WO2024050339A1 - Variants de mannanases et procédés d'utilisation - Google Patents

Variants de mannanases et procédés d'utilisation Download PDF

Info

Publication number
WO2024050339A1
WO2024050339A1 PCT/US2023/073055 US2023073055W WO2024050339A1 WO 2024050339 A1 WO2024050339 A1 WO 2024050339A1 US 2023073055 W US2023073055 W US 2023073055W WO 2024050339 A1 WO2024050339 A1 WO 2024050339A1
Authority
WO
WIPO (PCT)
Prior art keywords
mannanase
variant
amino acid
cleaning
composition
Prior art date
Application number
PCT/US2023/073055
Other languages
English (en)
Inventor
Brandon J. BURKHART
Taya FELDMAN
Thomas P. Graycar
Brian James Paul
Jahnavi Chandra PRASAD
Yixin REN
Original Assignee
Danisco Us Inc.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Danisco Us Inc. filed Critical Danisco Us Inc.
Publication of WO2024050339A1 publication Critical patent/WO2024050339A1/fr

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01078—Mannan endo-1,4-beta-mannosidase (3.2.1.78), i.e. endo-beta-mannanase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2477—Hemicellulases not provided in a preceding group
    • C12N9/2488—Mannanases
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2477—Hemicellulases not provided in a preceding group
    • C12N9/2488—Mannanases
    • C12N9/2494—Mannan endo-1,4-beta-mannosidase (3.2.1.78), i.e. endo-beta-mannanase
    • C11D2111/12—
    • C11D2111/14—

