution at amino acid residue 58 is X58G / A / P; and / or(b) the amino acid substitution at amino acid residue 72 is X72L / M Z.

3. The variant polypeptide of claim 1 or 2, wherein the variant polypeptide additionally comprises an amino acid substitution at amino acid residue 100, preferably wherein the amino acid substitution at amino acid residue 100 is X100R / K / Q.

4. The variant polypeptide of any one of the preceding claims, wherein the variant polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94 and 96 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.

5. The variant polypeptide of claim 4, wherein:(a) the amino acid substitution at amino acid residue 79 is X79K / H / R; and / or(b) the amino acid substitution at amino acid residue 92 is X92 K / E / Q / R / H; and / or(c) the amino acid substitution at amino acid residue 94 is X94D / E / N / K / Q; and / or(d) the amino acid substitution at amino acid residue 96 is X96E / D / K / Q.

6. The variant polypeptide of any one of the preceding claims, wherein the variant polypeptide additionally comprises an amino acid substitution at amino acid residue 234 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , preferably wherein the amino acid substitution at amino acid residue 234 is X234Q / T.

7. The variant polypeptide of any one of the preceding claims, wherein the variant polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.

8. The variant polypeptide of claim 7, wherein:(a) the amino acid substitution at amino acid residue 103 is X103N / D; and / orBASF SE 240828W00180 B19118WO(b) the amino acid substitution at amino acid residue 107 is X107E; and / or(c) the amino acid substitution at amino acid residue 201 is X201 L; and / or(d) the amino acid substitution at amino acid residue 205 is X205N; and / or(e) the amino acid substitution at amino acid residue 225 is X225Y; and / or(f) the amino acid substitution at amino acid residue 251 is X251 L; and / or(g) the amino acid substitution at amino acid residue 256 is X256S; and / or(h) the amino acid substitution at amino acid residue 257 is X257T; and / or(i) the amino acid substitution at amino acid residue 258 is X258D; and / or(j) the amino acid substitution at amino acid residue 260 is X260A; and / or(k) the amino acid substitution at amino acid residue 269 is X269S; and / or(l) the amino acid substitution at amino acid residue 271 is X271 N; and / or(m) the amino acid substitution at amino acid residue 272 is X272S; and / or(n) the amino acid substitution at amino acid residue 275 is X275D; and / or(o) the amino acid substitution at amino acid residue 280 is X280V; and / or(p) the amino acid substitution at amino acid residue 282 is X282Y / F; and / or(q) the amino acid substitution at amino acid residue 284 is X284E; and / or(r) the amino acid substitution at amino acid residue 293 is X293L; and / or(s) the amino acid substitution at amino acid residue 295 is X295G; and / or(t) the amino acid substitution at amino acid residue 299 is X299S / L.

9. The variant polypeptide of any one of the preceding claims, wherein said variant polypeptide additionally comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 2, 5, 7, 29, 31 , 33, 41 , 44, 59, 66, 71 , 97, 99, 108, 110, 111 , 118, 134, 135, 138, 158, 160, 168, 175, 182, 243, 259 and 289 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 .

10. The variant polypeptide of claim 9, wherein:(a) the amino acid substitution at amino acid residue 2 is X2S; and / or(b) the amino acid substitution at amino acid residue 5 is X5H; and / or(c) the amino acid substitution at amino acid residue 7 is X7S; and / or(d) the amino acid substitution at amino acid residue 29 is X29T / A; and / or(e) the amino acid substitution at amino acid residue 31 is X31 Y; and / or(f) the amino acid substitution at amino acid residue 33 is X33S; and / or(g) the amino acid substitution at amino acid residue 41 is X41 G; and / or(h) the amino acid substitution at amino acid residue 44 is X44N; and / or(i) the amino acid substitution at amino acid residue 59 is X59V; and / or(j) the amino acid substitution at amino acid residue 66 is X66D; and / or(k) the amino acid substitution at amino acid residue 71 is X71V; and / or(l) the amino acid substitution at amino acid residue 97 is X97A; and / or(m) the amino acid substitution at amino acid residue 99 is X99M; and / orBASF SE 240828W00181 B19118WO(n) the amino acid substitution at amino acid residue 108 is X108L; and / or(o) the amino acid substitution at amino acid residue 110 is X110D; and / or(p) the amino acid substitution at amino acid residue 111 is X111 T; and / or(q) the amino acid substitution at amino acid residue 118 is X118K; and / or(r) the amino acid substitution at amino acid residue 134 is X134G; and / or(s) the amino acid substitution at amino acid residue 135 is X135G; and / or(t) the amino acid substitution at amino acid residue 138 is X138E; and / or(u) the amino acid substitution at amino acid residue 158 is X158I; and / or(v) the amino acid substitution at amino acid residue 160 is X160A; and / or(w) the amino acid substitution at amino acid residue 168 is X168K / Q; and / or(x) the amino acid substitution at amino acid residue 175 is X175Q; and / or(y) the amino acid substitution at amino acid residue 182 is X182T; and / or(z) the amino acid substitution at amino acid residue 243 is X243T; and / or(aa) the amino acid substitution at amino acid residue 259 is X259M; and / or(bb) the amino acid substitution at amino acid residue 289 is X289E.11 . The variant polypeptide of any one of the preceding claims, wherein the variant polypeptide has a length of 200 to 350 amino acids, preferably of 299 amino acids.