Definitions

  • compositions containing the mannanases are suitable for use as detergents and for cleaning fabrics and hard surfaces, as well as in a variety of other industrial applications.
  • Mannanase enzymes including endo-P-mannanases, have been employed in detergent cleaning compositions for the removal of gum stains by hydrolyzing mannans.
  • a variety of mannans are found in nature, such as, for example, linear mannan, glucomannan, galactomannan, and glucogalactomannan.
  • Each such mannan is comprised of polysaccharides that contain a P-l,4-linked backbone of mannose residues that may be substituted up to 33% with glucose residues (Yeoman et al., Adv Appl Microbiol, 70: 1, 2010, Elsevier).
  • galactomannans or glucogalactomannnans galactose residues are linked in alpha- 1,6-linkages to the mannan backbone (Moreira and Filho, Appl Microbiol Biotechnol, 79: 165, 2008).
  • hydrolysis of mannan to its component sugars requires endo-l,4-P-mannanases that hydrolyze the backbone linkages to generate short chain manno-oligosaccharides that are further degraded to monosaccharides by 1,4-P-mannosidases.
  • mannanases such as, for example, endo-P-mannanases have been known in the art of industrial enzymes, there remains a need for improved mannanase variants.
  • Variants, compositions and methods disclosed herein relate to a recombinant mannanase, or a recombinant polypeptide generated through conventional molecular biology techniques (see, e.g., Sambrook et al, Molecular Cloning: Cold Spring Harbor Laboratory Press).
  • mannanase variants are provided, where the mannanase variants comprise one or more amino acid substitutions at one or more positions selected from 32, 72, 161 and 172 wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • the mannanase variant is a variant comprising an amino acid substitution selected from the group consisting of 19D, 32Y, 34D, 72V, 93Q, 13 IS, 136P, 139R, 161G, 172F, 225N/Q, 259D, 261DZE and 276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • the mannanase variant is a variant comprising two or more amino acid substitutions selected from the group consisting of 19D, 32Y, 72V, 93Q, 13 IS, 136P, 139R, 161G, 168T, 172F, 225N/Q, 259DZE, 261DZE and 276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • the mannanase variant is a variant comprising amino acid substitutions selected from the group consisting of 19D-276W, 32Y-259D, 93Q-276W, 131S- 276W, 136P-276W, 139R-276W, 161G-276W, 225N/Q-276W, 259D/E-276W, and 261D/E- 276W.
  • the mannanase variant is a variant comprising amino acid substitutions selected from the group consisting of 19D-131S-276W, 32Y-261D-276W, 32Y- 259D-276W, 32Y-172F-259D, 168T-259D-276W, 259D-261E-276W, and 259Q-261E-276W.
  • the mannanase variant is a variant comprising amino acid substitutions selected from the group consisting of Y061W-G259D-R261E-F276W, Y061W- T062E-G259D-R261E-F276W, Y061W-V228T-G259D-R261E-F276W, V228T-G259D- R261E-F276W, F032Y-G259D-R261E-F276W, F032Y-Y061W-Y167F-P168S-G259D-R261E- F276W, F032Y-Y061W-G259D-R261E-F276W, F032Y-Y061W-T062E-G259D-R261E- F276W, F032Y-T062E-R261D-F276W, F032Y-T062
  • N010T-F032Y-V059S-Q060L-T062E-Y167F-P168S-V228T-G259D-F276W-T284E N010T-F032Y-V059S-Q060L-T062E-I072V-V228T-G259D-F276W-T284E
  • the mannanase variant is a mannanase variant described herein, wherein the variant comprises an amino acid sequence having at least 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the amino acid sequence of SEQ ID NO: 1.
  • the mannanase variant is a mannanase variant described herein, wherein said variant is derived from a parent or reference polypeptide with 60%, 65%, 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% amino acid sequence identity to SEQ ID NO: 1.
  • the mannanase variant is a mannanase variant described herein, wherein said variant has improved stability when compared to a parent or reference mannanase.
  • the mannanase variant is a mannanase variant described herein, wherein said variant has equal or improved cleaning performance in a detergent when compared to a parent or reference mannanase.
  • the mannanase variant is a mannanase variant described herein, wherein the mannanase variant has mannanase activity.
  • polynucleotide compositions comprising a nucleic acid sequence encoding one or more mannanase variants described herein, wherein said polynucleotide is, optionally, isolated.
  • the enzyme compositions comprising one or more mannanase variant described herein.
  • the enzyme compositions is an enzyme granule.
  • the enzyme composition further comprises one or more other enzymes selected from acyl transferases, amylases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinases, arabinosidases, aryl esterases, beta-galactosidases, beta-glucanases, carrageenases, catalases, cellulases, chondroitinases, cutinases, dispersins, endo-glucanases, endo-beta-mannanases, exo- beta-mannanases, esterases, exo-mannanases, galactanases, glucoamylases, hemicellulases, hexosaminidase ⁇ hyaluronidases, ker
  • cleaning compositions comprising one or more mannanase variant described herein.
  • the cleaning composition is a detergent composition selected from the group consisting of a laundry detergent, a fabric softening detergent, a dishwashing detergent, a medical instrument cleaning detergent, and a hard-surface cleaning detergent.
  • the disclosure also provides methods of cleaning.
  • the method is a method of cleaning comprising, contacting a surface or an item in need of cleaning with an effective amount of a mannanase variant described herein or the enzyme composition described herein; and optionally further comprising the step of rinsing said surface or item after contacting said surface or item with said variant or enzyme composition.
  • the item is dishware or fabric.
  • the mannanase variant has cleaning activity in a detergent composition. In some embodiments, the mannanase variant has mannanase activity in the presence of a protease. In some embodiments, the mannanase variant retains at least 50% mannanase activity in the presence of a protease. In some embodiments, the mannanase variant is capable of hydrolyzing a substrate selected from the group consisting of guar gum, locust bean gum, and combinations thereof. In some embodiments, the mannanase variant does not further comprise a carbohydrate-binding module.
  • the method is a method of cleaning comprising, contacting a surface or an item in need of cleaning with an effective amount of a mannanase described herein or the enzyme composition comprising a mannanase variant described herein; and optionally further comprising the step of rinsing said surface or item after contacting said surface or item with said variant or enzyme composition.
  • Yet further embodiments are directed to a method of cleaning comprising contacting a surface or item comprising a soil or stain comprising mannan with a (i) mannanase variant or recombinant polypeptide, or (ii) a cleaning composition described herein, wherein the mannan contained is said soil or stain is hydrolyzed.
  • Some embodiments are further directed to nucleic acids or isolated nucleic acids encoding the mannanase variants or recombinant polypeptides described herein. Further embodiments are directed to an expression vector comprising a nucleic acid or isolated nucleic acid described herein operably linked to a regulatory sequence. Even further embodiments are directed to a host cell comprising an expression vector described herein, or nucleic acids encoding the mannanase variants or recombinant polypeptides described herein. In some embodiments, the host cell is a bacterial cell or a fungal cell.
  • Still further embodiments are directed to methods of producing a mannanase variant described herein comprising: stably transforming a host cell with an expression vector comprising a polynucleotide encoding the mannanase variant; culturing the transformed host cell under suitable conditions to produce the mannanase variant; and recovering the mannanase variant.
  • the present disclosure provides one or more mannanase variant comprising one or more amino acid substitutions as described in more detail below.
  • the variants provided herein demonstrate one or more improved properties, such as an improved stability when compared to a reference mannanase having the amino acid sequence of SEQ ID NO: 1 or 2.
  • the mannanase variants provided herein find use in the preparation of cleaning compositions (e.g. automatic dishwashing compositions).
  • the mannanase variants provided herein also find use in methods of cleaning (e.g. dish washing methods) using such variants or compositions comprising such mannanase variants.
  • one or more mannanase variant described herein can be made and used by a variety of techniques used in molecular biology, microbiology, protein purification, protein engineering, protein and DNA sequencing, recombinant DNA fields, and industrial enzyme use and development.
  • the one or more mannanase variant described herein have glycosyl hydrolase activity and/or are stable in the presence of a protease. These features of the mannanase variants described herein make them well suited for use in a variety of cleaning and other industrial applications, for example, where the enzyme can hydrolyze mannans in the presence of surfactant, protease, and/or other components found in a detergent composition.
  • nucleic acid sequences are written left to right in 5' to 3' orientation; and amino acid sequences are written left to right in amino to carboxy orientation.
  • Each numerical range used herein includes every narrower numerical range that falls within such broader numerical range, as if such narrower numerical ranges were all expressly written herein.
  • the nomenclature of the amino acid substitutions of the one or more mannanase variants described herein uses one or more of the following: position; positiomamino acid substitution(s); or starting amino acid(s):position:amino acid substitution(s).
  • Reference to a “position” e.g. 5, 8, 17, 22, etc) encompasses any starting amino acid that may be present at such position, and any substitution that may be present at such position.
  • Reference to a “position: amino acid substitution(s)” e.g. 1S/T/G, 3G, 17T, etc) encompasses any starting amino acid that may be present at such position and the one or more amino acid(s) with which such starting amino acid may be substituted.
  • Reference to a position can be recited in several forms, for example, position 003 can also be referred to as position 03 or 3.
  • Reference to a starting or substituted amino acid may be further expressed as several starting, or substituted amino acids separated by a foreslash (“/”).
  • D275S/K indicates position 275 is substituted with serine (S) or lysine (K)
  • P/S197K indicates that starting amino acid proline (P) or serine (S) at position 197 is substituted with lysine (K).
  • Reference to an X as the amino acid in a position refers to any amino acid at the recited position.
  • the position of an amino acid residue in a given amino acid sequence is numbered by correspondence with the amino acid sequence of SEQ ID NO: 1. That is, the amino acid sequence of SEQ ID NO: 1 serves as a reference sequence for numbering of positions of an amino acid residue.
  • the amino acid sequence of one or more mannanase variant described herein is aligned with the amino acid sequence of SEQ ID NO: 1 using an alignment algorithm as described herein, and each amino acid residue in the given amino acid sequence that aligns (preferably optimally aligns) with an amino acid residue in SEQ ID NO: 1 is conveniently numbered by reference to the numerical position of that corresponding amino acid residue.
  • Sequence alignment algorithms such as, for example, described herein will identify the location or locations where insertions or deletions occur in a subject sequence when compared to a query sequence (also sometimes referred to as a “reference sequence”).
  • mannan endo-l,4-P-mannosidase refers to an enzyme capable of the random hydrolysis of 1,4-P-D-mannosidic linkages in mannans, galactomannans and glucomannans.
  • Endo-l,4-P-mannanases are members of several families of glycosyl hydrolases, including GH26 and GH5.
  • endo-P-mannanases constitute a group of poly saccharases that degrade mannans and denote enzymes that are capable of cleaving polyose chains containing mannose units ( . e. , are capable of cleaving glycosidic bonds in mannans, glucomannans, galactomannans and galactogluco-mannans).
  • endo-P- mannanases may possess additional enzymatic activities (e.g., endo-l,4-P- glucanase, 1,4- p -mannosidase, and cellodextrinase activities).
  • mannanase refers to an enzyme, polypeptide, or protein that can degrade mannan.
  • the mannanase enzyme may, for example, be an endo-P- mannanase, an exo-P-mannanase, or a glycosyl hydrolase.
  • mannanase activity may be determined according to any procedure known in the art (See, e.g., Lever, Anal. Biochem, 47:273, 1972; Eriksson and Winell, Acta Chem. Scand., (1968), 22: 1924; US 6,602,842; and WO 95/35362A1).
  • mannans are polysaccharides having a backbone composed of P-1, 4- linked mannose
  • glucomannans are polysaccharides having a backbone of more or less regularly alternating P-1,4 linked mannose and glucose
  • galactomannans and galactoglucomannans are mannans and glucomannans with alpha- 1,6 linked galactose side- branches. These compounds may be acetylated. The degradation of galactomannans and galactoglucomannans is facilitated by full or partial removal of the galactose side-branches.
  • acetylated mannans, glucomannans, galactomannans and galactoglucomannans is facilitated by full or partial deacetylation.
  • Acetyl groups can be removed by alkali or by mannan acetylesterases.
  • the oligomers that are released from the mannanases or by a combination of mannanases and alpha-galactosidase and/or mannan acetyl esterases can be further degraded to release free maltose by P-mannosidase and/or P-glucosidase.
  • protease refers to an enzyme that has the ability to break down proteins and peptides.
  • a protease has the ability to conduct “proteolysis,” by hydrolysis of peptide bonds that link amino acids together in a peptide or polypeptide chain forming the protein.
  • proteolytic activity This activity of a protease as a protein-digesting enzyme is referred to as “proteolytic activity.”
  • proteolytic activity may be ascertained by comparative assays that analyze the respective protease’s ability to hydrolyze a suitable substrate.
  • Exemplary substrates useful in the analysis of protease or proteolytic activity include, but are not limited to, di-methyl casein (Sigma C- 9801), bovine collagen (Sigma C-9879), bovine elastin (Sigma E-1625), and Keratin Azure (Sigma-Aldrich K8500). Colorimetric assays utilizing these substrates are well known in the art (See e.g, WO99/34011 and US 6,376,450).
  • modification refers to any change or alteration in an amino acid sequence, including the substitution of an amino acid at the identified position of the amino acid sequence of interest with an amino acid that is different from the starting amino acid, deletion of an amino acid at the identified position of the amino acid sequence of interest, insertion of an amino acid at the identified position of the amino acid sequence of interest, replacement of an amino acid side chain in the amino acid sequence of interest, and or chemical modification of the amino acid sequence of interest.
  • catalytic activity or “activity” describes quantitatively the conversion of a given substrate under defined reaction conditions.
  • residual activity is defined as the ratio of the catalytic activity of the enzyme under a certain set of conditions to the catalytic activity under a different set of conditions.
  • specific activity describes quantitatively the catalytic activity per amount of enzyme under defined reaction conditions.
  • pH-stability describes the ability of a protein to withstand a limited exposure to pH-values significantly deviating from the pH where its stability is optimal (e.g., more than one pH-unit above or below the pH-optimum), without losing its activity under conditions where its activity is measurable.
  • detergent stability refers to the stability of a specified detergent composition component (such as a hydrolytic enzyme) in a detergent composition mixture.
  • perhydrolase refers to an enzyme capable of catalyzing a reaction that results in the formation of a peracid suitable for applications such as cleaning, bleaching, and disinfecting.
  • aqueous refers to a composition that is made up of at least 50% water.
  • An aqueous composition may contain at least 50%, 60%, 70%, 80%, 90%, 95%, 97%, 98%, or 99% water.
  • surfactant refers to any compound generally recognized in the art as having surface active qualities. Surfactants generally include anionic, cationic, nonionic, and zwitterionic compounds, which are further described, herein.
  • chelator stability refers to mannanase variants of the present disclosure that retain a specified amount of enzymatic activity over a given period of time under conditions prevailing during the mannosidic, hydrolyzing, cleaning, or other process disclosed herein, for example while exposed to or contacted with chelating agents.
  • the mannanase variant retains at least about 50%, about 60%, about 70%, about 75%, about 80%, about 85%, about 90%, about 92%, about 95%, about 96%, about 97%, about 98%, or about 99% mannanase activity after contact with a chelating agent over a given time period, for example, at least about 10 minutes, about 20 minutes, about 40 minutes, about 60 minutes, about 100 minutes, etc.
  • thermo stability and “thermostable” refer to mannanase variants that retain a specified amount of enzymatic activity after exposure to elevated temperatures over a given period of time under conditions prevailing during the mannosidic, hydrolyzing, cleaning, or other process, for example, while exposed to elevated temperatures.
  • the mannanase retains at least about 50%, about 60%, about 70%, about 75%, about 80%, about 85%, about 90%, about 92%, about 95%, about 96%, about 97%, about 98%, or about 99% mannanase activity after exposure to elevated temperatures, for example, at least about 50°C, about 55°C, about 60°C, about 65°C, or about 70°C, over a given time period, for example, at least about 5 minutes, 10 minutes, 15 minutes, 20 minutes, 30 minutes, 40 minutes, 50 minutes, 60 minutes, 120 minutes, 180 minutes, 240 minutes, 300 minutes, etc.
  • cleaning activity refers to the cleaning performance achieved by a mannanase variant under conditions prevailing during the mannosidic, hydrolyzing, cleaning, or other process disclosed herein.
  • cleaning performance is determined by the application of various cleaning assays concerning enzyme sensitive stains arising from food products, household agents or personal care products.
  • Some of these stains include, for example, ice cream, ketchup, BBQ sauce, mayonnaise, soups, chocolate milk, chocolate pudding, frozen desserts, shampoo, body lotion, sun protection products, toothpaste, locust bean gum, or guar gum as determined by various chromatographic, spectrophotometric or other quantitative methodologies after subjection of the stains to standard wash conditions.
  • Exemplary assays include, but are not limited to those described in WO99/34011, US 6,605,458, and US 6,566,114, as well as those methods described in the Examples.
  • clean surface and “clean textile” refer to a surface or textile respectively that has a percent stain removal of at least 10%, preferably at least 15%, 20%, 25%, 30%, 35%, or 40% of a soiled surface or textile.
  • the term “effective amount” when used in conjunction with a mannanase variant refers to the quantity of mannanase variant needed to achieve the desired level of enzymatic activity in the specified cleaning composition. Such effective amounts are readily ascertained by one of ordinary skill in the art and are based on many factors, such as the particular mannanase variant that is used, the cleaning application, the specific composition of the cleaning composition, and whether a liquid or dry (e.g., granular, bar, powder, solid, liquid, tablet, gel, paste, foam, sheet, or unit dose) composition is required.
  • a liquid or dry composition e.g., granular, bar, powder, solid, liquid, tablet, gel, paste, foam, sheet, or unit dose
  • adjunct ingredient when used in conjunction with a cleaning composition means any liquid, solid or gaseous material selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, granule, powder, bar, paste, spray, tablet, gel, unit dose, sheet, or foam composition), which materials are also preferably compatible with the mannanase variant used in the composition.
  • granular compositions are in “compact” form, while in other embodiments, the liquid compositions are in a “concentrated” form.
  • cleaning compositions and “cleaning formulations” refer to admixtures of chemical ingredients that find use in the removal of undesired compounds (e.g., soil or stains) from items or surfaces to be cleaned, such as, for example, fabric, dishes, contact lenses, solid surfaces, hair, skin, and teeth.
  • the compositions or formulations may be in the form of a liquid, gel, granule, powder, bar, paste, spray tablet, gel, unit dose, sheet, or foam, depending on the surface or item to be cleaned and the desired form of the composition or formulation.
  • Detergent composition and “detergent formulation” refer to mixtures of chemical and/or biological ingredients intended for use in a wash medium for the cleaning of soiled objects.
  • Detergent compositions/formulations generally include at least one surfactant, and may optionally include hydrolytic enzymes, oxido-reductases, builders, bleaching agents, bleach activators, bluing agents, fluorescent dyes, caking inhibitors, masking agents, enzyme activators, antioxidants, solubilizers, and one or more microorganisms or microbes or microbial extracts.
  • Microorganisms may be used as the only biologically active ingredient, but they may also be used in conjunction with one or more of the enzymes described herein.
  • a bacillus strain having the deposit accession number PTA-7543 may be used to reduce malodor as described in WO 2012/112718.
  • Other purposes could include in-situ production of desirable biological compounds, or inoculation/population of a locus with the microorganism(s) to competitively prevent other non-desirable microorganisms form populating the same locus (competitive exclusion).
  • the term “dishwashing composition” refers to all forms of compositions including, for example, granular, unit-dose, and liquid forms for cleaning dishware and cutlery.
  • the dishwashing composition is an “automatic dishwashing” composition that finds use in automatic dishwashing machines.
  • the term “dishware” refers to dishes e.g., plates, cups, glasses, bowls, and containers) and cutlery (e.g., utensils including, but not limited to spoons, knives, and forks) of any material, including but not limited to ceramics, plastics, metals, china, glass, and acrylics.
  • bleaching refers to the treatment of a material (e.g., fabric, laundry, pulp, etc.) or surface for a sufficient length of time and under appropriate pH and temperature conditions to effect a brightening (i.e., whitening) and/or cleaning of the material.
  • chemicals suitable for bleaching include but are not limited to CIO2, H2O2, peracids, and NO2.
  • wash performance of a mannanase variant refers to the contribution of the variant to washing that provides additional cleaning performance to the detergent composition. Wash performance is compared under relevant washing conditions.
  • relevant washing conditions is used herein to indicate the conditions, particularly washing temperature, time, washing mechanics, suds concentration, type of detergent, and water hardness, actually used in households in a dish or laundry detergent market segment.
  • the term “disinfecting” refers to the removal of contaminants from the surfaces, as well as the inhibition or killing of microbes on the surfaces of items.
  • the “compact” form of the cleaning compositions herein is best reflected by density and, in terms of composition, by the amount of inorganic filler salt.
  • Inorganic filler salts are conventional ingredients of detergent compositions in powder form. In conventional detergent compositions, the filler salts are present in substantial amounts, typically about 17 to about 35% by weight of the total composition. In contrast, in compact compositions, the filler salt is present in amounts not exceeding about 15% of the total composition. In some embodiments, the filler salt is present in amounts that do not exceed about 10%, or more preferably, about 5%, by weight of the composition.
  • the inorganic filler salts are selected from the alkali and alkaline-earth-metal salts of sulfates and chlorides. In some embodiments, a preferred filler salt is sodium sulfate.
  • fabric refers to, for example, woven, knit, and non-woven material, as well as staple fibers and filaments that can be converted to, for example, yams and woven, knit, and non-woven fabrics.
  • the term encompasses material made from natural, as well as synthetic (e.g., manufactured) fibers.
  • a nucleic acid or polynucleotide is “isolated” when it is at least partially or completely separated from other components, including but not limited to, for example, other proteins, nucleic acids, and cells.
  • a polypeptide, protein or peptide is “isolated” when it is at least partially or completely separated from other components, including but not limited to, for example, other proteins, nucleic acids, and cells.
  • an isolated species is more abundant than are other species in a composition.
  • an isolated species may comprise at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% (on a molar basis) of all macromolecular species present.
  • the species of interest is purified to essential homogeneity (i.e., contaminant species cannot be detected in the composition by conventional detection methods).
  • Purity and homogeneity can be determined using a number of techniques well known in the art, such as agarose or polyacrylamide gel electrophoresis of a nucleic acid or a protein sample, respectively, followed by visualization upon staining.
  • a high-resolution technique such as high performance liquid chromatography (HPLC) or a similar means can be utilized for purification of the material.
  • nucleic acids or polypeptides generally denotes a nucleic acid or polypeptide that is essentially free from other components as determined by analytical techniques well known in the art (e.g., a purified polypeptide or polynucleotide forms a discrete band in an electrophoretic gel, chromatographic eluate, and/or a media subjected to density gradient centrifugation).
  • a nucleic acid or polypeptide that gives rise to essentially one band in an electrophoretic gel is “purified.”
  • a purified nucleic acid or polypeptide is at least about 50% pure, usually at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8% or more pure (e.g., percent by weight on a molar basis).
  • a composition is enriched for a molecule when there is a substantial increase in the concentration of the molecule after application of a purification or enrichment technique.
  • the term “enriched” refers to a compound, polypeptide, cell, nucleic acid, amino acid, or other specified material or component that is present in a composition at a relative or absolute concentration that is higher than in a starting composition.
  • polypeptide refers to a molecule comprising a plurality of amino acids linked through peptide bonds.
  • polypeptide refers to a molecule comprising a plurality of amino acids linked through peptide bonds.
  • the terms “polypeptide,” “peptide,” and “protein” are used interchangeably. Proteins may optionally be modified (e.g., glycosylated, phosphorylated, acylated, farnesylated, prenylated, and sulfonated) to add functionality. Where such amino acid sequences exhibit activity, they may be referred to as an “enzyme”.
  • the conventional one-letter or three-letter codes for amino acid residues are used, with amino acid sequences being presented in the standard amino-to-carboxy terminal orientation (z.e., N— >C).
  • polynucleotide encompasses DNA, RNA, heteroduplexes, and synthetic molecules capable of encoding a polypeptide. Nucleic acids may be single-stranded or doublestranded, and may have chemical modifications. The terms “nucleic acid” and “polynucleotide” are used interchangeably. Because the genetic code is degenerate, more than one codon may be used to encode a particular amino acid, and the present compositions and methods encompass nucleotide sequences which encode a particular amino acid sequence. Unless otherwise indicated, nucleic acid sequences are presented in a 5'-to-3' orientation.
  • wild-type and “native” refer to polypeptides or polynucleotides that are found in nature.
  • wild-type and parental refer to a naturally- occurring polypeptide that does not include a man-made substitution, insertion, or deletion at one or more amino acid positions.
  • wild-type and parental refer to a naturally-occurring polynucleotide that does not include a manmade substitution, insertion, or deletion at one or more nucleosides.
  • a polynucleotide encoding a wild-type or parental polypeptide is not limited to a naturally- occurring polynucleotide, and encompasses any polynucleotide encoding the wild-type or parental polypeptide.
  • the term “reference”, with respect to a polypeptide, refers to a naturally-occurring polypeptide that does not include a man-made substitution, insertion, or deletion at one or more amino acid positions, as well as a polypeptide that includes one or more man-made substitutions, insertions, or deletions at one or more amino acid positions.
  • the term “reference”, with respect to a polynucleotide refers to a naturally-occurring polynucleotide that does not include a man-made substitution, insertion, or deletion of one or more nucleosides, as well as a polynucleotide that includes one or more man-made substitutions, insertions, or deletions at one or more nucleosides.
  • a polynucleotide encoding a wild-type or parental polypeptide is not limited to a naturally-occurring polynucleotide, and encompasses any polynucleotide encoding the wild-type or parental polypeptide.
  • the one letter code “Z” identifies an insertion or deletion in a parent or reference amino acid sequence.
  • the one letter code “Z” is on the left side of the position number and further includes a number (e.g., .01) before each amino acid being inserted therein to indicate the order of the insertions.
  • the insertion of one amino acid, glutamine (Q), at position 298 would be depicted as “Z298.01Q”; the insertion of one amino acid, X (where X can be any amino acid) at position 298 would be depicted as “Z298.01X”; and the insertion of three amino acids alanine (A), serine (S) and tyrosine (Y) between position 87 and 88 would be depicted as “Z87.01A/Z87.02S/Z87.03Y”.
  • the one letter code "Z" is on the right side of the position number.
  • the deletion of an alanine (A) from position 100 would be depicted as A100Z.
  • a combination of some of the above insertions and deletions would be depicted as: “G87S/Z87.01A/Z87.02S/Z87.03Y/A100Z”.
  • mannanase variant refers to a polypeptide that is derived from a reference polypeptide by the substitution, addition, or deletion, of one or more amino acids, typically by recombinant DNA techniques.
  • a mannanase variant may differ from a reference polypeptide by a small number of amino acid residues and may be defined by the level of primary amino acid sequence homology/identity with the reference polypeptide over the length of the catalytic domain.
  • a mannanase variant has at least 59%, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% amino acid sequence identity with a reference polypeptide.
  • the reference polypeptide includes, but is not limited to, naturally occurring and recombinant mannanases, such as but not limiting to mannanases within the GH5 8 sub family of mannanases (endo-1,4 P-mannosidases, EC 3.2.1.78).
  • exemplary reference GH5 8 bacterial mannanases include, for example, NDL-Clade mannanases, such as, for example, PspMan4 (SEQ ID NO: 1), PspManl38 (SEQ ID NO:2) and PspMan9 (SEQ ID NO:3); and other mannanases such as, for example, SEQ ID NOs:4-6
  • PspMan4 SEQ ID NO: 1
  • PspManl38 SEQ ID NO:2
  • PspMan9 SEQ ID NO:3
  • other mannanases such as, for example, SEQ ID NOs:4-6
  • variant polynucleotide refers to a polynucleotide that encodes a mannanase variant, has a specified degree of homology/identity with a parent polynucleotide, or hybridizes under stringent conditions to a parent polynucleotide or the complement thereof.
  • a variant polynucleotide has at least 59%, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% nucleotide sequence identity with a parent polynucleotide.
  • Sequence identity may be determined from protein sequence alignments using known programs such as BLAST, ALIGN, and CLUSTAL using standard parameters.
  • BLAST Altschul et al. [1990] J. Mol. Biol. 215:403-410; Henikoff et al. [1989] Proc. Natl. Acad. Sci. USA 89: 10915; Karin et al. [1993] Proc. Natl. Acad. Sci. USA 90:5873; and Higgins et al. [1988] Gene 73:237-244).
  • Software for performing BLAST analyses is publicly available through the National Center for Biotechnology Information (NCBI).
  • polypeptides may also be searched using FASTA (Pearson et al. [1988] Proc. Natl. Acad. Sci. USA 85:2444-2448).
  • FASTA Pearson et al. [1988] Proc. Natl. Acad. Sci. USA 85:2444-2448.
  • One indication that two polypeptides are substantially identical is that the first polypeptide is immunologically cross-reactive with the second polypeptide.
  • polypeptides that differ by conservative amino acid substitutions are immunologically cross-reactive.
  • a polypeptide is substantially identical to a second polypeptide, for example, where the two peptides differ only by a conservative substitution.
  • Another useful algorithm for alignment and comparison of multiple protein sequences is the MUSCLE program (Robert C. Edgar. MUSCLE: multiple sequence alignment with high accuracy and high throughput NucL Acids Res. (2004) 32 (5): 1792-1797) available from Geneious software (Biomatters Ltd.).
  • derived from encompasses the terms “originated from,” “obtained from,” “obtainable from,” “isolated from,” and “created from” and generally indicates that one specified material find its origin in another specified material or has features that can be described with reference to the another specified material.
  • hybridization refers to the process by which a strand of nucleic acid joins with a complementary strand through base pairing, as known in the art.
  • hybridization conditions refers to the conditions under which hybridization reactions are conducted. These conditions are typically classified by degree of “stringency” of the conditions under which hybridization is measured.
  • the degree of stringency can be based, for example, on the melting temperature (Tm) of the nucleic acid binding complex or probe.
  • Tm melting temperature
  • maximum stringency typically occurs at about T m -5°C (5°C below the Tm of the probe); “high stringency” at about 5-10°C below the T m ; “intermediate stringency” at about 10- 20°C below the Tm of the probe; and “low stringency” at about 20-25°C below the Tm.
  • maximum stringency conditions may be used to identify nucleic acid sequences having strict identity or near-strict identity with the hybridization probe; while high stringency conditions are used to identify nucleic acid sequences having about 80% or more sequence identity with the probe.
  • it is typically desirable to use relatively stringent conditions to form the hybrids e.g., relatively low salt and/or high temperature conditions are used).
  • substantially similar and “substantially identical” in the context of at least two nucleic acids or polypeptides means that a polynucleotide or polypeptide comprises either a sequence that has at least about 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity to a parent or reference sequence, or a sequence that includes amino acid substitutions, insertions, deletions, or modifications made only to circumvent the present description without adding functionality.
  • expression vector refers to a DNA construct containing a DNA sequence that encodes the specified polypeptide and is operably linked to a suitable control sequence capable of effecting the expression of the polypeptides in a suitable host.
  • control sequences include a promoter to effect transcription, an optional operator sequence to control such transcription, a sequence encoding suitable mRNA ribosome binding sites, and sequences which control termination of transcription and translation.
  • the vector may be a plasmid, a phage particle, or simply a potential genomic insert. Once transformed into a suitable host, the vector may replicate and function independently of the host genome, or may, in some instances, integrate into the genome itself.
  • the term “recombinant” refers to genetic material (z.e., nucleic acids, the polypeptides they encode, and vectors and cells comprising such polynucleotides) that has been modified to alter its sequence or expression characteristics, such as by mutating the coding sequence to produce an altered polypeptide, fusing the coding sequence to that of another gene, placing a gene under the control of a different promoter, expressing a gene in a heterologous organism, expressing a gene at a decreased or elevated levels, expressing a gene conditionally or constitutively in manner different from its natural expression profile, and the like.
  • signal sequence refers to a sequence of amino acids bound to the N-terminal portion of a polypeptide, and which facilitates the secretion of the mature form of the protein from the cell.
  • the mature form of the extracellular protein lacks the signal sequence which is cleaved off during the secretion process.
  • selectable marker refers to a gene capable of expression in a host cell that allows for ease of selection of those hosts containing an introduced nucleic acid or vector.
  • selectable markers include but are not limited to antimicrobial substances (e.g., hygromycin, bleomycin, or chloramphenicol) and/or genes that confer a metabolic advantage, such as a nutritional advantage, on the host cell.
  • selectable gene product refers to a gene that encodes an enzymatic activity that confers resistance to an antibiotic or drug upon the cell in which the selectable marker is expressed.
  • regulatory element refers to a genetic element that controls some aspect of the expression of nucleic acid sequences.
  • a promoter is a regulatory element which facilitates the initiation of transcription of an operably linked coding region. Additional regulatory elements include splicing signals, polyadenylation signals and termination signals.
  • host cells generally refers to prokaryotic or eukaryotic hosts which are transformed or transfected with vectors constructed using recombinant DNA techniques known in the art. Transformed host cells are capable of either replicating vectors encoding the protein variants or expressing the desired protein variant. In the case of vectors which encode the pre- or pro-form of the protein variant, such variants, when expressed, are typically secreted from the host cell into the host cell medium.
  • the term “introduced” in the context of inserting a nucleic acid sequence into a cell means transformation, transduction, or transfection.
  • Means of transformation include protoplast transformation, calcium chloride precipitation, electroporation, naked DNA, and the like as known in the art. (See, Chang and Cohen [1979] Mol. Gen. Genet. 168:111-115; Smith et al. [1986] Appl. Env. Microbiol. 51 :634; and the review article by Ferrari et al., in Harwood, Bacillus ⁇ Plenum Publishing Corporation, pp. 57-72, 1989).
  • variants, compositions and methods disclosed herein relate to a recombinant mannanase, comprising one or more modifications, wherein such variants are generated through conventional molecular biology techniques (see, e.g., Sambrook et al, Molecular Cloning: Cold Spring Harbor Laboratory Press).
  • the variant mannanase comprises one or more modifications selected from at least one substitution, at least one deletion, and at least one insertion.
  • the modification comprises a combination of mutations, such as, for example, a combination of at least one substitution and at least one deletion, at least one deletion and at least one insertion, at least one insertion and at least one substitution, or at least one substitution, at least one deletion, and at least one insertion.
  • mannanase variants are provided, where the mannanase variants comprise one or more amino acid substitutions at one or more positions selected from 32, 72, 161 and 172 wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • the mannanase variant is a mannanase variant comprising an amino acid substitution selected from the group consisting of 19D, 32Y, 34D, 72V, 93Q, 13 IS, 136P, 139R, 161G, 172F, 225N/Q, 259D, 261D/E and 276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • the mannanase variant is a mannanase variant comprising two or more amino acid substitutions selected from the group consisting of 19D, 32Y, 72V, 93Q, 13 IS, 136P, 139R, 161G, 168T, 172F, 225N/Q, 259D/E, 261D/E and 276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • the mannanase variant is a variant comprising amino acid substitutions selected from the group consisting of 19D-276W, 32Y-259D, 93Q-276W, 131S- 276W, 136P-276W, 139R-276W, 161G-276W, 225N/Q-276W, 259D/E-276W, and 261D/E- 276W
  • the mannanase variant is a variant comprising amino acid substitutions selected from the group consisting of 19D-131S-276W, 32Y-261D-276W, 32Y- 259D-276W, 32Y-172F-259D, 168T-259D-276W, 259D-261E-276W, and 259Q-261E-276W.
  • the mannanase variant is a mannanase variant comprising amino acid substitutions selected from the group consisting of Y061W-G259D-R261E-F276W, Y061W-T062E-G259D-R261E-F276W, Y061W-V228T-G259D-R261E-F276W, V228T- G259D-R261E-F276W, F032Y-G259D-R261E-F276W, F032Y-Y061W-Y167F-P168S- G259D-R261E-F276W, F032Y-Y061W-G259D-R261E-F276W, F032Y-Y061W-T062E- G259D-R261E-F276W, F032Y-T062E-R261D-
  • the mannanase variant is a mannanase variant described herein, wherein the variant comprises an amino acid sequence having at least 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the amino acid sequence of SEQ ID NO: 1.
  • the mannanase variant is a mannanase variant described herein, wherein said variant is derived from a parent or reference polypeptide with 60%, 65%, 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% amino acid sequence identity to SEQ ID NO: 1.
  • the mannanase variant is a mannanase variant described herein, wherein said variant has improved stability when compared to a parent or reference mannanase.
  • the mannanase variant is a mannanase variant described herein, wherein said variant has equal or improved cleaning performance in a detergent when compared to a parent or reference mannanase.
  • the mannanase variant is a mannanase variant described herein, wherein the mannanase variant has mannanase activity.
  • Another embodiment is directed to a mannanase variant comprising an amino acid sequence having at least 59%, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% amino acid sequence identity to the amino acid sequence of SEQ ID NO: 1-6.
  • the reference polypeptide is selected from SEQ ID NO: 1 or SEQ ID NO:2.
  • one or more mannanase variant described herein has at least 59%, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% amino acid sequence identity to the amino acid sequence of SEQ ID NO: 1, SEQ ID NO:2, SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, and/or SEQ ID NO:6.
  • the mannanase variants or recombinant polypeptides described herein are isolated.
  • the mannanase variants described herein are endo-P- mannanases.
  • the mannanase variants described herein have mannanase activity.
  • the mannanase variants described herein have mannanase activity in the presence of a surfactant.
  • the mannanase activity is activity on mannan gum, locust bean gum galactomannan, and/or konjac glucomannan.
  • the mannanase variants described herein have cleaning activity in a detergent composition. Still other embodiments are directed to mannanase variants or recombinant polypeptides that have mannanase activity in the presence of a protease. Further embodiments are directed to mannanase variants or recombinant polypeptides that hydrolyze a substrate selected from the group consisting of guar gum, locust bean gum, and combinations thereof. In some embodiments, the mannanase variants or recombinant polypeptides described herein do not comprise a carbohydrate-binding module.
  • the mannanase variant has enzymatic activity over a broad range of pH conditions. In certain embodiments, the mannanase variant has enzymatic activity from a pH of about 4.0 to about 11.0. In further embodiments, the mannanase variants or recombinant polypeptides have at least 50%, 60%, 70%, 80%, 90%, 95%, or 100% mannanase activity at a pH of from about 4.0 to about 11.0, about 4.5 to about 9.0, about 5.5 to about 8.5, or about 6.0 to about 7.5.
  • the mannanase variants or recombinant polypeptides have mannanase activity at a temperature ranging from about 20°C to about 90°C, about 30°C to about 80°C, about 20°C to about 50°C, or about 30°C to about 66°C.
  • the mannanase variants or recombinant polypeptides have at least 50%, 60%, 70%, 80%, 90%, 95%, or 100% mannanase activity at a temperature range from about 20°C to about 90°C, about 30°C to about 80°C, about 20°C to about 50°C, or about 30°C to about 66°C.
  • Yet still further embodiments are directed to mannanase variants or recombinant polypeptides described herein, wherein the variant retains at least 70% of its maximal mannanase activity at a pH range of 4.5-9.0, 5.5-8.5, or 6.0-7.5.
  • Some embodiments are directed to mannanase variants or recombinant polypeptides described herein, wherein the variant retains at least 70% of its maximal mannanase activity at a pH above 3.0, 3.5, 4.0 or 4.5 or at a pH below 9.0, 9.5, or 10.0.
  • one or more mannanase variant described herein has one or more improved property when compared to a reference polypeptide, wherein the improved property is selected from improved stability in the presence of protease, improved stability in detergent or buffer, improved cleaning performance, and improved aged cleaning performance.
  • Aged cleaning performance refers to the difference in stain removal measured for a sample of aged test sample (where the enzyme is pre-incubated in detergent for an extended period of time such as 3-4 weeks at an elevated temperature such as 37°C) compared to the ‘fresh’ stain cleaning for the same enzyme (no pre-incubation).
  • an enzyme with improved aged cleaning performance displays a smaller difference between the aged and freshly prepared samples when compared to the same evaluation carried out with a reference/parent enzyme.
  • one or more mannanase variant described herein has one or more improved property when compared to a reference polypeptide, wherein the improved property is selected from improved stability in the presence of protease, improved stability in detergent or buffer, improved cleaning performance, wherein the reference polypeptide is selected from SEQ ID NO: 1 or 2.