12. The variant polypeptide of any one of the preceding claims, wherein the variant polypeptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14.

13. The variant polypeptide of any one of the preceding claims, wherein the variant polypeptide exhibits one or more improved properties compared to the mannanase according to SEQ ID NO: 15, preferably wherein the improved properties are selected from:(i) increase in stability,(ii) increase in storage stability,(iii) increase in storage stability in an enzyme formulation, and(iv) increase in storage stability in a detergent composition.

14. A polynucleotide encoding the variant polypeptide of any one of the preceding claims.

15. A composition comprising the variant polypeptide of any one of claims 1 to 13 and at least one additional component, preferably wherein the composition comprises one or more additional enzymes different from the variant polypeptide referred to in any of claims 1 to 13, preferably one or more additional enzymes selected from the group consisting of protease, amylase, cellulase, oxidoreductase, transferase, hydrolase, lyase, isomerase, ligase, aminopeptidase, asparaginase, carbohydrase, carboxypeptidase, catalase, chitinase, cutinase, cyclodextrinBASF SE 240828W00182 B19118WO glycosyltransferase, deoxyribonuclease, endo-beta 1 ,3 glucanase, endo- beta 1 ,4 glucanase, xanthan endoglucanase, esterase, alpha-galactosidase, betagalactosidase, glucoamylase, alpha-glucosidase, beta-glucosidase, glycosyl hydrolase, hyaluronic acid synthase, invertase, laccase, lipase, mannosidase, mutanase, oxidase, a pectinolytic enzyme, peroxidase, phytase, polyphenoloxidase, pullulanase, ribonuclease, transglutaminase, dispersin, and xylanase, preferably protease, amylase or cellulase, most preferably protease.

16. A variant polypeptide having mannanase activity, wherein:(i) the variant polypeptide has an amino acid sequence which is at least 85% identical to an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13 and SEQ ID NO: 14; and(ii) the polypeptide comprises at least one amino acid substitution at an amino acid residue selected from the group consisting of 58 and 72 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , preferably comprises at least one amino acid substitution selected from the group consisting of X58G / A / P and X72L / MA / compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.

17. The variant polypeptide of claim 16, further comprising at least one amino acid substitution at an amino acid residue selected from the group consisting of 79, 92, 94, 96, and 100 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1 , preferably comprising at least one amino acid substitution selected from the group consisting of X79K / H / R, X92K / E / Q / R / H, X94D / E / N / K / Q, X96E / D / K / Q, and X100R / K / Q compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering of SEQ ID NO: 1.

18. The variant polypeptide of claim 16 or 17, further comprising at least one amino acid substitution at an amino acid residue selected from the group consisting of 103, 107, 201 , 205, 225, 234, 251 , 256, 257, 258, 260, 269, 271 , 272, 275, 280, 282, 284, 293, 295 and 299 compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1 , preferably comprising at least one amino acid substitution selected from the group consisting of X103N / D, X107E, X201 L, X205N, X225Y, X234Q / T, X251 L, X256S, X257T, X258D, X260A, X269S, X271 N, X272S, X275D, X280V, X282Y / F, X284E, X293L, X295G and X299S / L compared to the amino acid sequence as set forth in SEQ ID NO: 1 and referring to the numbering in SEQ ID NO: 1.