  • the mannanase variants or recombinant polypeptides are substantially identical to SEQ ID NO:1 or 2, meaning that they can contain amino acid substitutions, insertions, or deletions that do not significantly affect the structure, function, or expression of the variant or polypeptide .
  • Such mannanase variants or recombinant polypeptides include those designed only to circumvent the present description.
  • the mannanase variants have 1,4-P-D-mannosidic hydrolase activity, which includes mannanase, endo-l,4-P-D-mannanase, exo-l,4-P-D-mannanase galactomannanase, and/or glucomannanase activity.
  • 1,4-P-D-mannosidic hydrolase activity can be determined and measured using the assays described herein, or by other assays known in the art.
  • a polypeptide of the present invention has activity in the presence of a detergent composition.
  • the mannanase variants described herein are produced as an N- and/or C-terminal fusion protein, for example, to aid in extraction, detection and/or purification and/or to add functional properties to the variant or recombinant polypeptides or active fragments thereof.
  • fusion protein partners include, but are not limited to, glutathione-S-transferase (GST), 6XHis, GAL4 (DNA binding and/or transcriptional activation domains), FLAG, MYC, BCE103 (WO 2010/044786), or other tags well known to anyone skilled in the art.
  • a proteolytic cleavage site is provided between the fusion protein partner and the protein sequence of interest to allow removal of fusion protein sequences.
  • the fusion protein does not hinder the activity of the mannanase variants or recombinant polypeptides described herein.
  • the mannanase variants or recombinant polypeptides described herein are fused to a functional domain including a leader peptide, propeptide, one or more binding domain (modules) and/or a catalytic domain.
  • Suitable binding domains include, but are not limited to, carbohydrate-binding modules (CBM) of various specificities, providing increased affinity to carbohydrate components present during the application of the mannanase variants or recombinant polypeptides described herein.
  • CBM carbohydrate-binding modules
  • the CBM and catalytic domain of a polypeptide of the present invention are operably linked.
  • a CBM is defined as a contiguous amino acid sequence within a carbohydrateactive enzyme with a discreet fold having carbohydrate-binding activity.
  • CBMs in cellulosomal scaffold in proteins and rare instances of independent putative CBMs.
  • the requirement of CBMs existing as modules within larger enzymes sets this class of carbohydrate-binding proteins apart from other non-catalytic sugar binding proteins such as lectins and sugar transport proteins.
  • CBMs were previously classified as cellulose-binding domains (CBDs) based on the initial discovery of several modules that bound cellulose (Tomme et al., Eur J Biochem, 170:575-581, 1988; and Gilkes et al., J Biol Chem, 263: 10401-10407, 1988).
  • CBDs cellulose-binding domains
  • additional modules in carbohydrate-active enzymes are continually being found that bind carbohydrates other than cellulose, yet otherwise meet the CBM criteria, hence the need to reclassify these polypeptides using more inclusive terminology.
  • Previous classification of cellulose-binding domains was based on amino acid similarity. Groupings of CBDs were called "Types" and numbered with Roman numerals (e.g. Type I or Type II CBDs).
  • Families 1 to 13 are the same as Types I to XIII (Tomme et al., in Enzymatic Degradation of Insoluble Polysaccharides (Saddler, J.N. & Penner, M., eds.), Cellulose-binding domains: classification and properties, pp. 142-163, American Chemical Society, Washington, 1995).
  • a detailed review on the structure and binding modes of CBMs can be found in Boraston et al., Biochem J, 382:769-81, 2004.
  • CBMs The family classification of CBMs is expected to aid in the identification of CBMs, predict binding specificity, aid in identifying functional residues, reveal evolutionary relationships, and possibly be predictive of polypeptide folds. Because the fold of proteins is better conserved than their sequences, some of the CBM families can be grouped into superfamilies or clans. The current CBM families are 1- 63. CBDs are found at the N-and C-termini of proteins or are internal.
  • Enzyme hybrids are known in the art (See e.g., W090/00609 and WO95/16782) and may be prepared by transforming into a host cell a DNA construct comprising at least a fragment of DNA encoding the cellulose-binding domain ligated, with or without a linker, to a DNA sequence encoding a mannanase variant described herein and growing the host cell to express the fused gene.
  • Enzyme hybrids may be described by the following formula: CBM-MR-X or X-MR-CBM, wherein CBM is the N-terminal or the C-terminal region of an amino acid sequence corresponding to at least the carbohydrate-binding module; MR is the middle region (the linker), and may be a bond, or a short linking group of from about 2 to about 100 carbon atoms, from about 2 to about 40 carbon atoms, from about 2 to about 100 amino acids, or from about 2 to about 40 amino acids; and X is an N-terminal or C-terminal region of a mannanase variant described herein that has mannanase catalytic activity.
  • a mannanase may contain more than one CBM or other module(s)/domain(s) of non-glycolytic function.
  • module and “domain” are used interchangeably in the present disclosure.
  • catalytic domains include: cellulases; hemicellulases, such as xylanase; exo-mannanases; glucanases; arabinases; galactosidases; pectinases; and/or other activities such as proteases, lipases, acid phosphatases and/or others or functional fragments thereof.
  • Fusion proteins are optionally linked to a mannanase variant described herein through a linker sequence that simply joins the mannanase variant and the fusion domain without significantly affecting the properties of either component, or the linker optionally has a functional importance for the intended application.
  • the enzymes are mannanse variants as provided herein in combination with one or more additional enzymes selected from the group consisting of acyl transferases, amylases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinases, arabinosidases, aryl esterases, beta-galactosidases, beta-glucanases, carrageenases, catalases, cellulases, chondroitinases, cutinases, dispersins, DNAses (also known as nucleases or dispersins), endo-glucanases, endo-beta-mannanases, exo-beta-mannanases, esterases, exo- mannanases, galactanases, glucoamylases, hemicellulases, hexosaminidase i hyaluronidases, ker
  • a mannanase variant described herein is fused to a signal peptide for directing the extracellular secretion of the variant or polypeptide .
  • the signal peptide is the native signal peptide of the mannanase variant described herein.
  • the signal peptide is a non-native signal peptide such as the B. subtilis AprE signal peptide.
  • a polypeptide of the present invention is expressed in a heterologous organism, i.e., an organism other than Paenibacillus spp.
  • exemplary heterologous organisms are Gram(+) bacteria such as B. subtilis, B. Ucheniformis, B. lentus, B. brevis, Geobacillus (formerly Bacillus') stearothermophilus, B. alkalophilus, B. amyloliquefaciens, B. coagulans, B. circulans, B. lautus, B. megaterium, B. thuringiensis, S. lividans, or S. murinus,' Gram(-) bacteria such as E.
  • yeast such as Saccharomyces spp. or Schizosaccharomyces spp., e.g. S. cerevisiae and filamentous fungi such as Aspergillus spp., e.g., A. oryzae or A. niger, and T. reesei.
  • filamentous fungi such as Aspergillus spp., e.g., A. oryzae or A. niger, and T. reesei.
  • a mannanase variant described herein is expressed in a heterologous organism as a secreted polypeptide, in which case, the compositions and method encompass a method for expressing the variant as a secreted polypeptide in a heterologous organism.
  • Yet another embodiment is directed to a polynucleotide that encodes a mannanase variant described herein.
  • the polynucleotide is contained in an expression vector contained in a heterologous organism, such as those identified, herein.
  • the polynucleotide may be operably-linked to regulatory elements (e.g., a promoter, terminator, enhancer, and the like) to assist in expressing the encoded variants or recombinant polypeptides described herein.
  • Some embodiments are directed to a polynucleotide that encodes a mannanase variant having at least 59%, 60%, 65%, 70%, 75%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% amino acid sequence identity to the amino acid sequence of SEQ ID NO: 1-6.
  • the polynucleotide is codon-optimized for expression in a different host, mutated to introduce cloning sites, or otherwise altered to add functionality.
  • the polynucleotide that encodes a mannanase described herein is fused downstream of a coding sequence of a signal peptide that directs the extracellular secretion of variant .
  • Expression vectors may be provided in a heterologous host cell suitable for expressing a variant described herein, or suitable for propagating the expression vector prior to introducing it into a suitable host cell.
  • DNA that encodes a mannanase variant described herein can be chemically synthesized from published sequences or obtained directly from host cells harboring the gene (e.g., by cDNA library screening or PCR amplification).
  • a polynucleotide is included in an expression cassette and/or cloned into a suitable expression vector by standard molecular cloning techniques.
  • Such expression cassettes or vectors contain sequences that assist initiation and termination of transcription (e.g., promoters and terminators), and generally contain a selectable marker.
  • the expression cassette or vector is introduced into a suitable expression host cell, which then expresses the corresponding mannanase variant described herein.
  • suitable expression hosts are bacterial expression host genera including Escherichia (e.g., E. coli), Pseudomonas (e.g., P. fluorescens or P. stutzerei), Proteus (e.g., P. mirabilis), Ralstonia (e.g., R. eutropha), Streptomyces, Staphylococcus (e.g., S. carnosus), Lactococcus (e.g., L.
  • Escherichia e.g., E. coli
  • Pseudomonas e.g., P. fluorescens or P. stutzerei
  • Proteus e.g., P. mirabilis
  • Ralstonia e.g., R. eutropha
  • Streptomyces
  • yeast expression hosts such as S. cerevisiae, S. pombe, Y. lipolytica, H. polymorpha, K. lactis or P. pastoris.
  • fungal expression hosts such as C. lucknow ense, Aspergillus (e.g., A. oryzae, A. niger, A. nidulans, etc.) or T. reesei.
  • mammalian expression hosts such as mouse (e.g, NS0), Chinese Hamster Ovary (CHO) or Baby Hamster Kidney (BHK) cell lines.
  • eukaryotic hosts such as insect cells or viral expression systems (e.g, bacteriophages such as M13, T7 phage or Lambda, or viruses such as Baculovirus) are also suitable for producing a mannanase variant described herein.
  • Promoters and/or signal sequences associated with secreted proteins in a particular host of interest are candidates for use in the heterologous production and secretion of mannanases in that host or in other hosts.
  • the promoters that drive the genes for cellobiohydrolase I (cbhl), glucoamylase A (glaA), TAKA- amylase (amyA), xylanase (exlA), the gpd-promoter cbhl, cbhll, endoglucanase genes EGI- EGV, Cel61B, Cel74A, egll-egl5, gpd promoter, Pgkl, pkil, EF-lalpha, tefl, cDNAl and hexl are particularly suitable and can be derived from a number of different organisms (e.g., A.
  • the polynucleotide is recombinantly associated with a polynucleotide encoding a suitable homologous or heterologous signal sequence that leads to secretion of a mannanase variant described herein into the extracellular (or periplasmic) space, thereby allowing direct detection of enzyme activity in the cell supernatant (or periplasmic space or lysate).
  • a suitable homologous or heterologous signal sequence that leads to secretion of a mannanase variant described herein into the extracellular (or periplasmic) space, thereby allowing direct detection of enzyme activity in the cell supernatant (or periplasmic space or lysate).
  • Particularly suitable signal sequences for A are particularly suitable signal sequences for A.
  • coli other Gram negative bacteria and other organisms known in the art include those that drive expression of the HlyA, DsbA, Pbp, PhoA, PelB, OmpA, OmpT or M13 phage Gill genes.
  • particularly suitable signal sequences further include those that drive expression of AprE, NprB, Mpr, AmyA, AmyE, Blac, SacB, and for S. cerevisiae or other yeast, include the killer toxin, Bari, Suc2, Mating factor alpha, Inul A or Ggplp signal sequence.
  • Signal sequences can be cleaved by a number of signal peptidases, thus removing them from the rest of the expressed protein.
  • the rest of the polypeptide is expressed alone or as a fusion with other peptides, tags or proteins located at the N- or C-terminus (e.g., 6XHis, HA or FLAG tags).
  • Suitable fusions include tags, peptides or proteins that facilitate affinity purification or detection (e.g., BCE103, 6XHis, HA, chitin binding protein, thioredoxin or FLAG tags), as well as those that facilitate expression, secretion or processing of the target mannanase.
  • Suitable processing sites include enterokinase, STE13, Kex2 or other protease cleavage sites for cleavage in vivo or in vitro.
  • a mannanase variant described herein can be introduced into expression host cells by a number of transformation methods including, but not limited to, electroporation, lipid-assisted transformation or transfection (“lipofection”), chemically mediated transfection (c.g, CaCl and/or CaP), lithium acetate-mediated transformation (e.g., of host-cell protoplasts), biolistic “gene gun” transformation, PEG-mediated transformation (e.g., of host-cell protoplasts), protoplast fusion (e.g., using bacterial or eukaryotic protoplasts), liposome-mediated transformation, Agrobacterium lumefaciens, adenovirus or other viral or phage transformation or transduction.
  • lipofection lipid-assisted transformation or transfection
  • CaCl and/or CaP chemically mediated transfection
  • lithium acetate-mediated transformation e.g., of host-cell protoplasts
  • biolistic “gene gun” transformation e.g., PEG-mediated
  • a mannanase variant described herein can be expressed intracellularly.
  • a permeabilisation or lysis step can be used to release the polypeptide into the supernatant.
  • the disruption of the membrane barrier is effected by the use of mechanical means such as ultrasonic waves, pressure treatment (French press), cavitation or the use of membrane-digesting enzymes such as lysozyme or enzyme mixtures.
  • the polynucleotides encoding a mannanase variant described herein can be expressed by use of a suitable cell-free expression system.
  • RNA is exogenously added or generated without transcription and translated in cell free systems.
  • Another embodiment is directed to a cleaning composition comprising a mannanase variant and methods for using such compositions in cleaning applications.
  • Cleaning applications include, but are not limited to, laundry or textile cleaning, laundry or textile softening, dishwashing (manual and automatic), stain pre-treatment, and the like.
  • mannans e.g., locust bean gum, guar gum, etc.
  • mannans e.g., locust bean gum, guar gum, etc.
  • Cleaning compositions typically include an effective amount of a mannanase variant described herein, e.g., at least 0.0001 weight percent, from about 0.0001 to about 1, from about 0.001 to about 0.5, from about 0.01 to about 0.1 weight percent, or even from about 0.1 to about 1 weight percent, or more.
  • An effective amount of a mannanase variant in the cleaning composition results in the mannanase variant having enzymatic activity sufficient to hydrolyze a mannan-containing substrate, such as locust bean gum, guar gum, or combinations thereof.
  • Some embodiments are directed to a cleaning composition in a form selected from powder, liquid, granular, bar, solid, semi-solid, gel, paste, emulsion, tablet, capsule, unit dose, sheet, and foam.
  • the cleaning composition is a detergent composition.
  • the cleaning composition or detergent composition is selected from a laundry detergent, a fabric softening detergent, a dishwashing detergent, a medical instrument cleaning detergent, and a hard-surface cleaning detergent.
  • the cleaning compositions comprising one or more mannanase variant described herein is a detergent composition selected from the group consisting of a laundry detergent, a fabric softening detergent, a dishwashing detergent, a medical instrument cleaning detergent, and a hard-surface cleaning detergent.
  • the invention is directed to detergent compositions comprising at least two proteases in combination with one or more additional cleaning composition components such as, but not limiting to, a liquid laundry composition described in WO2022106404.
  • the one or more mannanase variant described herein can be part of, or added to, a liquid laundry detergent composition such as, but not limiting to, a liquid laundry composition described in US11046919B2, WO2021/223552, WO2022/167251, W02022/074037, WO2021/123184, WO2021/037895, WO2022/10372, W02020/264077, W02022/106404 and/or WO2017/54983; a compacted liquid laundry composition (US10683474B2); a water-soluble unit dose article comprising a fatty alkyl ester alkoxylate nonionic surfactant and an alkoxylated alcohol non-ionic surfactant (US20220162523A1); a liquid laundry detergent composition comprising improved alkylbenzenesulfonate surfactants (W02021/108307); a liquid laundry detergent composition comprising benzyl benzoate (WO2020/223959); and
  • the cleaning compositions comprising one or more mannanase variant described herein is a liquid laundry detergent composition containing alkyl ether carboxylic acids, betaines, anionic surfactant, non-ionic surfactant for providing softening benefits (WO2013/087286).
  • the cleaning compositions comprising one or more mannanase variant described herein is a liquid laundry detergent composition containing sulfite radical scavengers, protease stabilizers/inhibitors or combinations thereof (WO2022/157311) [00131]
  • the cleaning composition comprising one or more mannanase variant described herein is a liquid laundry detergent composition as described in US20210317387A1, WO2021/219296 , WO2021/127662, WO2021/041685, US11208619, US20220186144
  • the cleaning composition comprising one or more mannanase variant described herein is a liquid laundry detergent composition comprising dispersin variants, such as but limiting to a liquid laundry detergent composition described in US20210317387A1.
  • the cleaning composition comprising one or more mannanase variant described herein is a liquid laundry detergent composition is a highly alkaline textile washing agent, such as but limiting to a liquid laundry detergent composition described in WO202 1/219296
  • the cleaning composition comprising one or more mannanase variant described herein is a liquid laundry detergent composition is a low density unit dose detergent with encapsul ted fragrance, such as but limiting to a detergent composition described in WO2021/127662.
  • the cleaning composition comprising one or more mannanase variant described herein is a liquid laundry detergent composition containing polyethylene glycol and an organic acid, such as but limiting to, a detergent composition described in WO202 1/041685.
  • the cleaning composition comprising one or more mannanase variant described herein is a detergent composition containing polyethylene glycol and an organic acid, such as but limiting to, a detergent composition described in WO2021/041685.
  • the cleaning composition comprising one or more mannanase variant described herein is a detergent composition with effect on protein stains, such as but limiting to, a detergent composition described in US11208619.
  • the cleaning composition comprising one or more mannanase variant described herein is a detergent composition containing soil release polymers, such as but limiting to, a detergent composition described in US20220186144.
  • the cleaning compositions described herein further comprise a surfactant.
  • the surfactant is selected from a non-ionic, ampholytic, semi- polar, anionic, cationic, zwitterionic, and combinations and mixtures thereof.
  • the surfactant is selected from an anionic surfactant, a cationic surfactant, a zwitterionic surfactant, and combinations thereof.
  • the cleaning compositions described herein comprise from about 0.1% to about 60%, about 1% to about 50%, or about 5% to about 40% surfactant by weight of the composition.
  • Exemplary surfactants include, but are not limited to sodium dodecylbenzene sulfonate, Cl 2- 14 pareth-7, Cl 2- 15 pareth-7, sodium Cl 2- 15 pareth sulfate, Cl 4- 15 pareth-4, sodium laureth sulfate (e.g., Steol CS- 370), sodium hydrogenated cocoate, C12 ethoxylates (Alfonic 1012-6, Hetoxol LA7, Hetoxol LA4), sodium alkyl benzene sulfonates (e.g., Nacconol 90G), and combinations and mixtures thereof.
  • Anionic surfactants include but are not limited to linear alkylbenzenesulfonate (LAS), alpha-olefinsulfonate (AOS), alkyl sulfate (fatty alcohol sulfate) (AS), alcohol ethoxysulfate (AEOS or AES), secondary alkanesulfonates (SAS), alpha-sulfo fatty acid methyl esters, alkyl- or alkenylsuccinic acid, or soap.
  • LAS linear alkylbenzenesulfonate
  • AOS alpha-olefinsulfonate
  • AS alkyl sulfate
  • AEOS or AES alcohol ethoxysulfate
  • SAS secondary alkanesulfonates
  • alpha-sulfo fatty acid methyl esters alkyl- or alkenylsuccinic acid, or soap.
  • Nonionic surfactants include but are not limited to alcohol ethoxylate (AEO or AE), carboxylated alcohol ethoxylates, nonylphenol ethoxylate, alkylpolyglycoside, alkyldimethylamine oxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide (e.g., as described in WO92/06154), polyoxyethylene esters of fatty acids, polyoxyethylene sorbitan esters (e.g., TWEENs), polyoxyethylene alcohols, polyoxyethylene isoalcohols, polyoxyethylene ethers (e.g., TRITONs and BRIJ), polyoxyethylene esters, poly oxy ethyl ene- -tert-octyl phenols or octylphenyl-ethylene oxide condensates (e.g., NONIDET P40), ethylene oxide condensates with fatty alcohols (e
  • the detergent compositions disclosed herein further comprise a surfactant mixture that includes, but is not limited to 5-15% anionic surfactants, ⁇ 5% nonionic surfactants, cationic surfactants, phosphonates, soap, enzymes, perfume, butylphenyl methylpropionate, geraniol, zeolite, polycarboxylates, hexyl cinnamal, limonene, cationic surfactants, citronellol, and benzisothiazolinone.
  • a surfactant mixture that includes, but is not limited to 5-15% anionic surfactants, ⁇ 5% nonionic surfactants, cationic surfactants, phosphonates, soap, enzymes, perfume, butylphenyl methylpropionate, geraniol, zeolite, polycarboxylates, hexyl cinnamal, limonene, cationic surfactants, citronellol, and benzisothi
  • the cleaning compositions described herein may additionally include one or more detergent builders or builder systems, a complexing agent, a polymer, a bleaching system, a stabilizer, a foam booster, a suds suppressor, an anti-corrosion agent, a soil-suspending agent, an anti-soil redeposition agent, a dye, a bactericide, a hydrotope, a tarnish inhibitor, an optical brightener, a fabric conditioner, and a perfume.
  • the cleaning compositions described herein may also include additional enzymes selected from proteases, amylases, cellulases, lipases, pectin degrading enzymes, xyloglucanases, or additional carboxylic ester hydrolases.
  • the cleaning composition described herein further comprises from about 1%, from about 3% to about 60% or even from about 5% to about 40% builder by weight of the cleaning composition.
  • Builders may include, but are not limited to, the alkali metals, ammonium and alkanolammonium salts of polyphosphates, alkali metal silicates, alkaline earth and alkali metal carbonates, aluminosilicates, polycarboxylate compounds, ether hydroxypolycarboxylates, copolymers of maleic anhydride with ethylene or vinyl methyl ether, 1,3,5-trihydroxy benzene-2,4,6-trisulphonic acid, and carboxymethyloxysuccinic acid, the various alkali metals, ammonium and substituted ammonium salts of polyacetic acids such as ethylenediamine tetraacetic acid and nitrilotriacetic acid, as well as polycarboxylates such as mellitic acid, succinic acid
  • the builders form water-soluble hardness ion complexes (e.g., sequestering builders), such as citrates and polyphosphates (e.g., sodium tripolyphosphate and sodium tripolyphospate hexahydrate, potassium tripolyphosphate, and mixed sodium and potassium tripolyphosphate, etc.).
  • sequestering builders such as citrates and polyphosphates (e.g., sodium tripolyphosphate and sodium tripolyphospate hexahydrate, potassium tripolyphosphate, and mixed sodium and potassium tripolyphosphate, etc.).
  • Any suitable builder can find use in the compositions described herein, including those known in the art (See, e.g., EP 2100949).
  • the cleaning compositions described herein further comprise an adjunct ingredient including, but not limited to surfactants, builders, bleaches, bleach activators, bleach catalysts, other enzymes, enzyme stabilizing systems, chelants, optical brighteners, soil release polymers, dye transfer agents, dye transfer inhibiting agents, catalytic materials, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal agents, structure elasticizing agents, dispersants, suds suppressors, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric conditioners, hydrolyzable surfactants, solvents, preservatives, anti-oxidants, anti-shrinkage agents, anti-wrinkle agents, germicides, fungicides, color speckles, silvercare, anti-tarnish and/or anti-corrosion agents, alkalinity sources, solubilizing agents, carriers, processing aids, pigments, and
  • one or more adjunct is incorporated for example, to assist or enhance cleaning performance, for treatment of the substrate to be cleaned, or to modify the aesthetics of the cleaning composition as is the case with perfumes, colorants, dyes or the like.
  • Any such adjunct ingredient is in addition to the mannanase variant described herein.
  • the precise nature of these additional components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the cleaning operation for which it is to be used.
  • suitable methods can be employed to keep the cleaning adjunct ingredient and mannanases separated (i.e., not in contact with each other) until combination of the two components is appropriate.
  • Such separation methods include any suitable method known in the art (e.g., gelcaps, encapsulation, tablets, physical separation, etc.).
  • suitable adjunct ingredients is readily made by considering the surface, item, or fabric to be cleaned, and the desired form of the composition for the cleaning conditions during use (e.g., through the wash detergent use).
  • the cleaning compositions described herein are advantageously employed for example, in laundry applications, hard surface cleaning, dishwashing applications, as well as cosmetic applications.
  • the polypeptides of the present invention may find use in granular and liquid compositions.
  • a mannanase variant described herein may also find use in cleaning additive products.
  • the additive is packaged in a dosage form suitable for addition to a cleaning process.
  • the additive is packaged in a dosage form for addition to a cleaning process where a source of peroxygen is employed and increased bleaching effectiveness is desired.
  • Any suitable single unit dosage form finds use with the present disclosure, including but not limited to pills, tablets, gelcaps, or other single unit dosage form such as pre-measured powders or liquids.
  • filler(s) or carrier material(s) are included to increase the volume of such compositions.
  • Suitable filler or carrier materials include, but are not limited to various salts of sulfate, carbonate, and silicate as well as talc, clay, and the like.
  • Suitable filler or carrier materials for liquid compositions include, but are not limited to water or low molecular weight primary and secondary alcohols including polyols and diols. Examples of such alcohols include, but are not limited to methanol, ethanol, propanol, and isopropanol. In some embodiments, the compositions contain from about 5% to about 90% of such materials. Acidic fillers find use to reduce pH. Alternatively, in some embodiments, the cleaning additive includes one or more adjunct ingredients.
  • the cleaning composition or cleaning additive contains an effective amount of a mannanase variant described herein, optionally in combination with other mannanases and/or additional enzymes.
  • the additional enzymes include, but are not limited to, at least one enzyme selected from of acyl transferases, amylases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinases, arabinosidases, aryl esterases, beta-galactosidases, beta-glucanases, carrageenases, catalases, cellulases, chondroitinases, cutinases, dispersins, DNAses (also known as nucleases or dispersins), endo-glucanases, endo- beta-mannanases, exo-beta-mannanases, esterases, exo-mannanases, galactanases, glucoamylases
  • the cleaning compositions herein are typically formulated such that, during use in aqueous cleaning operations, the wash water will have a pH of from about 3.0 to about 11.
  • Liquid product formulations are typically formulated to have a neat pH from about 5.0 to about 9.0.
  • Granular laundry products are typically formulated to have a pH from about 8.0 to about 11.0.
  • Techniques for controlling pH at recommended usage levels include the use of buffers, alkalis, acids, etc., and are well known to those skilled in the art.
  • Suitable low pH cleaning compositions typically have a neat pH of from about 3.0 to about 5.0 or even from about 3.5 to about 4.5.
  • Low pH cleaning compositions are typically free of surfactants that hydrolyze in such a pH environment.
  • surfactants include sodium alkyl sulfate surfactants that comprise at least one ethylene oxide moiety or even from about 1 to about 16 moles of ethylene oxide.
  • Such cleaning compositions typically comprise a sufficient amount of a pH modifier, such as sodium hydroxide, monoethanolamine, or hydrochloric acid, to provide such cleaning composition with a neat pH of from about 3.0 to about 5.0.
  • Such compositions typically comprise at least one acid stable enzyme. In some embodiments, the compositions are liquids, while in other embodiments, they are solids.
  • the pH of such liquid compositions is typically measured as a neat pH.
  • the pH of such solid compositions is measured as a 10% solids solution of the composition wherein the solvent is distilled water. In these embodiments, all pH measurements are taken at 20°C, unless otherwise indicated.
  • Suitable high pH cleaning compositions typically have a neat pH of from about 9.0 to about 11.0, or even a neat pH of from 9.5 to 10.5.
  • Such cleaning compositions typically comprise a sufficient amount of a pH modifier, such as sodium hydroxide, monoethanolamine, or hydrochloric acid, to provide such cleaning composition with a neat pH of from about 9.0 to about 11.0.
  • Such compositions typically comprise at least one base-stable enzyme.
  • the compositions are liquids, while in other embodiments, they are solids.
  • the pH of such liquid compositions is typically measured as a neat pH.
  • the pH of such solid compositions is measured as a 10% solids solution of said composition wherein the solvent is distilled water.
  • the mannanase variant is in the form of an encapsulated particle to protect it from other components of the granular composition during storage.
  • encapsulation is also a means of controlling the availability of the mannanase variant during the cleaning process.
  • encapsulation enhances the performance of the mannanase variant and/or additional enzymes.
  • the mannanase variant is encapsulated with any suitable encapsulating material known in the art. Typically, the encapsulating material is water-soluble and/or water-dispersible.
  • the encapsulating material has a glass transition temperature (Tg) of 0°C or higher. Glass transition temperature is described in more detail in WO97/11151.
  • the encapsulating material is typically selected from carbohydrates, natural or synthetic gums, chitin, chitosan, cellulose and cellulose derivatives, silicates, phosphates, borates, polyvinyl alcohol, polyethylene glycol, paraffin waxes, and combinations thereof.
  • the encapsulating material is typically selected from monosaccharides, oligosaccharides, polysaccharides, and combinations thereof.
  • the encapsulating material is a starch (See, e.g., EP0922499 and US 4,977,252; 5,354,559; and 5,935,826).
  • the encapsulating material is a microsphere made from plastic such as thermoplastics, acrylonitrile, methacrylonitrile, polyacrylonitrile, polymethacrylonitrile, and mixtures thereof; commercially available microspheres that find use include, but are not limited to those supplied by EXPANCEL® (Stockviksverken, Sweden), and PM6545, PM6550, PM7220, PM7228, EXTENDOSPHERES®, LUXSIL®, Q-CEL®, and SPHERICEL® (PQ Corp., Valley Forge, PA).
  • the term “granular composition” refers to a conglomeration of discrete solid, macroscopic particles. Powders are a special class of granular material due to their small particle size, which makes them more cohesive and more
  • Concentrations of detergent compositions in typical wash solutions throughout the world vary from less than about 800 ppm of detergent composition (“low detergent concentration geographies”), for example about 667 ppm in Japan, to between about 800 ppm to about 2000 ppm (“medium detergent concentration geographies”), for example about 975 ppm in U.S. and about 1500 ppm in Brazil, to greater than about 2000 ppm (“high detergent concentration geographies”), for example about 4500 ppm to about 5000 ppm in Europe and about 6000 ppm in high suds phosphate builder geographies.
  • low detergent concentration geographies for example about 667 ppm in Japan
  • intermediate detergent concentration geographies for example about 975 ppm in U.S. and about 1500 ppm in Brazil
  • high detergent concentration geographies for example about 4500 ppm to about 5000 ppm in Europe and about 6000 ppm in high suds phosphate builder geographies.
  • the detergent compositions described herein may be utilized at a temperature of from about 10°C to about 60°C, or from about 20°C to about 60°C, or from about 30°C to about 60°C, from about 40°C to about 60°C, from about 40°C to about 55°C, or all ranges within 10°C to 60°C.
  • the detergent compositions described herein are used in “cold water washing” at temperatures of from about 10°C to about 40°C, or from about 20°C to about 30°C, from about 15°C to about 25°C, from about 15°C to about 35°C, or all ranges within 10°C to 40°C.
  • Water hardness is usually described in terms of the grains per gallon mixed Ca 2+ /Mg 2+ .
  • Hardness is a measure of the amount of calcium (Ca 2+ ) and magnesium (Mg 2+ ) in the water. Most water in the United States is hard, but the degree of hardness varies. Moderately hard (60- 120 ppm) to hard (121-181 ppm) water has 60 to 181 parts per million (parts per million converted to grains per U.S. gallon is ppm # divided by 17.1 equals grains per gallon) of hardness minerals.
  • European water hardness is typically greater than about 10.5 (for example about 10.5 to about 20.0) grains per gallon mixed Ca 2+ /Mg 2+ (e.g., about 15 grains per gallon mixed Ca 2+ /Mg 2+ ).
  • North American water hardness is typically greater than Japanese water hardness, but less than European water hardness.
  • North American water hardness can be between about 3 to about 10 grains, about 3 to about 8 grains or about 6 grains.
  • Japanese water hardness is typically lower than North American water hardness, usually less than about 4, for example about 3 grains per gallon mixed Ca 2+ /Mg 2+ .
  • a mannanase variant described herein is comparable in wash performance to commercially available mannanases. In some embodiments, a mannanase variant described herein exhibits enhanced wash performance as compared to commercially available mannanases. In some embodiments, a mannanase variant described herein exhibits enhanced cleaning capabilities under various conditions, and/or enhanced chelator stability. In addition, a mannanase variant described herein may find use in cleaning compositions that do not include detergents, again either alone or in combination with builders and stabilizers.
  • Suitable mannanases include, but are not limited to, mannanases of the GH26 family of glycosyl hydrolases, mannanases of the GH5 family of glycosyl hydrolases, acidic mannanases, neutral mannanases, and alkaline mannanases.
  • alkaline mannanases examples include those described in US 6,060,299; 6,566,114; and 6,602,842; and WO9535362, WO9964573, WO9964619, and WO2015022428. Additionally, suitable mannanases include, but are not limited to those of animal, plant, fungal, or bacterial origin. Chemically or genetically modified mutants are encompassed by the present disclosure. [00161] Examples of useful mannanases include Bacillus endo-P-mannanases such as B. subtilis endo-P-mannanase (See, e.g., US 6,060,299 and WO9964573), Bacillus sp.
  • endo-P- mannanase See, e.g., US 6,566,114 and WO9964619), Bacillus sp. AAI12 endo-P-mannanase (See, e.g., US 6,566,114 and WO9964619), B. sp. AA349 endo-P-mannanase (See, e.g., US 6,566,114 and WO9964619), B. agaradhaerens NCIMB 40482 endo-P-mannanase (See, e.g., US 6,566,114 and WO9964619), B. halodurans endo-P-mannanase, B.
  • clausii endo-P- mannanase See, e.g., US 6,566,114 and WO9964619
  • B. licheniformis endo-P-mannanase See, e.g., US 6,566,114 and WO9964619A1
  • Humicola endo-P-mannanases such as H. insolens endo-P-mannanase (See, e.g., US 6,566,114 and WO9964619)
  • Caldocellulosiruptor endo- P-mannanases such as C. sp. endo-P-mannanase (See, e.g., US 6,566,114 and WO9964619).
  • mannanases find use in some embodiments of the present disclosure, including but not limited to A bisporus mannanase (See, Tang et al., [2001] Appl. Environ. Microbiol. 67:2298- 2303), A. tamarii mannanase (See, Civas et al., [1984] Biochem. J. 219:857-863), A. aculeatus mannanase (See, Christgau et al., [1994] Biochem. Mol. Biol. Int. 33:917-925), A.
  • awamori mannanase See, Setati et al., [2001] Protein Express Purif. 21 : 105-114), A. fumigatus mannanase (See, Puchart et al., [2004] Biochimica et biophysica Acta. 1674:239-250), A. niger mannanase (See, Ademark et al., [1998] J. Biotechnol. 63 : 199-210), A. oryzae NRRL mannanase (See, Regalado et al., [2000] J. Sci. Food Agric. 80: 1343-1350), A.
  • B. subtilis mannanase See, Mendoza et al., [1994] World J. Microbiol. Biotechnol. 10:51-54
  • B. subtilis B36 mannanase Li et al., [2006] Z. Naturforsch (C). 61 :840-846
  • B. subtilis BM9602 mannanase See, Cui et al., [1999] Wei Sheng Wu Xue Bao. 39(1): 60-63
  • B. subtilis BM9602 mannanase See, Cui et al., [1999] Wei Sheng Wu Xue Bao. 39(1): 60-63
  • B. subtilis BM9602 mannanase See, Cui et al., [1999] Wei Sheng Wu Xue Bao. 39(1): 60-63
  • B. subtilis BM9602 mannanase See, Cui et al., [19
  • subtilis SA-22 mannanase See, Sun et al., [2003] Sheng Wu Gong Cheng Xue Bao. 19(3): 327-330), B. subliHs ⁇ 6?> mannanase (See, Helow and Khattab, [1996] Acta Microbiol. Immunol. Hung. 43:289-299), B. ovatus mannanase (See, Gherardini et al., [1987] J. Bacteriol. 169:2038-2043), B. ruminicola mannanase (See, Matsushita et al., [1991] J. Bacteriol. 173:6919-6926), C.
  • butyricum/beijerinckii mannanase See, Nakajima and Matsuura, [1997] Biosci. Biotechnol. Biochem. 61 :1739-1742), C. cellulolyticum mannanase (See, Perret et al., [2004] Biotechnol. Appl. Biochem. 40:255-259), C. tertium mannanase (See, Kataoka and Tokiwa, [1998] J. Appl. Microbiol. 84:357-367), C. thermocellum mannanase (See, Halstead et al., [1999] Microbiol. 145:3101-3108), D.
  • thermophilum mannanase See, Gibbs et al., [1999] Curr. Microbiol. 39(6):351-357
  • Flavobacterium sp. mannanase See, Zakaria et al., [1998] Biosci. Biotechnol. Biochem. 62:655-660
  • G. pulmonata mannanase See, Charrier and Rouland, [2001] J. Expt. Zool. 290: 125-135)
  • Z. brevicula mannanase See, Yamamura et al., [1996] Biosci. Biotechnol. Biochem. 60:674-676), Z.
  • Additional suitable mannanases include commercially available endo-P- mannanases such as HEMICELL® (Chemgen); GAMANASE® and MANNAWAY®, (Novozymes A/S, Denmark); EFFECTENZTM M 1000, PREFERENZ® M 100, PURABRITETM and MANNASTARTM (DuPont); and PYROLASE® 160 and PYROLASE® 200 (Diversa).
  • the composition described herein comprises one or more mannanase variant described herein and one or more additional enzyme.
  • the one or more additional enzyme is selected from acyl transferases, alpha-amylases, beta-amylases, alphagalactosidases, arabinosidases, aryl esterases, beta-galactosidases, carrageenases, catalases, cellobiohydrolases, cellulases, chondroitinases, cutinases, endo-beta-1, 4-glucanases, endo-beta- mannanases, esterases, exo-mannanases, galactanases, glucoamylases, hemicellulases, hyaluronidases, keratinases, laccases, lactases, ligninases, lipases, lipoxygenases, additional mannanases, metalloproteases
  • Some embodiments are directed to a combination of enzymes (i.e., a “cocktail”) comprising conventional enzymes like amylase, lipase, cutinase, protease and/or cellulase in conjunction with one or more mannanase variant described herein and/or one or more additional mannanase.
  • a combination of enzymes i.e., a “cocktail” comprising conventional enzymes like amylase, lipase, cutinase, protease and/or cellulase in conjunction with one or more mannanase variant described herein and/or one or more additional mannanase.
  • the cleaning compositions described herein further comprise a protease.
  • the composition comprises from about 0.00001 % to about 10% protease by weight of the composition.
  • the cleaning composition comprises from about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% protease by weight of the composition.
  • the protease is a serine protease. Suitable proteases include those of animal, vegetable or microbial origin.
  • the protease is a microbial protease.
  • the protease is a chemically or genetically modified mutant.
  • the protease is an alkaline microbial protease or a trypsin-like protease.
  • alkaline proteases include subtilisins derived from, for example, Bacillus (e.g., subtilisin, lentus, amyloliquefaciens, gibsonii, subtilisin Carlsberg, subtilisin 309, sp. TY- 145, subtilisin 147 and subtilisin 168).
  • Exemplary additional proteases include but are not limited to those described in WO92/21760, WO95/23221, W02008/010925, W009/149200, WO09/149144, WO09/149145, WO 10/056640, W010/056653, WO2010/0566356, WO1 1/072099, WO2011/13022, WO11/140364, WO12/151534, WO2015/038792, WO20 15/089447, WO2015/089441, WO2015/143360, WO2016/061438, WO2016/069548, WO20 16/069544, WO2016/069557, WO2016/069563, WO2016/069569, WO2016/069552, WO2016/145428, US Publ.
  • PCT/US16/32514 and PCT/US2016/038245 as well as metalloproteases described in WO1999014341, WO1999033960, WO1999014342, W01999034003, W02007044993, W02009058303, WO 2009058661, W02014071410, WO2014194032, WO2014194034, WO 2014194054, and WO 2014/194117.
  • Exemplary proteases include, but are not limited to trypsin (e.g., of porcine or bovine origin) and the Fusarium protease described in W089/06270.
  • Exemplary commercial proteases include, but are not limited to MAXATASE®, MAXACALTM, MAXAPEMTM, OPTICLEAN®, OPTIMASE®, PROPERASE®, PURAFECT®, PURAFECT® OXP, PURAMAXTM, EXCELLASETM, PREFERENZTM proteases (e.g. P100, Pl 10, P280), EFFECTENZTM proteases (e.g. P1000, P1050, P2000), EXCELLENZTM proteases (e.g.
  • the cleaning compositions described herein further comprise a suitable amylase.
  • the composition comprises from about 0.00001 % to about 10%, about 0.0001 % to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% amylase by weight of the composition.
  • Any amylase e.g., alpha and/or beta
  • suitable for use in alkaline solutions may be useful to include in such composition.
  • An exemplary amylase can be a chemically or genetically modified mutant.
  • amylases include, but are not limited to those of bacterial or fungal origin, such as, for example, amylases described in GB 1,296,839, W09100353, WO9402597, WO94183314, W09510603, WO9526397, WO9535382, WO9605295, WO9623873, WO9623874, WO 9630481, WO9710342, WO9741213, WO9743424, WO9813481, WO 9826078, W09902702, WO 9909183, WO9919467, WO9923211, WO9929876, WO9942567, WO 9943793, WO9943794, WO 9946399, W00029560, W00060058, W00060059, W00060060, WO 0114532, WO0134784, WO 0164852, WO0166712, W00188107, WO0196537, WO02092797,
  • Exemplary commercial amylases include, but are not limited to AMPLIFY®, AMPLIFY PRIME®, DUR AMYL” TERM AMYL” , FUNGAM YL” , STAINZYME®, STAINZYME PLUS®, STAINZYME PLUS®, STAINZYME ULTRA® EVITY®, and BANTM (Novozymes); EFFECTENZTM S 1000, POWERASETM, PREFERENZTM S 100, PREFERENZTM S 110, EXCELLENZTM S 2000, RAPIDASE® and MAXAMYL® P (DuPont).
  • the cleaning compositions described herein further comprise a suitable pectin degrading enzyme.
  • pectin degrading enzyme(s) encompass arabinanase (EC 3.2.1.99), galactanases (EC 3.2.1.89), polygalacturonase (EC 3.2.1.15) exo-polygalacturonase (EC 3.2.1.67), exo-poly-alpha-galacturonosidase (EC 3.2.1.82), pectin lyase (EC 4.2.2.10), pectin esterase (EC 3.1.1.11), pectate lyase (EC 4.2.2.2), exo- polygalacturonate lyase (EC 4.2.2.9) and hemicellulases such as endo-l,3-P-xylosidase (EC 3.2.1.32), xylan- 1,4-P-xylosidase (EC 3.2.1.37) and a-
  • Pectin degrading enzymes are natural mixtures of the above mentioned enzymatic activities.
  • Pectin enzymes therefore include the pectin methylesterases which hydrolyse the pectin methyl ester linkages, polygalacturonases which cleave the glycosidic bonds between galacturonic acid molecules, and the pectin transeliminases or lyases which act on the pectic acids to bring about non-hydrolytic cleavage of a- 1,4 glycosidic linkages to form unsaturated derivatives of galacturonic acid.
  • Suitable pectin degrading enzymes include those of plant, fungal, or microbial origin. In some embodiments, chemically or genetically modified mutants are included.
  • the pectin degrading enzymes are alkaline pectin degrading enzymes, i.e., enzymes having an enzymatic activity of at least 10%, at least 25%, or at least 40% of their maximum activity at a pH of from about 7.0 to about 12. In certain other embodiments, the pectin degrading enzymes are enzymes having their maximum activity at a pH of from about 7.0 to about 12.
  • Alkaline pectin degrading enzymes are produced by alkalophilic microorganisms e.g., bacterial, fungal, and yeast microorganisms such as Bacillus species.
  • the microorganisms are B. firmus. B. circulans, and 7>. subtilis as described in JP 56131376 and JP 56068393.
  • Alkaline pectin decomposing enzymes may include but are not limited to galacturan-l,4-a-galacturonidase (EC 3.2.1.67), poly-galacturonase activities (EC 3.2.1.15, pectin esterase (EC 3.1.1.11), pectate lyase (EC 4.2.2.2) and their iso enzymes.
  • Alkaline pectin decomposing enzymes can be produced by the Erwinia species.
  • the alkaline pectin decomposing enzymes are produced by E.chrysanthemi, E.carotovora, E.amylovora, E.herbicola, and E.dissolvens as described in JP 59066588, JP 63042988, and in World J. Microbiol. Biotechnol. (8, 2, 115-120) 1992.
  • the alkaline pectin enzymes are produced by Bacillus species as disclosed in JP 73006557 and Agr. Biol. Chem. (1972), 36 (2) 285-93.
  • the cleaning compositions described herein further comprise about 0.00001% to about 10%, about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% of pectin degrading enzyme by weight of the composition.
  • the cleaning compositions described herein further comprise a suitable xyloglucanase.
  • Suitable xyloglucanases include, but are not limited to those of plant, fungal, or bacterial origin. Chemically or genetically modified mutants are included in some embodiments.
  • xyloglucanase(s) encompass the family of enzymes described by Vincken and Voragen at Wageningen University [Vincken et al (1994) Plant Physiol., 104, 99-107] and are able to degrade xyloglucans as described in Hayashi et al (1989) Annu. Rev. Plant. Physiol. Plant Mol. Biol., 40, 139-168.
  • Vincken et al demonstrated the removal of xyloglucan coating from cellulose of the isolated apple cell wall by a xyloglucanase purified from Trichoderma viride (endo-IV-glucanase). This enzyme enhances the enzymatic degradation of cell wall-embedded cellulose and work in synergy with pectic enzymes.
  • Rapidase LIQ+ from DSM contains a xyloglucanase activity.
  • the cleaning compositions described herein further comprise from about 0.00001% to about 10%, about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% xyloglucanase by weight of the composition.
  • xyloglucanases for specific applications are alkaline xyloglucanases, i.e., enzymes having an enzymatic activity of at least 10%, at least 25%, or at least 40% of its maximum activity at a pH ranging from 7 to 12.
  • the xyloglucanases are enzymes having a maximum activity at a pH of from about 7.0 to about 12.
  • the detergent compositions described herein further comprise a suitable cellulase.
  • the composition comprises from about 0.00001% to about 10%, 0.0001 % to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% cellulase by weight of the composition. Any suitable cellulase may find use in a composition described herein.
  • An exemplary cellulase can be a chemically or genetically modified mutant.
  • Exemplary cellulases include, but are not limited to those of bacterial or fungal origin, such as, for example, those described in W02005054475, W02005056787, US 7,449,318, US 7,833,773, US 4,435,307; EP 0495257; and US Provisional Appl. No. 62/296,678.
  • Exemplary commercial cellulases include, but are not limited to, CELLUCLEAN®, CELLUZYME®, CAREZYME®, ENDOLASE®, RENOZYME®, and CAREZYME® PREMIUM (Novozymes); REVITALENZTM 100, REVITALENZTM 200/220, and REVITALENZ® 2000 (DuPont); and KAC-500(B)TM (Kao Corporation).
  • cellulases are incorporated as portions or fragments of mature wild-type or variant cellulases, wherein a portion of the N-terminus is deleted (see, e.g., US 5,874,276).
  • the detergent compositions described herein further comprise a suitable lipase.
  • the composition comprises from about 0.00001 % to about 10%, about 0.0001 % to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, or about 0.005% to about 0.5% lipase by weight composition.
  • An exemplary lipase can be a chemically or genetically modified mutant.
  • Exemplary lipases include, but are not limited to, e.g., those of bacterial or fungal origin, such as, e.g., H. lanuginosa lipase (see, e.g., EP 258068 and EP 305216), T.
  • lanuginosus lipase see, e.g., WO 2014/059360 and W02015/010009
  • Rhizomucor miehei lipase see, e.g., EP 238023
  • Candida lipase such as C. antarctica lipase (e.g., C. antarctica lipase A or B) (see, e.g., EP 214761), Pseudomonas lipases such as P. alcaligenes and P. pseudoalcaligenes lipase (see, e.g. , EP 218272), P. cepacia lipase (see, e.g., EP 331376), P.
  • C. antarctica lipase e.g., C. antarctica lipase A or B
  • Pseudomonas lipases such as P. alcaligenes and P. pseudoalcaligenes lipase (see
  • stutzeri lipase see, e.g., GB 1,372,034
  • P. fluorescens lipase Bacillus lipase (e.g., B. subtilis lipase (Dartois et al., Biochem. Biophys. Acta 1131 :253-260 (1993)), B. stearothermophilus lipase (see, e.g., JP 64/744992), and B. pumilus lipase (see, e.g., WO 91/16422)).
  • Exemplary cloned lipases include, but are not limited to Penicillium camembertii lipase (See, Yamaguchi et al., Gene 103:61-67 (1991)), Geotricum candidum lipase (See, Schimada et al., J. Biochem., 106:383-388 (1989)), and various Rhizopus lipases, such as, R. delemar lipase (See, Hass et al., Gene 109: 117-113 (1991)), R. niveus lipase (Kugimiya et al., Biosci. Biotech. Biochem. 56:716-719 (1992)) and R oryzae lipase.
  • Penicillium camembertii lipase See, Yamaguchi et al., Gene 103:61-67 (1991)
  • Geotricum candidum lipase See, Schimada et al., J. Biochem.,
  • lipolytic enzymes such as cutinases
  • cutinases may also find use in one or more composition described herein, including, but not limited to, e.g., cutinase derived from Pseudomonas mendocina (see, WO 88/09367) and/ or Fusarium solani pisi (see, W090/09446).
  • Exemplary commercial lipases include, but are not limited to Ml LIPASETM, LUMA FASTTM, and LIPOMAXTM (DuPont); LIPEX®, LIPOCLEAN®, LIPOLASE® and LIPOLASE® ULTRA (Novozymes); and LIPASE PTM (Amano Pharmaceutical Co. Ltd).
  • cleaning compositions described herein further comprise peroxidases in combination with hydrogen peroxide or a source thereof (e.g., a percarbonate, perborate or persulfate).
  • oxidases are used in combination with oxygen. Both types of enzymes are used for "solution bleaching" (i.e., to prevent transfer of a textile dye from a dyed fabric to another fabric when the fabrics are washed together in a wash liquor), preferably together with an enhancing agent (See, e.g., WO94/12621 and WO95/01426).
  • Suitable peroxidases/oxidases include, but are not limited to those of plant, bacterial or fungal origin.
  • the cleaning compositions of the present disclosure further comprise from about 0.00001% to about 10%, about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, about 0.005% to about 0.5% of peroxidase and/or oxidase by weight of the composition.
  • cleaning compositions described herein further comprise additional enzymes, including but not limited to perhydrolases (See, e.g., WO 05/056782).
  • Some embodiments are directed to mixtures of one or more above mentioned protease, amylase, lipase, mannanase, and/or cellulase.
  • the cleaning compositions described herein are compact granular fabric cleaning compositions, while in other embodiments the composition is a granular fabric cleaning composition useful in the laundering of colored fabrics.
  • the composition is a granular fabric cleaning composition which provides softening through the wash capacity, and in additional embodiments the composition is a heavy duty liquid (HDL) fabric cleaning composition.
  • the cleaning compositions described herein are fabric cleaning compositions such as, for example, those described in US 6,610,642 and 6,376,450.
  • the cleaning compositions described herein are suitable hard surface cleaning compositions.
  • Suitable hard surface cleaning compositions include, for example, those described in US 6,610,642; 6,376,450; and 6,376,450.
  • the cleaning compositions described herein are dishwashing compositions.
  • the compositions described herein are oral care compositions such as, for example, those described in US 6,376,450 and 6,605,458. The formulations and descriptions of the compounds and cleaning adjunct materials contained in the aforementioned US 6,376,450; 6,605,458; and 6,610,642 find use with a polypeptide of the present invention.
  • the cleaning compositions described herein are fabric softening compositions such as, for example, those described in GB 400898, GB 514276, EP0011340, EP0026528, EP0242919, EP0299575, EP0313146, and US 5,019,292.
  • the cleaning compositions described herein can be formulated into any suitable form and prepared by any process chosen by the formulator, non-limiting examples of which are described in US 5,879,584; 5,691,297; 5,574,005; 5,569,645; 5,565,422; 5,516,448; 5,489,392; and 5,486,303.
  • the pH of such composition is adjusted via the addition of a material such as monoethanolamine or an acidic material such as HC1.
  • the cleaning compositions described herein are provided in unit dose form, including tablets, capsules, sachets, pouches, sheets, and multi-compartment pouches.
  • the unit dose format is designed to provide controlled release of the ingredients within a multi-compartment pouch (or other unit dose format). Suitable unit dose and controlled release formats are known in the art (See e.g., EP2100949, EP2100947, W002/102955, WO04/111178, WO2013/165725, and US 4,765,916 and 4,972,017).
  • the unit dose form is provided by tablets wrapped with a water-soluble film or water-soluble pouches.
  • the cleaning compositions described herein further comprise at least one chelating agent.
  • Suitable chelating agents may include, but are not limited to copper, iron, and/or manganese chelating agents, and mixtures thereof.
  • the cleaning compositions of the present disclosure comprise from about 0.1% to about 15% or even from about 3.0% to about 10% chelating agent by weight of the cleaning composition.
  • the cleaning compositions described herein further comprise at least one deposition aid.
  • Suitable deposition aids include, but are not limited to, polyethylene glycol, polypropylene glycol, polycarboxylate, soil release polymers such as polyterephthalic acid, clays such as kaolinite, montmorillonite, attapulgite, illite, bentonite, halloysite, and mixtures thereof.
  • the cleaning compositions described herein further comprise at least one anti-redeposition agent.
  • the anti-redeposition agent is a non-ionic surfactant, such as, for example, described in EP2100949.
  • non-ionic surfactants are used as surface modifiers, in particular for sheeting, to avoid filming and spotting and to improve shine.
  • the cleaning compositions described herein further comprise one or more dye transfer inhibiting agents.
  • Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones, and polyvinylimidazoles, or mixtures thereof.
  • the cleaning compositions described herein comprise from about 0.0001% to about 10%, from about 0.01% to about 5%, or even from about 0.1% to about 3% dye transfer inhibiting agent by weight of the cleaning composition.
  • the cleaning compositions described herein further comprise one or more silicates.
  • sodium silicates e.g., sodium disilicate, sodium metasilicate, and crystalline phyllosilicates
  • the cleaning compositions described herein comprise from about 1% to about 20% or from about 5% to about 15% silicate by weight of the composition.
  • the cleaning compositions described herein further comprise one or more dispersant.
  • Suitable water-soluble organic materials include, but are not limited to the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.
  • the enzymes used in the cleaning compositions are stabilized by any suitable technique.
  • the enzymes employed herein are stabilized by the presence of water-soluble sources of calcium and/or magnesium ions in the finished compositions.
  • the enzyme stabilizers include oligosaccharides, polysaccharides, and inorganic divalent metal salts, including alkaline earth metals, such as calcium salts. It is contemplated that various techniques for enzyme stabilization will find use in the present disclosure.
  • the enzymes employed herein are stabilized by the presence of water-soluble sources of zinc (II), calcium (II), and/or magnesium (II) ions in the finished compositions, as well as other metal ions e.g., barium (II), scandium (II), iron (II), manganese (II), aluminum (III), tin (II), cobalt (II), copper (II), nickel (II), and oxovanadium (IV)). Chlorides and sulfates also find use in some embodiments.
  • oligosaccharides and polysaccharides are known in the art (See, e.g., WO07/145964).
  • reversible protease inhibitors such as boron-containing compounds (e.g., borate, 4-formyl phenyl boronic acid) and/or a peptide aldehyde US9,181,296B2) find use to further improve stability.
  • the cleaning compositions described herein further comprise one or more bleach, bleach activator, and/or bleach catalyst.
  • the cleaning compositions described herein comprise inorganic and/or organic bleaching compound(s).
  • Inorganic bleaches may include, but are not limited to perhydrate salts (e.g, perborate, percarbonate, perphosphate, persulfate, and persilicate salts).
  • inorganic perhydrate salts are alkali metal salts.
  • inorganic perhydrate salts are included as the crystalline solid, without additional protection, although in some other embodiments, the salt is coated. Suitable salts include, for example, those described in EP2100949.
  • Bleach activators are typically organic peracid precursors that enhance the bleaching action in the course of cleaning at temperatures of 60°C and below.
  • Bleach activators suitable for use herein include compounds which, under perhydrolysis conditions, give aliphatic peroxy carboxylic acids having preferably from about 1 to about 10 carbon atoms, in particular from about 2 to about 4 carbon atoms, and/or optionally substituted perbenzoic acid.
  • Suitable bleach activators include, for example, those described in EP2100949.
  • Bleach catalysts typically include, for example, manganese triazacyclononane and related complexes, and cobalt, copper, manganese, and iron complexes, as well as those described in US 4,246,612; 5,227,084; 4,810,410; and WO99/06521and EP2100949.
  • the cleaning compositions described herein further comprise one or more catalytic metal complex.
  • a metal-containing bleach catalyst finds use.
  • the metal bleach catalyst comprises a catalyst system comprising a transition metal cation of defined bleach catalytic activity (e.g., copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganese cations), an auxiliary metal cation having little or no bleach catalytic activity (e.g., zinc or aluminum cations), and a sequestrate having defined stability constants for the catalytic and auxiliary metal cations, particularly ethylenediaminetetraacetic acid, ethylenediaminetetra (methylenephosphonic acid) and water-soluble salts thereof are used (See, e.g., US 4,430,243).
  • a transition metal cation of defined bleach catalytic activity e.g., copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganese cations
  • the cleaning compositions described herein are catalyzed by means of a manganese compound.
  • a manganese compound Such compounds and levels of use are well known in the art (See, e.g., US 5,576,282).
  • cobalt bleach catalysts find use in the cleaning compositions described herein.
  • Various cobalt bleach catalysts are known in the art (See, e.g., US 5,597,936 and 5,595,967) and are readily prepared by known procedures.
  • the cleaning compositions described herein further comprise a transition metal complex of a macropolycyclic rigid ligand (MRL).
  • MRL macropolycyclic rigid ligand
  • the compositions and cleaning processes provided herein are adjusted to provide on the order of at least one part per hundred million of the active MRL species in the aqueous washing medium, and in other embodiments, provide from about 0.005 ppm to about 25 ppm, from about 0.05 ppm to about 10 ppm, or from about 0.1 ppm to about 5 ppm of the MRL in the wash liquor.
  • the transition-metal in the instant transition-metal bleach catalyst include, but are not limited to manganese, iron, and chromium.
  • MRLs include, but are not limited to special ultra-rigid ligands that are cross-bridged (e.g., 5,12- diethyl-l,5,8,12-tetraazabicyclo[6.6.2] hexadecane). Suitable transition metal MRLs are readily prepared by known procedures (See, e.g., WO 2000/32601 and US 6,225,464).
  • the cleaning compositions described herein further comprise a metal care agent.
  • Metal care agents are used to prevent and/or reduce tarnishing, corrosion, and/or oxidation of metals, including aluminum, stainless steel, and non-ferrous metals (e.g., silver and copper). Suitable metal care agents include those described in EP2100949, WO94/26860, and WO94/26859).
  • the metal care agent is a zinc salt.
  • the cleaning compositions described herein comprise from about 0.1% to about 5% by weight of one or more metal care agent.
  • the cleaning compositions described herein can be used to clean a surface, dishware, or fabric. Typically, at least a portion of the surface, dishware, or fabric is contacted with at least one (i) variant described herein, or (ii) at least one cleaning composition described herein, and then the surface, dishware, or fabric is optionally washed and/or rinsed.
  • “washing” includes but is not limited to, scrubbing and mechanical agitation.
  • the cleaning compositions are typically employed at concentrations of from about 500 ppm to about 15,000 ppm in solution.
  • the wash solvent is water
  • the water temperature typically ranges from about 5 °C to about 90°C and, when fabric is involved, the water to fabric mass ratio is typically from about 1 : 1 to about 30: 1.
  • Some embodiments are directed to a method of cleaning comprising contacting an effective amount of (i) a mannanase variant described herein, or (ii) a cleaning composition described herein with an item or surface comprising a soil or stain comprising mannan to hydrolyze the mannan contained in the soil or stain.
  • one or more mannanase variant described herein is used to prevent, reduce and/or remove a biofilm on one or more item selected from a textile and fabric.
  • One or more mannanase variant described herein hydrolyzes polysaccharide chains containing mannose units, including, but not limited to, mannans, galactomannans, and glucomannans, making such polypeptides particularly useful for performing mannan hydrolysis reactions involving polysaccharide substrates containing 1,4-P-D-mannosidic linkages.
  • a donor molecule is incubated in the presence of a mannanase variant described herein under conditions suitable for performing a mannan hydrolysis reaction, followed by, optionally, isolating a product from the reaction.
  • the product may become a component of the foodstuff without isolation.
  • the donor molecule is a polysaccharide chain comprising mannose units, including but not limited to mannans, glucomannans, galactomannans, and galactoglucomannans.
  • one or more mannanase variants described herein is used in a process for extracting palm kernel oil.
  • Another embodiment is directed to a process for extracting palm kernel oil from palm kernels or a palm kernel meal, comprising providing palm kernels and/or palm kernel meal and treating said seeds or cake with one or more mannanase variant described herein.
  • a composition comprising a mannanase variant described herein is used to process and/or manufacture animal feed or food for humans.
  • a mannanase variant described herein can be an additive to feed for non-human animals.
  • a mannanase variant described herein can be useful for human food, such as, for example, as an additive to human food.
  • plant material containing oligomannans such as mannan, galactomannan, glucomannan and galactoglucomannan can reduce an animal’s ability to digest and absorb nutritional compounds such as minerals, vitamins, sugars, and fats.
  • oligomannans such as mannan, galactomannan, glucomannan and galactoglucomannan can reduce an animal’s ability to digest and absorb nutritional compounds such as minerals, vitamins, sugars, and fats.
  • mannanase variant described herein can break down the mannan- containing polymers into simpler sugars, which can be more readily assimilated to provide additional energy.
  • animal feed containing plant material is incubated in the presence of a mannanase variant described herein under conditions suitable for breaking down mannan-containing polymers.
  • a bread improver composition comprises a mannanase variant described herein, optionally in combination with a source of mannan or glucomannan or galactomannan, and further optionally in combination with one or more other enzymes.
  • non-human animal includes all non-ruminant and ruminant animals.
  • the non-ruminant animal is selected from the group consisting of, but is not limited to, horses and monogastric animals such as, but not limited to, pigs, poultry, swine and fish.
  • the pig may be, but is not limited to, a piglet, a growing pig, and a sow;
  • the poultry may be, but is not limited to, a turkey, a duck and a chicken including, but not limited to, a broiler chick and a layer;
  • fish may be, but is not limited to salmon, trout, tilapia, catfish and carps; and crustaceans including but not limited to shrimps and prawns.
  • the ruminant animal is selected from the group consisting of, but is not limited to, cattle, young calves, goats, sheep, giraffes, bison, moose, elk, yaks, water buffalo, deer, camels, alpacas, llamas, antelope, pronghorn, and nilgai.
  • a mannanase variant described herein is used to pretreat feed instead of as a feed additive.
  • a mannanase variant described herein is added to, or used to pretreat, feed for weanling pigs, nursery pigs, piglets, fattening pigs, growing pigs, finishing pigs, laying hens, broiler chicks, and turkeys.
  • a mannanase variant described herein is added to, or used to pretreat, feed from plant material such as palm kernel, coconut, konjac, locust bean gum, gum guar, soy beans, barley, oats, flax, wheat, corn, linseed, citrus pulp, cottonseed, groundnut, rapeseed, sunflower, peas, and lupines.
  • plant material such as palm kernel, coconut, konjac, locust bean gum, gum guar, soy beans, barley, oats, flax, wheat, corn, linseed, citrus pulp, cottonseed, groundnut, rapeseed, sunflower, peas, and lupines.
  • a mannanase variant described herein is thermostable, and as a result, a mannanase variant described herein can be used in processes of producing pelleted feed in which heat is applied to the feed mixture before the pelleting step.
  • a mannanase variant described herein is added to the other feed ingredients either in advance of the pelleting step or after the pelleting step (i.e., to the already formed feed pellets).
  • food processing or feed supplement compositions that contain a mannanase variant described herein may optionally further contain other substituents selected from coloring agents, aroma compounds, stabilizers, vitamins, minerals, and other feed or food enhancing enzymes. This applies in particular to the so-called pre-mixes.
  • a food additive according to the present invention may be combined in an appropriate amount with other food components, such as, for example, a cereal or plant protein to form a processed food product.
  • an animal feed composition and/or animal feed additive composition and/or pet food comprises a polypeptide described herein.
  • Another embodiment relates to a method for preparing an animal feed composition and/or animal feed additive composition and/or pet food comprising mixing a mannanase variant described herein with one or more animal feed ingredients and/or animal feed additive ingredients and/or pet food ingredients.
  • a further embodiment relates to the use of a mannanase variant described herein to prepare an animal feed composition and/or animal feed additive composition and/or pet food.
  • the phrase “pet food” means food for a household animal such as, but not limited to, dogs; cats; gerbils; hamsters; chinchillas; fancy rats; guinea pigs; avian pets, such as canaries, parakeets, and parrots; reptile pets, such as turtles, lizards and snakes; and aquatic pets, such as tropical fish and frogs.
  • animal feed composition feedstuff and fodder are used interchangeably and may comprise one or more feed materials selected from the group comprising a) cereals, such as small grains (e.g., wheat, barley, rye, oats and combinations thereof) and/or large grains such as maize or sorghum; b) by-products from cereals, such as corn gluten meal, Distillers Dried Grain Solubles (DDGS) (particularly corn based Distillers Dried Grain Solubles (cDDGS)), wheat bran, wheat middlings, wheat shorts, rice bran, rice hulls, oat hulls, palm kernel, and citrus pulp; c) protein obtained from sources such as soya, sunflower, peanut, lupin, peas, fava beans, cotton, canola, fish meal, dried plasma protein, meat and bone meal, potato protein, whey, copra, and sesame; d) oils and fats obtained from vegetable and animal sources; and e)
  • cereals such as small
  • the food composition or additive may be liquid or solid.
  • the food composition is a beverage, including, but not limited to, a fermented beverage such as beer and wine.
  • the term “fermented beverage” is meant to comprise any beverage produced by a method comprising a fermentation process, such as a microbial fermentation, such as a bacterial and/or yeast fermentation.
  • the fermented beverage is beer.
  • beer is meant to comprise any fermented wort produced by fermentation/brewing of a starch-containing plant material. Often, beer is produced from malt or adjunct, or any combination of malt and adjunct as the starch-containing plant material.
  • malt is understood as any malted cereal grain, such as malted barley or wheat.
  • adjunct refers to any starch and/or sugar containing plant material which is not malt, such as barley or wheat malt.
  • adjuncts include, for example, common corn grits, refined corn grits, brewer's milled yeast, rice, sorghum, refined corn starch, barley, barley starch, dehusked barley, wheat, wheat starch, torrified cereal, cereal flakes, rye, oats, potato, tapioca, cassava and syrups, such as corn syrup, sugar cane syrup, inverted sugar syrup, barley and/or wheat syrups, and the like may be used as a source of starch.
  • the term "mash” refers to an aqueous slurry of any starch and/or sugar containing plant material such as grist, e. g. comprising crushed barley malt, crushed barley, and/or other adjunct or a combination hereof, mixed with water, later to be separated into wort and spent grains.
  • wort refers to the unfermented liquor run-off following extracting the grist during mashing.
  • the invention in another aspect relates to a method of preparing a fermented beverage such as beer comprising mixing a mannanase variant described herein with a malt and/or adjunct.
  • Examples of beers comprise: full malted beer, beer brewed under the “Rösgebo ’, ale, IP A, lager, bitter, Happoshu (second beer), third beer, dry beer, near beer, light beer, low alcohol beer, low calorie beer, porter, bock beer, stout, malt liquor, non-alcoholic beer, non-alcoholic malt liquor and the like, as well as alternative cereal and malt beverages such as fruit flavoured malt beverages, e. g. citrus flavoured, such as lemon-, orange-, lime-, or berry -flavoured malt beverages; liquor flavoured malt beverages, e. g. , vodka-, rum-, or tequila- flavoured malt liquor; or coffee flavoured malt beverages, such as caffeine-flavoured malt liquor; and the like.
  • fruit flavoured malt beverages e. g. citrus flavoured, such as lemon-, orange-, lime-, or berry -flavoured
  • One aspect of the invention relates to the use of a mannanase variant described herein in the production of a fermented beverage, such as a beer.
  • Another aspect concerns a method of providing a fermented beverage comprising the step of contacting a mash and/or wort with a mannanase variant described herein.
  • a further aspect relates to a method of providing a fermented beverage comprising the steps of: (a) preparing a mash, (b) filtering the mash to obtain a wort, and (c) fermenting the wort to obtain a fermented beverage, such as a beer, wherein a mannanase variant described herein is added to: (i) the mash of step (a) and/or (ii) the wort of step (b) and/or (iii) the wort of step (c).
  • a fermented beverage such as a beer
  • a method comprising the step(s) of (1) contacting a mash and/or a wort with a mannanase variant described herein; and/or (2) (a) preparing a mash, (b) filtering the mash to obtain a wort, and (c) fermenting the wort to obtain a fermented beverage, such as a beer, wherein a mannanase variant described herein is added to: (i) the mash of step (a) and/or (ii) the wort of step (b) and/or (iii) the wort of step (c).
  • the coffee extract is incubated in the presence of a mannanase variant described herein under conditions suitable for hydrolyzing galactomannans present in liquid coffee extract.
  • the invention in another aspect relates to a method of preparing baked products comprising addition of a mannanase variant described herein to dough, followed by baking the dough.
  • baked products are well known to those skilled in the art and include breads, rolls, puff pastries, sweet fermented doughs, buns, cakes, crackers, cookies, biscuits, waffles, wafers, tortillas, breakfast cereals, extruded products, and the like.
  • a mannanase variant described herein may be added to dough as part of a bread improver composition.
  • Bread improvers are compositions containing a variety of ingredients, which improve dough properties and the quality of bakery products, e.g. bread and cakes.
  • Bread improvers are often added in industrial bakery processes because of their beneficial effects e.g. the dough stability and the bread texture and volume.
  • Bread improvers usually contain fats and oils as well as additives like emulsifiers, enzymes, antioxidants, oxidants, stabilizers and reducing agents.
  • enzymes which may also be present in the bread improver or which may be otherwise used in conjunction with any of the polypeptides of the present invention include amylases, hemicellulases, amylolytic complexes, lipases, proteases, xylanases, pectinases, pullulanases, nonstarch polysaccharide degrading enzymes and redox enzymes like glucose oxidase, lipoxygenase or ascorbic acid oxidase.
  • a mannanase variant described herein may be added to dough as part of a bread improver composition which also comprises a glucomannan and/or galactomannan source such as konjac gum, guar gum, locust bean gum (Ceratonia siliqua), copra meal, ivory nut mannan (Phytelephas macrocarpa), seaweed mannan extract, coconut meal, and the cell wall of brewer’s yeast (may be dried, or used in the form of brewer’s yeast extract).
  • a glucomannan and/or galactomannan source such as konjac gum, guar gum, locust bean gum (Ceratonia siliqua), copra meal, ivory nut mannan (Phytelephas macrocarpa), seaweed mannan extract, coconut meal, and the cell wall of brewer’s yeast (may be dried, or used in the form of brewer’s yeast extract).
  • mannan derivatives for use in the current invention include unbranched P-l,4-linked mannan homopolymer and manno-oligosaccharides (mannobiose, mannotriose, mannotetraose and mannopentoase).
  • a mannanase variant described herein can be further used either alone, or in combination with a glucomannan and/or galactomannan and/or galactoglucomannan to improve the dough tolerance; dough flexibility and/or dough stickiness; and/or bread crumb structure, as well as retarding staling of the bread.
  • the mannanase hydrolysates act as soluble prebiotics such as manno-oligosaccharides (MOS) which promote the growth of lactic acid bacteria commonly associated with good health when found at favourable population densities in the colon.
  • MOS manno-oligosaccharides
  • the dough to which any polypeptide of the invention is added comprises bran or oat, rice, millet, maize, or legume flour in addition to or instead of pure wheat flour (i.e., is not a pure white flour dough).
  • a mannanase variant described herein may be added to milk or any other dairy product to which has also been added a glucomannan and/or galactomannan.
  • Typical glucomannan and/or galactomannan sources are listed above in the bakery aspects, and include guar or konjac gum.
  • mannanase variants described herein with a glucomannan and/or galactomannan releases mannanase hydrolysates (mannooligosaccharides) which act as soluble prebiotics by promoting the selective growth and proliferation of probiotic bacteria (especially Bifidobacteria and Lactobacillus lactic acid bacteria) commonly associated with good health when found at favourable population densities in the large intestine or colon.
  • probiotic bacteria especially Bifidobacteria and Lactobacillus lactic acid bacteria
  • Another aspect relates to a method of preparing milk or dairy products comprising addition of a mannanase variant described herein and any glucomannan or galactomannan or galactoglucomannan.
  • a mannanase variant described herein is used in combination with any glucomannan or galactomannan prior to or following addition to a dairy based foodstuff to produce a dairy based foodstuff comprising prebiotic mannan hydrolysates.
  • the thusly produced mannooligosacharide-containing dairy product is capable of increasing the population of beneficial human intestinal microflora
  • the dairy based foodstuff may comprise a mannanase variant described herein together with any source of glucomannan and/or galactomannan and/or galactoglucomannan, and a dose sufficient for inoculation of at least one strain of bacteria (such as Bifidobacteria o Lactobacillus') known to be of benefit in the human large intestine.
  • the dairy -based foodstuff is a yoghurt or milk drink.
  • the mannanase variant described herein finds further use in the enzyme aided bleaching of paper pulps such as chemical pulps, semi-chemical pulps, kraft pulps, mechanical pulps, and pulps prepared by the sulfite method.
  • paper pulps are incubated with a mannanase variant described herein under conditions suitable for bleaching the paper pulp.
  • the pulps are chlorine free pulps bleached with oxygen, ozone, peroxide or peroxyacids.
  • a mannanase variant described herein is used in enzyme aided bleaching of pulps produced by modified or continuous pulping methods that exhibit low lignin contents.
  • a mannanase variant described herein is applied alone or preferably in combination with xylanase and/or endoglucanase and/or alpha-galactosidase and/or cellobiohydrolase enzymes.
  • Galactomannans such as guar gum and locust bean gum are widely used as thickening agents e.g., in food (e.g., ice cream) and print paste for textile printing such as prints on T-shirts.
  • a mannanase variant described herein also finds use in reducing the thickness or viscosity of mannan-containing substrates.
  • one or more mannanase variant described herein is used to hydrolyze galactomannans in a food (e.g., ice cream) manufacturing waste stream.
  • a mannanase variant described herein is used for reducing the viscosity of residual food in processing equipment thereby facilitating cleaning after processing.
  • a mannanase variant described herein is used for reducing viscosity of print paste, thereby facilitating wash out of surplus print paste after textile printings.
  • a mannan-containing substrate is incubated with a mannanase variant described herein under conditions suitable for reducing the viscosity of the mannan-containing substrate.
  • one or more mannanase variant described herein can be used in the oil and gas industry to, for example, control the viscosity of drilling fluids; increase the rate at which the fluids used in hydraulic fracturing create subterranean fractures that extend from the borehole into the rock; clean the borehole filter cake; and combinations thereof.
  • compositions and methods disclosed herein are as follows: [00236] 1.
  • a mannanase variant comprising an amino acid substitution comparing to a parent mannanase enzyme at a position selected from the group consisting of 32, 72, 161 and 172 wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of the parent enzyme of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • a mannanase variant comprising an amino acid substitution, wherein said variant comprises a substitution selected from the group consisting of 19D, 32Y, 34D, 72V, 93Q, 13 IS, 136P, 139R, 161G, 172F, 225N/Q, 259D, 261DZE and 276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • a mannanase variant comprising an amino acid substitution, wherein said variant comprises a substitution selected from the group consisting of P019D, F032Y, N034D, I072V, K093Q, T131S, A136P, D139R, A161G, V172F, G225N/Q, G259D, N261D/E, and F276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • a mannanase variant comprising an amino acid substitution, wherein said variant comprises a substitution selected from the group consisting of E019D, F032Y, N034D, I072V, K093Q, T131S, A136P, D139R, A161G, V172F, C225N/Q, G259D, R261D/E, and F276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 2, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 2.
  • a mannanase variant comprising two or more amino acid substitutions selected from the group consisting of 19D, 32Y, 72V, 93Q, 13 IS, 136P, 139R, 161G, 168T, 172F, 225N/Q, 259DZE, 261DZE and 276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • a mannanase variant comprising two or more amino acid substitutions selected from the group consisting of P019D, F032Y, I072V, K093Q, T131S, A136P, D139R, A161G, P168T, V172F, G225N/Q, G259D/E, N261D/E and F276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 1, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 1.
  • 3b A mannanase variant comprising two or more amino acid substitutions selected from the group consisting of P019D, F032Y, I072V, K093Q, T131S, A136P, D139R, A161G, P168T, V172F, G225N/Q, G259D/E, N261D/E and F276W, wherein the amino acid positions of the variant are numbered by
  • a mannanase variant comprising two or more amino acid substitutions selected from the group consisting of E019D, F032Y, I072V, K093Q, T131S, A136P, D139R, A161G, P168T, V172F, C225N/Q, G259D/E, R261D/E and F276W, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of SEQ ID NO: 2, and wherein the variant has at least 80% identity to the amino acid sequence of SEQ ID NO: 2. [00243] 4.
  • mannanase variant of embodiment 3b wherein the variant comprises amino acid substitutions selected from the group consisting of E019D-F276W, F032Y-G259D, K093Q-F276W, T131S-F276W, A136P-F276W, D139R-F276W, A161G-F276W, C225N - F276W, C225Q-F276W, G259D-F276W, G259E-F276W, R261D-F276W and R261E-F276W. [00245] 5.
  • amino acid substitutions selected from the group consisting of E019D-A068S-F276W, E019D-T131S- F276W, F032Y-R261D-F276W, F032Y-G259D-F276W, F032Y-T06
  • a mannanase variant comprising amino acid substitutions selected from the group consisting of Y061W-G259D-R261E-F276W, Y061W-T062E-G259D-R261E-F276W, Y061W-V228T-G259D-R261E-F276W, V228T-G259D-R261E-F276W, F032Y-G259D- R261E-F276W, F032Y-Y061W-Y167F-P168S-G259D-R261E-F276W, F032Y-Y061W- G259D-R261E-F276W, F032Y-Y061W-T062E-G259D-R261E-F276W, F032Y-T062E- R261D-F276W, F032Y-T062E- R2
  • mannanase variant according to any preceding embodiment, wherein the variant comprises an amino acid sequence having at least 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% sequence identity to the amino acid sequence of SEQ ID NO: 1.
  • mannanase variant according to embodiments 1-3, wherein said variant is derived from a parent or reference polypeptide with 60%, 65%, 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% amino acid sequence identity to SEQ ID NO: 1.
  • mannanase variant according to any preceding embodiment, wherein said variant is derived from a parent or reference polypeptide with 60%, 65%, 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% amino acid sequence identity to SEQ ID NO: 1 or SEQ ID NO: 2 or SEQ ID NO:3 or SEQ ID NO:4 or SEQ ID NO:5 or SEQ ID NO: 6.
  • I la The mannanase variant according to any preceding embodiment, wherein the mannanase variant has mannanase activity.
  • a polynucleotide comprising a nucleic acid sequence encoding a variant of any one of embodiments 1-3, wherein said polynucleotide is, optionally, isolated.
  • 12a A polynucleotide comprising a nucleic acid sequence encoding a variant according to any preceding embodiment, wherein said polynucleotide is, optionally, isolated.
  • 12b The polynucleotide of embodiment 12 or 12a, wherein the nucleic acid sequence is operably linked to a promoter.
  • a recombinant host cell comprising the polynucleotide of embodiment 12 or
  • An enzyme composition comprising one or more mannanase variant according to embodiments 1-3.
  • a cleaning composition comprising the mannanase variant of any one of embodiments 1-11.
  • the cleaning composition of embodiment 16, further comprising: at least one surfactant; at least one ion selected from calcium and zinc; at least one adjunct ingredient; at least one stabilizer; from about 0.001% to about 1.0 weight% of said mannanase variant of any one of embodiments 1-11; at least one bleaching agent; and/or at least one enzyme or enzyme derivative selected from the group consisting of acyl transferases, amylases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinases, arabinosidases, aryl esterases, betagalactosidases, beta-glucanases, carrageenases, catalases, cellulases, chondroitinases, cutinases, dispersins, DNAses (also known as nucleases or dispersins), endo-glucanases, endo-beta- mannanases, exo-beta-
  • composition contains phosphate or is phosphate-free and/or contains boron or is boron-free.
  • a method of cleaning comprising, contacting a surface or an item in need of cleaning with an effective amount of a mannanase variant of any one of embodiments 1-3 or the enzyme composition of any one of embodiments 13-15; and optionally further comprising the step of rinsing said surface or item after contacting said surface or item with said variant or enzyme composition.
  • a method for producing a mannanase variant of any one of embodiments 1-3 comprising: (a) stably transforming a host cell of embodiment 12c with the expression vector of embodiment 12b; (b) cultivating said transformed host cell under conditions suitable for said host cell to produce said mannanase variant or recombinant polypeptide or active fragment thereof; and (c) recovering said mannanase variant or recombinant polypeptide or active fragment thereof.
  • a food or feed composition and/or food additive comprising the mannanase variant or recombinant polypeptide of any one of embodiments 1-3.
  • a mannanase variant comprising amino acid substitutions selected from the group consisting of X0136P-X019D, X0136P-X0225N, X0136P-X032Y, X0136P-X072V, X0136P-X093Q, X0136P-X131S, X0136P-X139R, X0136P-X161G, X0136P-X168T, X0136P- X172F, X0136P-X225Q, X0136P-X259D, X0136P-X259E, X0136P-X261D, X0136P-X261E, X0136P-X276W, X019D-X0225N, X019D-X032Y, X019D-X072V, X019D-X093Q, X019D- X131S,
  • a mannanase variant comprising amino acid substitutions selected from the group consisting of X0136P-X019D-X0225N, X0136P-X019D-X032Y, X0136P-X019D- X072V, X0136P-X019D-X093Q, X0136P-X019D-X131S, X0136P-X019D-X139R, X0136P- X019D-X161G, X0136P-X019D-X168T, X0136P-X019D-X172F, X0136P-X019D-X225Q, X0136P-X019D-X259D, X0136P-X019D-X259E, X0136P-X019D-X261D, X0136P-X019D-X261E, X0136P-X019D-X
  • a mannanase variant comprising amino acid substitutions selected from the group consisting of X0136P-X019D-X0225N-X032Y, X0136P-X019D-X0225N-X072V, X0136P- X019D-X0225N-X093 Q, X0136P-X019D-X0225N-X131 S, X0136P-X019D-X0225N-X139R, X0136P-X019D-X0225N-X161 G, X0136P-X019D-X0225N-X168T, XO 136P-X019D-X0225N- X172F, , X0136P-X019D-X0225N-X259D, X0136P-X019D-X0225N-X259E, X0136P-X019D- X0225N
  • HPLC detection and quantitation- Protein concentration determination was performed using a high-performance liquid chromatography (HPLC) method measuring integrated peak area.
  • Samples were obtained from filtered culture supernatants and prepared as 3 -fold dilutions in 10 mM HEPES buffer, pH 8.
  • HPLC was carried out on an Agilent 1200 Series HPLC system equipped with a Poroshell 300SB-C8 column (2.1x75 mm) and Poroshell 300SB-C8 guard column (2.1X12.5mm) using a gradient elution composed of water and acetonitrile solvents, each supplemented with 0.1% TFA. Samples were eluted at 65° C, at a flow rate of 0.5 mL/min.
  • Proteins were detected by measuring absorbance at 225 nm, and peaks were integrated using ChemStation OpenLab software (Agilent Technologies). The protein concentration of samples was determined based on a standard curve of a parent protein. [00285] Bradford protein quantitation- Protein concentration measurement was performed using the Bradford assay (Thermo Scientific Coomassie Protein Assay Kit #23200). Samples were obtained from filtered culture supernatants and prepared as 3 -fold dilutions in 10 mM HEPES buffer, pH 8. The protein concentration of samples was determined based on a standard curve of a parent protein. Background protein was subtracted utilizing the Bacillus subtilis host not expressing a recombinant mannanase.
  • the mannanase activity was determined by measuring the hydrolysis of locust bean gum (LBG) galactomannan (Sigma-Aldrich, #GO753) substrate in solution (approximately 0.5% (w/v) LBG substrate).
  • LBG locust bean gum
  • Enzymes were diluted into enzyme dilution buffer (lOOmM HEPES, pH 8, 0.005% TWEEN®80) and aliquots of the diluted enzyme solutions were added to the wells of a microtiter plate (e.g. Corning 3358) containing the LBG substrate solution.
  • the plates were sealed and incubated at 40°C with agitation at 900 rpm for 10 min (e.g. in an iEMS incubator/shaker, Thermo Fisher). After incubation, the released reducing sugars were quantified using the BCA reagent assay (Catalog No. 23225, Thermo Scientific Pierce).
  • the stability of the mannanase variants was tested under the stress condition described in the examples and by measuring the residual mannanase activity of samples after incubation under those conditions.
  • the enzyme samples were diluted in lOOmM HEPES, pH 8, 0.005% TWEEN®80 and added to the detergent condition as described in the Examples followed by immediate storage at -80° C.
  • the enzyme samples were diluted in lOOmM HEPES, pH 8, 0.005% TWEEN®80 and added to the detergent condition and incubated as described in the Examples followed by storage at -80° C.
  • the assay measures the release of LBG from the technical soils containing LBG.
  • the BCA reaction using a commercially available reagent (Catalog No. 23225, Thermo Scientific Pierce) was used to measure reducing ends of oligosaccharides in solution in the presence of enzyme, compared to a blank control. This measurement correlates with the cleaning performance of the enzyme.
  • a commercially available reagent Catalog No. 23225, Thermo Scientific Pierce
  • the performance index (PI) of an enzyme compares the performance of the variant (measured value) with the parent or reference enzyme (theoretical value or measured value) tested at the same protein concentration.
  • Theoretical values for the cleaning performance of the parent or reference enzyme at the relevant protein concentrations were calculated using the parameters extracted from a Langmuir fit of measured values for a standard curve of the parent or reference enzyme.
  • PspManl38 is a variant of PspMan4 with the following mutations: P019E- S030T-T038E-S059V-L060Q-K063R-N067D-N097D-V103I-Y129M-F167Y-Q184L-G225C- T228V-Y235L-K244L-S258D-N261R-ins298Q.
  • Model HDL detergent formulation A described in Example 1 using Stress Condition B (55°C incubation for 20 minutes) or Stress Condition C (55°C incubation for 60 minutes). The residual activity results are reported in Table 5.

Abstract

L'invention concerne un ou plusieurs variants de mannanases, des polynucléotides codant pour les mannanases, des compositions contenant les mannanases, et des procédés d'utilisation de ceux-ci, y compris un ou plusieurs variants de mannanases qui ont une stabilité améliorée par rapport à une ou plusieurs mannanases de référence. Des compositions contenant des mannanases sont appropriées pour être utilisées comme détergents et pour le nettoyage des tissus et surfaces dures, ainsi que dans diverses autres applications industrielles.
PCT/US2023/073055 2022-09-02 2023-08-29 Variants de mannanases et procédés d'utilisation WO2024050339A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US202263374387P 2022-09-02 2022-09-02
US63/374,387 2022-09-02

Publications (1)

Publication Number Publication Date
WO2024050339A1 true WO2024050339A1 (fr) 2024-03-07

Family

ID=88098467

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/US2023/073055 WO2024050339A1 (fr) 2022-09-02 2023-08-29 Variants de mannanases et procédés d'utilisation

Country Status (1)

Country Link
WO (1) WO2024050339A1 (fr)

Citations (227)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB400898A (en) 1932-07-13 1933-11-02 Chem Fab Buckau Process for the production of rubber chloride
GB514276A (en) 1938-04-29 1939-11-03 Betterwear Products Ltd Improvements in or relating to combined combs and brushes
GB1296839A (fr) 1969-05-29 1972-11-22
GB1372034A (en) 1970-12-31 1974-10-30 Unilever Ltd Detergent compositions
EP0011340A1 (fr) 1978-11-20 1980-05-28 THE PROCTER & GAMBLE COMPANY Composition détergente ayant des propriétés adoucissantes sur les textiles
US4246612A (en) 1979-02-28 1981-01-20 Barr & Stroud Limited Optical raster scanning system
EP0026528A1 (fr) 1979-09-29 1981-04-08 THE PROCTER & GAMBLE COMPANY Compositions détergentes
US4430243A (en) 1981-08-08 1984-02-07 The Procter & Gamble Company Bleach catalyst compositions and use thereof in laundry bleaching and detergent compositions
US4435307A (en) 1980-04-30 1984-03-06 Novo Industri A/S Detergent cellulase
EP0214761A2 (fr) 1985-08-07 1987-03-18 Novo Nordisk A/S Additif enzymatique pour détergent, détergent et procédé de lavage
EP0218272A1 (fr) 1985-08-09 1987-04-15 Gist-Brocades N.V. Enzymes lipolytiques et leur usage dans des compositions détergentes
EP0238023A2 (fr) 1986-03-17 1987-09-23 Novo Nordisk A/S Procédé de production de produits protéiniques dans aspergillus oryzae et promoteur à utiliser dans aspergillus
EP0242919A1 (fr) 1986-04-23 1987-10-28 The Procter & Gamble Company Compositions détergentes d'assouplissement contenant un amide comme agent d'assouplissement
EP0258068A2 (fr) 1986-08-29 1988-03-02 Novo Nordisk A/S Additif enzymatique pour détergent
US4765916A (en) 1987-03-24 1988-08-23 The Clorox Company Polymer film composition for rinse release of wash additives
JPS6342988B2 (fr) 1981-09-30 1988-08-26 Nippon Electric Co
WO1988009367A1 (fr) 1987-05-29 1988-12-01 Genencor, Inc. Compositions de nettoyage a base de cutinase
EP0299575A1 (fr) 1987-07-14 1989-01-18 The Procter & Gamble Company Compositions détergentes
EP0305216A1 (fr) 1987-08-28 1989-03-01 Novo Nordisk A/S Lipase recombinante de humicola et procédé de production de lipases recombinantes de humicola
US4810410A (en) 1986-12-13 1989-03-07 Interox Chemicals Limited Bleach activation
JPS6474492A (en) 1987-09-17 1989-03-20 Koito Kogyo Kk Road surface snowfall depth meter
EP0313146A2 (fr) 1987-10-19 1989-04-26 The Procter & Gamble Company Compositions détergentes
WO1989006270A1 (fr) 1988-01-07 1989-07-13 Novo-Nordisk A/S Detergent enzymatique
EP0331376A2 (fr) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. ADN recombinant, bactérie du genre pseudomonas le contenant et son utilisation dans un procédé de production de lipase
WO1990000609A1 (fr) 1988-07-08 1990-01-25 The University Of British Columbia Proteines de fusion se liant a la cellulose
WO1990009446A1 (fr) 1989-02-17 1990-08-23 Plant Genetic Systems N.V. Cutinase
US4972017A (en) 1987-03-24 1990-11-20 The Clorox Company Rinse soluble polymer film composition for wash additives
US4977252A (en) 1988-03-11 1990-12-11 National Starch And Chemical Investment Holding Corporation Modified starch emulsifier characterized by shelf stability
WO1991000353A2 (fr) 1989-06-29 1991-01-10 Gist-Brocades N.V. α-AMYLASES MICROBIENNES MUTANTES PRESENTANT UNE MEILLEURE STABILITE THERMIQUE, AUX ACIDES ET/OU AUX ALCALINS
US5019292A (en) 1987-06-30 1991-05-28 The Procter & Gamble Company Detergent compositions
WO1991016422A1 (fr) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Lipases bacillaires alcalines, sequences d'adn de codage pour celles-ci et bacilles produisant ces lipases
WO1992006154A1 (fr) 1990-09-28 1992-04-16 The Procter & Gamble Company Tensioactifs d'amides de l'acide gras de polyhydroxy destines a ameliorer l'efficacite des enzymes
EP0495257A1 (fr) 1991-01-16 1992-07-22 The Procter & Gamble Company Compositions de détergent compactes contenant de la cellulase de haute activité
WO1992021760A1 (fr) 1991-05-29 1992-12-10 Cognis, Inc. Enzymes proteolytiques mutantes tirees de bacillus
US5227084A (en) 1991-04-17 1993-07-13 Lever Brothers Company, Division Of Conopco, Inc. Concentrated detergent powder compositions
WO1994002597A1 (fr) 1992-07-23 1994-02-03 Novo Nordisk A/S Alpha-amylase mutante, detergent, agent de lavage de vaisselle et de liquefaction
USRE34606E (en) 1984-05-29 1994-05-10 Genencor, Inc. Modified enzymes and methods for making same
WO1994012621A1 (fr) 1992-12-01 1994-06-09 Novo Nordisk Amelioration de reactions enzymatiques
US5354559A (en) 1990-05-29 1994-10-11 Grain Processing Corporation Encapsulation with starch hydrolyzate acid esters
WO1994026859A1 (fr) 1993-05-08 1994-11-24 Henkel Kommanditgesellschaft Auf Aktien Produit i de protection de l'argent contre la corrosion
WO1994026860A1 (fr) 1993-05-08 1994-11-24 Henkel Kommanditgesellschaft Auf Aktien Produits de protection de l'argent contre la corrosion ii
WO1995001426A1 (fr) 1993-06-29 1995-01-12 Novo Nordisk A/S Renforcement de reactions aux laccases
WO1995010603A1 (fr) 1993-10-08 1995-04-20 Novo Nordisk A/S Variants d'amylase
WO1995016782A1 (fr) 1993-12-17 1995-06-22 Genencor International, Inc. Nouvelles enzymes cellulases et systemes pour leur expression
WO1995023221A1 (fr) 1994-02-24 1995-08-31 Cognis, Inc. Enzymes ameliorees et detergents les contenant
WO1995026397A1 (fr) 1994-03-29 1995-10-05 Novo Nordisk A/S Amylase alcaline issue d'un bacille
WO1995035382A2 (fr) 1994-06-17 1995-12-28 Genecor International Inc. NOUVELLES ENZYMES AMYLOLYTIQUES DERIVEES DE B. LICHENIFORMIS α-AMYLASE, POSSEDANT DES CARACTERISTIQUES AMELIOREES
WO1995035362A1 (fr) 1994-06-17 1995-12-28 Genencor International Inc. Compositions de nettoyage contenant des enzymes de degradation de parois cellulaires vegetales et leur utilisation dans des procedes de nettoyage
US5486303A (en) 1993-08-27 1996-01-23 The Procter & Gamble Company Process for making high density detergent agglomerates using an anhydrous powder additive
US5489392A (en) 1994-09-20 1996-02-06 The Procter & Gamble Company Process for making a high density detergent composition in a single mixer/densifier with selected recycle streams for improved agglomerate properties
WO1996005295A2 (fr) 1994-08-11 1996-02-22 Genencor International, Inc. Composition de nettoyage amelioree
US5516448A (en) 1994-09-20 1996-05-14 The Procter & Gamble Company Process for making a high density detergent composition which includes selected recycle streams for improved agglomerate
WO1996023874A1 (fr) 1995-02-03 1996-08-08 Novo Nordisk A/S Technique de mise au point de mutants d'amylase-alpha dotes de proprietes predefinies
WO1996023873A1 (fr) 1995-02-03 1996-08-08 Novo Nordisk A/S Alleles d'amylase-alpha
WO1996030481A1 (fr) 1995-03-24 1996-10-03 Genencor International, Inc. Composition de detergents de lessive amelioree contenant de l'amylase
US5565422A (en) 1995-06-23 1996-10-15 The Procter & Gamble Company Process for preparing a free-flowing particulate detergent composition having improved solubility
US5569645A (en) 1995-04-24 1996-10-29 The Procter & Gamble Company Low dosage detergent composition containing optimum proportions of agglomerates and spray dried granules for improved flow properties
US5574005A (en) 1995-03-07 1996-11-12 The Procter & Gamble Company Process for producing detergent agglomerates from high active surfactant pastes having non-linear viscoelastic properties
US5576282A (en) 1995-09-11 1996-11-19 The Procter & Gamble Company Color-safe bleach boosters, compositions and laundry methods employing same
US5595967A (en) 1995-02-03 1997-01-21 The Procter & Gamble Company Detergent compositions comprising multiperacid-forming bleach activators
US5597936A (en) 1995-06-16 1997-01-28 The Procter & Gamble Company Method for manufacturing cobalt catalysts
WO1997010342A1 (fr) 1995-09-13 1997-03-20 Genencor International, Inc. Micro-organismes alcaliphiles et thermophiles et enzymes obtenues a partir de ceux-ci
WO1997011151A1 (fr) 1995-09-18 1997-03-27 The Procter & Gamble Company Systemes de liberation
US5646101A (en) 1993-01-18 1997-07-08 The Procter & Gamble Company Machine dishwashing detergents containing an oxygen bleach and an anti-tarnishing mixture of a paraffin oil and sequestrant
WO1997041213A1 (fr) 1996-04-30 1997-11-06 Novo Nordisk A/S MUTANTS DUNE AMYLASE-$g(a)
US5686014A (en) 1994-04-07 1997-11-11 The Procter & Gamble Company Bleach compositions comprising manganese-containing bleach catalysts
WO1997043424A1 (fr) 1996-05-14 1997-11-20 Genencor International, Inc. α-AMYLASES MODIFIEES POSSEDANT DES PROPRIETES MODIFIEES DE FIXATION DU CALCIUM
US5691297A (en) 1994-09-20 1997-11-25 The Procter & Gamble Company Process for making a high density detergent composition by controlling agglomeration within a dispersion index
US5695679A (en) 1994-07-07 1997-12-09 The Procter & Gamble Company Detergent compositions containing an organic silver coating agent to minimize silver training in ADW washing methods
US5698504A (en) 1993-07-01 1997-12-16 The Procter & Gamble Company Machine dishwashing composition containing oxygen bleach and paraffin oil and benzotriazole compound silver tarnishing inhibitors
US5700676A (en) 1984-05-29 1997-12-23 Genencor International Inc. Modified subtilisins having amino acid alterations
US5705464A (en) 1995-06-16 1998-01-06 The Procter & Gamble Company Automatic dishwashing compositions comprising cobalt catalysts
US5710115A (en) 1994-12-09 1998-01-20 The Procter & Gamble Company Automatic dishwashing composition containing particles of diacyl peroxides
WO1998013481A1 (fr) 1996-09-26 1998-04-02 Novo Nordisk A/S Enzyme a activite amylase
WO1998026078A1 (fr) 1996-12-09 1998-06-18 Genencor International, Inc. Enzymes alpha-amylase h-mutantes
US5801039A (en) 1994-02-24 1998-09-01 Cognis Gesellschaft Fuer Bio Und Umwelttechnologie Mbh Enzymes for detergents
US5855625A (en) 1995-01-17 1999-01-05 Henkel Kommanditgesellschaft Auf Aktien Detergent compositions
WO1999002702A1 (fr) 1997-07-11 1999-01-21 Genencor International, Inc. α-AMYLASE MUTANTE COMPORTANT UNE LIAISON DISULFURE
WO1999006521A1 (fr) 1997-08-02 1999-02-11 The Procter & Gamble Company Pastille detergente
WO1999009183A1 (fr) 1997-08-19 1999-02-25 Genencor International, Inc. ALPHA-AMYLASE MUTANTE COMPRENANT UNE MODIFICATION AU NIVEAU DES RESIDUS CORRESPONDANT A A210, H405 ET/OU T412 CHEZ LES $i(BACILLUS LICHENIFORMIS)
US5879584A (en) 1994-09-10 1999-03-09 The Procter & Gamble Company Process for manufacturing aqueous compositions comprising peracids
WO1999014342A1 (fr) 1997-09-15 1999-03-25 Genencor International, Inc. Proteases d'organismes gram positifs
WO1999014341A2 (fr) 1997-09-15 1999-03-25 Genencor International, Inc. Proteases extraites d'organismes gram positif
WO1999019467A1 (fr) 1997-10-13 1999-04-22 Novo Nordisk A/S MUTANTS D'α-AMYLASE
WO1999023211A1 (fr) 1997-10-30 1999-05-14 Novo Nordisk A/S Mutants d'alpha-amylase
EP0922499A2 (fr) 1993-12-15 1999-06-16 Ing. Erich Pfeiffer GmbH Distributeur de fluides
WO1999029876A2 (fr) 1997-12-09 1999-06-17 Genencor International, Inc. Alpha-amylases mutantes de bacillus licheniformis
WO1999034003A2 (fr) 1997-12-30 1999-07-08 Genencor International, Inc. Proteases provenant d'organismes a gram positif
WO1999034011A2 (fr) 1997-12-24 1999-07-08 Genencor International, Inc. Methode amelioree pour tester une enzyme preferee et/ou une composition detergente preferee
WO1999033960A2 (fr) 1997-12-30 1999-07-08 Genencor International, Inc. Proteases de germes gram positifs
US5935826A (en) 1997-10-31 1999-08-10 National Starch And Chemical Investment Holding Corporation Glucoamylase converted starch derivatives and their use as emulsifying and encapsulating agents
WO1999042567A1 (fr) 1998-02-18 1999-08-26 Novo Nordisk A/S Amylase bacillaire alcaline
WO1999043794A1 (fr) 1998-02-27 1999-09-02 Novo Nordisk A/S Variantes d'alpha-amylase maltogene
WO1999043793A1 (fr) 1998-02-27 1999-09-02 Novo Nordisk A/S Variantes d'enzymes amylolytiques
WO1999046399A1 (fr) 1998-03-09 1999-09-16 Novo Nordisk A/S Preparation enzymatique de sirop de glucose a partir d'amidon
US5955340A (en) 1984-05-29 1999-09-21 Genencor International, Inc. Modified subtilisins having amino acid alterations
WO1999064573A1 (fr) 1998-06-10 1999-12-16 Novozymes A/S Nouvelles mannanases
WO1999064619A2 (fr) 1998-06-10 1999-12-16 Novozymes A/S Nouvelles mannanases
WO2000029560A1 (fr) 1998-11-16 2000-05-25 Novozymes A/S VARIANTES DE α-AMYLASE
WO2000032601A2 (fr) 1998-11-30 2000-06-08 The Procter & Gamble Company Procede de preparation de tetraaza macrocycles pontes transversalement
WO2000060058A2 (fr) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides possedant une activite alcaline alpha-amylase et acides nucleiques codant pour ces polypeptides
WO2000060060A2 (fr) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides presentant une activite alcaline alpha-amylase et acides nucleiques les codant
WO2000060059A2 (fr) 1999-03-30 2000-10-12 NovozymesA/S Variantes d'alpha amylase
WO2001014532A2 (fr) 1999-08-20 2001-03-01 Novozymes A/S Amylase alcaline de bacillus
US6225464B1 (en) 1997-03-07 2001-05-01 The Procter & Gamble Company Methods of making cross-bridged macropolycycles
WO2001034784A1 (fr) 1999-11-10 2001-05-17 Novozymes A/S Variants alpha-amylase du type fungamyle
WO2001064852A1 (fr) 2000-03-03 2001-09-07 Novozymes A/S Polypeptides possedant une activite de l'alpha-amylase et acides nucleiques codant pour ces polypeptides
WO2001066712A2 (fr) 2000-03-08 2001-09-13 Novozymes A/S Variants possedant des proprietes modifiees
US6312936B1 (en) 1997-10-23 2001-11-06 Genencor International, Inc. Multiply-substituted protease variants
WO2001088107A2 (fr) 2000-05-12 2001-11-22 Novozymes A/S Variantes d'alpha-amylase avec une activite 1,6 alteree
WO2001096537A2 (fr) 2000-06-14 2001-12-20 Novozymes A/S Alpha-amylase pre-oxydee
WO2002010355A2 (fr) 2000-08-01 2002-02-07 Novozymes A/S Mutants d'alpha-amylase a proprietes modifiees
WO2002031124A2 (fr) 2000-10-13 2002-04-18 Novozymes A/S Variant de l'alpha-amylase possedant des proprietes modifiees
US6376445B1 (en) 1997-08-14 2002-04-23 Procter & Gamble Company Detergent compositions comprising a mannanase and a protease
US6376450B1 (en) 1998-10-23 2002-04-23 Chanchal Kumar Ghosh Cleaning compositions containing multiply-substituted protease variants
WO2002092797A2 (fr) 2001-05-15 2002-11-21 Novozymes A/S Variant d'alpha-amylases ayant des proprietes modifiees
WO2002102955A1 (fr) 2001-06-18 2002-12-27 Unilever Plc Conditionnement soluble dans l'eau et liquides contenus dans ce conditionnement
US6605458B1 (en) 1997-11-21 2003-08-12 Novozymes A/S Protease variants and compositions
WO2004055178A1 (fr) 2002-12-17 2004-07-01 Novozymes A/S Alpha-amylases thermostables
WO2004111178A1 (fr) 2003-05-23 2004-12-23 The Procter & Gamble Company Composition de nettoyage destinee a etre utilisee dans un lave-linge ou un lave-vaisselle
WO2004113551A1 (fr) 2003-06-25 2004-12-29 Novozymes A/S Procede d'hydrolyse de l'amidon
WO2005001064A2 (fr) 2003-06-25 2005-01-06 Novozymes A/S Polypeptides a activite alpha-amylase et polynucleotides codant pour ceux-ci
WO2005003311A2 (fr) 2003-06-25 2005-01-13 Novozymes A/S Enzymes de traitement d'amidon
WO2005018336A1 (fr) 2003-08-22 2005-03-03 Novozymes A/S Processus de preparation d'une pate contenant une exo-amylase glucogenique de degradation de l'amidon de famille 13
WO2005019443A2 (fr) 2003-08-22 2005-03-03 Novozymes A/S Variants d'alpha-amylases fongiques
WO2005054475A1 (fr) 2003-12-03 2005-06-16 Meiji Seika Kaisha, Ltd. Stce d'endoglucanase et preparation de cellulase le contenant
WO2005056787A1 (fr) 2003-12-08 2005-06-23 Meiji Seika Kaisha, Ltd. Cellulase supportant les tensioactifs et procede de transformation associe
WO2005056782A2 (fr) 2003-12-03 2005-06-23 Genencor International, Inc. Perhydrolase
WO2005066338A1 (fr) 2004-01-08 2005-07-21 Novozymes A/S Amylase
WO2006002643A2 (fr) 2004-07-05 2006-01-12 Novozymes A/S Variants d'alpha-amylases presentant des proprietes modifiees
WO2006012902A2 (fr) 2004-08-02 2006-02-09 Novozymes A/S Creation de diversite dans des polypeptides
WO2006012899A1 (fr) 2004-08-02 2006-02-09 Novozymes A/S Variants d'alpha-amylase maltogene
WO2006031554A2 (fr) 2004-09-10 2006-03-23 Novozymes North America, Inc. Procedes permettant de detruire, de reduire, d'eliminer ou d'empecher la formation d'un film biologique
WO2006063594A1 (fr) 2004-12-15 2006-06-22 Novozymes A/S Amylase de bacille alcaline
WO2006066594A2 (fr) 2004-12-23 2006-06-29 Novozymes A/S Variantes de l'alpha-amylase
WO2006066596A2 (fr) 2004-12-22 2006-06-29 Novozymes A/S Enzymes hybrides
WO2006136161A2 (fr) 2005-06-24 2006-12-28 Novozymes A/S Amylases a usage pharmaceutique
WO2007044993A2 (fr) 2005-10-12 2007-04-19 Genencor International, Inc. Utilisation et production d'une metalloprotease neutre stable au stockage
WO2007145964A2 (fr) 2006-06-05 2007-12-21 The Procter & Gamble Company Stabilisateur d'enzymes
WO2008000825A1 (fr) 2006-06-30 2008-01-03 Novozymes A/S Variantes d'alpha-amylases bactériennes
WO2008010925A2 (fr) 2006-07-18 2008-01-24 Danisco Us, Inc., Genencor Division Variantes de protéases actives sur une large plage de températures
WO2008088493A2 (fr) 2006-12-21 2008-07-24 Danisco Us, Inc., Genencor Division Compositions et utilisations pour un polypeptide alpha-amylase de l'espèce de bacille 195
WO2008092919A1 (fr) 2007-02-01 2008-08-07 Novozymes A/S Alpha-amylase et son utilisation
WO2008101894A1 (fr) 2007-02-19 2008-08-28 Novozymes A/S Polypeptides possédant une activité débranchante de l'amidon
WO2008112459A2 (fr) 2007-03-09 2008-09-18 Danisco Us Inc., Genencor Division Variants de l'α-amylase d'une espèce de bacillus alcaliphile, compositions comprenant des variants de l'α-amylase, et procédés d'utilisation
US7449318B2 (en) 2003-04-30 2008-11-11 Danisco A/S, Genencor Division Bacillus mHKcel cellulase
WO2009058661A1 (fr) 2007-10-31 2009-05-07 Danisco Us Inc., Genencor Division Utilisation et production de métalloprotéases neutres stables vis-à-vis des citrates
WO2009058303A2 (fr) 2007-11-01 2009-05-07 Danisco Us Inc., Genencor Division Production de thermolysine et de ses variants et utilisation dans des détergents liquides
WO2009061380A2 (fr) 2007-11-05 2009-05-14 Danisco Us Inc., Genencor Division Variants de bacillus sp. ts-23 alpha-amylase à propriétés modifiées
WO2009061381A2 (fr) 2007-11-05 2009-05-14 Danisco Us Inc., Genencor Division Variants d'alpha-amylase à propriétés modifiées
WO2009100102A2 (fr) 2008-02-04 2009-08-13 Danisco Us Inc., Genencor Division Variants ts23 de l’alpha-amylase à propriétés modifiées
EP2100947A1 (fr) 2008-03-14 2009-09-16 The Procter and Gamble Company Composition détergente de lave-vaisselle automatique
WO2009140504A1 (fr) 2008-05-16 2009-11-19 Novozymes A/S Polypeptides présentant une activité alpha-amylase et polynucléotides codant pour ces polypeptides
WO2009149200A2 (fr) 2008-06-06 2009-12-10 Danisco Us Inc. Compositions et procédés comprenant des protéases microbiennes variantes
WO2009149419A2 (fr) 2008-06-06 2009-12-10 Danisco Us Inc. Alpha amylases variantes de bacillus subtilis et leurs procédés d’utilisation
WO2010044786A1 (fr) 2008-10-15 2010-04-22 Danisco Us Inc., Genencor Division Variant modifié d’inhibiteurs de la protéase bowman-birk
WO2010056640A2 (fr) 2008-11-11 2010-05-20 Danisco Us Inc. Compositions et méthodes comportant des variantes de protéase à serine
WO2010056653A2 (fr) 2008-11-11 2010-05-20 Danisco Us Inc. Protéases comprenant une ou plusieurs mutations combinables
WO2010059413A2 (fr) 2008-11-20 2010-05-27 Novozymes, Inc. Polypeptides ayant une activité amylolytique renforcée et polynucléotides codant pour ceux-ci
WO2010088447A1 (fr) 2009-01-30 2010-08-05 Novozymes A/S Polypeptides ayant une activité alpha-amylase et polynucléotides codant pour ceux-ci
WO2010091221A1 (fr) 2009-02-06 2010-08-12 Novozymes A/S Polypeptides ayant une activité alpha-amylase et polynucléotides codant pour ceux-ci
WO2010104675A1 (fr) 2009-03-10 2010-09-16 Danisco Us Inc. Alpha-amylases associées à la souche bacillus megaterium dsm90, et leurs procédés d'utilisation
WO2010115028A2 (fr) 2009-04-01 2010-10-07 Danisco Us Inc. Système de lavage comprenant une alpha-amylase et une protéase
WO2010117511A1 (fr) 2009-04-08 2010-10-14 Danisco Us Inc. Alpha-amylases liées à la souche halomonas wdg195 et procédés d'utilisation
WO2011013022A1 (fr) 2009-07-28 2011-02-03 Koninklijke Philips Electronics N.V. Unité de lavage et de stérilisation
WO2011072099A2 (fr) 2009-12-09 2011-06-16 Danisco Us Inc. Compositions et procédés comprenant des variants de protéase
WO2011076897A1 (fr) 2009-12-22 2011-06-30 Novozymes A/S Utilisation de variants d'amylase à basse température
WO2011076123A1 (fr) 2009-12-22 2011-06-30 Novozymes A/S Compositions comprenant un polypeptide renforçateur et un enzyme dégradant l'amidon, et utilisations correspondantes
WO2011080354A1 (fr) 2010-01-04 2011-07-07 Novozymes A/S Alpha-amylases
WO2011098531A1 (fr) 2010-02-10 2011-08-18 Novozymes A/S Variants et compositions contenant des variants à stabilité élevée en présence d'un agent chélateur
WO2011140364A1 (fr) 2010-05-06 2011-11-10 Danisco Us Inc. Compositions et procédés comprenant des variants de la subtilisine
WO2012112718A1 (fr) 2011-02-15 2012-08-23 Novozymes Biologicals, Inc. Réduction des odeurs dans les machines de nettoyage et les procédés de nettoyage
WO2012151534A1 (fr) 2011-05-05 2012-11-08 Danisco Us Inc. Procédés et compositions comprenant des variants de la sérine protéase
WO2013063460A2 (fr) 2011-10-28 2013-05-02 Danisco Us Inc. Variants d'alpha-amylase pour obtention de maltohexaose variant
WO2013087286A1 (fr) 2011-12-12 2013-06-20 Unilever Plc Compositions pour lessiver
US8530219B2 (en) 2008-11-11 2013-09-10 Danisco Us Inc. Compositions and methods comprising a subtilisin variant
WO2013165725A1 (fr) 2012-04-30 2013-11-07 Danisco Us Inc. Systèmes de perhydrolase à format de dosage unitaire
WO2013184577A1 (fr) 2012-06-08 2013-12-12 Danisco Us Inc. Variants d'alpha-amylase dérivés de l'alpha-amylase de cytophaga sp. amylase/ (cspamy2)
WO2014059360A1 (fr) 2012-10-12 2014-04-17 Danisco Us Inc. Compositions comprenant un variant d'enzyme lipolytique et procédés associés
WO2014071410A1 (fr) 2012-11-05 2014-05-08 Danisco Us Inc. Compositions et procédés comportant des variants de thermolysine protéase
WO2014099523A1 (fr) 2012-12-21 2014-06-26 Danisco Us Inc. Variants d'alpha-amylase
WO2014164777A1 (fr) 2013-03-11 2014-10-09 Danisco Us Inc. Variantes combinatoires d'alpha-amylases
WO2014194054A1 (fr) 2013-05-29 2014-12-04 Danisco Us Inc. Métalloprotéases inédites
WO2014194034A2 (fr) 2013-05-29 2014-12-04 Danisco Us Inc. Métalloprotéases inédites
WO2014194117A2 (fr) 2013-05-29 2014-12-04 Danisco Us Inc. Métalloprotéases inédites
WO2014194032A1 (fr) 2013-05-29 2014-12-04 Danisco Us Inc. Métalloprotéases inédites
WO2015010009A2 (fr) 2013-07-19 2015-01-22 Danisco Us Inc. Compositions et méthodes comprenant un variant d'enzyme lipolytique
WO2015022428A1 (fr) 2013-08-15 2015-02-19 Novozymes A/S Procédé de production d'un extrait de café à l'aide d'enzymes ayant une activité bêta-1,3-galactanase
WO2015038792A1 (fr) 2013-09-12 2015-03-19 Danisco Us Inc. Compositions et procédés comprenant des variants de protéase lg12-clade
WO2015077126A1 (fr) 2013-11-20 2015-05-28 Danisco Us Inc. Variants d'alpha-amylases ayant une sensibilité réduite au clivage protéasique, et leurs procédés d'utilisation
WO2015089441A1 (fr) 2013-12-13 2015-06-18 Danisco Us Inc. Sérine protéases d'espèce de bacillus
WO2015089447A1 (fr) 2013-12-13 2015-06-18 Danisco Us Inc. Sérines protéases du clade du bacillus gibsonii
WO2015143360A2 (fr) 2014-03-21 2015-09-24 Danisco Us Inc. Sérine-protéases de l'espèce bacillus
US9181296B2 (en) 2008-03-26 2015-11-10 Novozymes A/S Stabilized liquid enzyme compositions
WO2016061438A1 (fr) 2014-10-17 2016-04-21 Danisco Us Inc. Sérines protéases de l'espèce bacillus
WO2016069552A1 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérines protéases
WO2016069563A1 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérine protéases
WO2016069548A2 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérine-protéases
WO2016069544A1 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérines protéases
WO2016069569A2 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérine protéases
WO2016069557A1 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérine-protéases de l'espèce bacillus
WO2016145428A1 (fr) 2015-03-12 2016-09-15 Danisco Us Inc Compositions et procédés comprenant des variants de protéase lg12-clade
WO2017054983A1 (fr) 2015-10-01 2017-04-06 Unilever Plc Composition de détergent à lessive liquide
WO2017079751A1 (fr) * 2015-11-05 2017-05-11 Danisco Us Inc Mannanases de paenibacillus sp.
WO2019032257A1 (fr) 2017-08-11 2019-02-14 The Procter & Gamble Company Article formant dose unitaire soluble dans l'eau, comprenant un polymère greffé amphiphile et un polyester téréphtalate
WO2019185726A1 (fr) * 2018-03-29 2019-10-03 Novozymes A/S Variants de mannanase et polynucléotides codant pour ceux-ci
US10683474B2 (en) 2015-06-05 2020-06-16 The Procter & Gamble Company Compacted liquid laundry detergent composition
WO2020223959A1 (fr) 2019-05-09 2020-11-12 The Procter & Gamble Company Composition de détergent à lessive liquide anti-acarien stable comprenant du benzoate de benzyle
WO2020264077A1 (fr) 2019-06-28 2020-12-30 The Procter & Gamble Company Composition nettoyante
WO2021041685A1 (fr) 2019-08-28 2021-03-04 Henkel IP & Holding GmbH Compositions détergentes contenant du polyéthylène glycol et un acide organique
WO2021037895A1 (fr) 2019-08-27 2021-03-04 Novozymes A/S Composition détergente
WO2021108307A1 (fr) 2019-11-27 2021-06-03 The Procter & Gamble Company Tensioactifs alkylbenzènesulfonate améliorés
WO2021123184A2 (fr) 2019-12-19 2021-06-24 Novozymes A/S Variants d'alpha-amylase
WO2021127662A1 (fr) 2019-12-19 2021-06-24 Henkel IP & Holding GmbH Détergents de faible densité en dose unitaire avec parfum encapsulé
US11046919B2 (en) 2018-06-26 2021-06-29 The Procter & Gamble Company Liquid laundry detergent composition
US20210317387A1 (en) 2020-04-06 2021-10-14 Henkel Ag & Co. Kgaa Cleaning compositions comprising dispersin variants
WO2021219296A1 (fr) 2020-04-29 2021-11-04 Henkel Ag & Co. Kgaa Détergent pour textiles fortement alcalin contenant une protéase
WO2021223552A1 (fr) 2020-05-08 2021-11-11 The Procter & Gamble Company Composition de détergent à lessive liquide
WO2021247801A1 (fr) 2020-06-05 2021-12-09 The Procter & Gamble Company Compositions détergentes contenant un tensioactif ramifié
US11208619B2 (en) 2019-08-22 2021-12-28 Henkel IP & Holding GmbH Unit dose detergent products with effect on protein stains
WO2022010372A1 (fr) 2020-07-10 2022-01-13 Institut Biosens-Istrazivacko Razvojni Institut Za Informacione Tehnologije Biosistema Système et procédé de prélèvement intelligent d'échantillons de sol
WO2022074037A2 (fr) 2020-10-07 2022-04-14 Novozymes A/S Variants d'alpha-amylase
US20220162523A1 (en) 2020-11-20 2022-05-26 The Procter & Gamble Company Water-soluble unit dose article comprising a fatty alkyl ester alkoxylate non-ionic surfactant and an alkoxylated alcohol non-ionic surfactant
WO2022106404A1 (fr) 2020-11-18 2022-05-27 Novozymes A/S Combinaison de protéases
US20220186144A1 (en) 2020-12-15 2022-06-16 Henkel IP & Holding GmbH Unit Dose Laundry Detergent Compositions Containing Soil Release Polymers
WO2022157311A1 (fr) 2021-01-22 2022-07-28 Novozymes A/S Composition d'enzyme liquide avec piégeur de sulfite
WO2022167251A1 (fr) 2021-02-04 2022-08-11 Henkel Ag & Co. Kgaa Composition détergente comprenant des variants de xanthane lyase et d'endoglucanase ayant une stabilité améliorée

Patent Citations (245)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB400898A (en) 1932-07-13 1933-11-02 Chem Fab Buckau Process for the production of rubber chloride
GB514276A (en) 1938-04-29 1939-11-03 Betterwear Products Ltd Improvements in or relating to combined combs and brushes
GB1296839A (fr) 1969-05-29 1972-11-22
GB1372034A (en) 1970-12-31 1974-10-30 Unilever Ltd Detergent compositions
EP0011340A1 (fr) 1978-11-20 1980-05-28 THE PROCTER & GAMBLE COMPANY Composition détergente ayant des propriétés adoucissantes sur les textiles
US4246612A (en) 1979-02-28 1981-01-20 Barr & Stroud Limited Optical raster scanning system
EP0026528A1 (fr) 1979-09-29 1981-04-08 THE PROCTER & GAMBLE COMPANY Compositions détergentes
US4435307A (en) 1980-04-30 1984-03-06 Novo Industri A/S Detergent cellulase
US4430243A (en) 1981-08-08 1984-02-07 The Procter & Gamble Company Bleach catalyst compositions and use thereof in laundry bleaching and detergent compositions
JPS6342988B2 (fr) 1981-09-30 1988-08-26 Nippon Electric Co
USRE34606E (en) 1984-05-29 1994-05-10 Genencor, Inc. Modified enzymes and methods for making same
US5955340A (en) 1984-05-29 1999-09-21 Genencor International, Inc. Modified subtilisins having amino acid alterations
US5700676A (en) 1984-05-29 1997-12-23 Genencor International Inc. Modified subtilisins having amino acid alterations
EP0214761A2 (fr) 1985-08-07 1987-03-18 Novo Nordisk A/S Additif enzymatique pour détergent, détergent et procédé de lavage
EP0218272A1 (fr) 1985-08-09 1987-04-15 Gist-Brocades N.V. Enzymes lipolytiques et leur usage dans des compositions détergentes
EP0238023A2 (fr) 1986-03-17 1987-09-23 Novo Nordisk A/S Procédé de production de produits protéiniques dans aspergillus oryzae et promoteur à utiliser dans aspergillus
EP0242919A1 (fr) 1986-04-23 1987-10-28 The Procter & Gamble Company Compositions détergentes d'assouplissement contenant un amide comme agent d'assouplissement
EP0258068A2 (fr) 1986-08-29 1988-03-02 Novo Nordisk A/S Additif enzymatique pour détergent
US4810410A (en) 1986-12-13 1989-03-07 Interox Chemicals Limited Bleach activation
US4765916A (en) 1987-03-24 1988-08-23 The Clorox Company Polymer film composition for rinse release of wash additives
US4972017A (en) 1987-03-24 1990-11-20 The Clorox Company Rinse soluble polymer film composition for wash additives
WO1988009367A1 (fr) 1987-05-29 1988-12-01 Genencor, Inc. Compositions de nettoyage a base de cutinase
US5019292A (en) 1987-06-30 1991-05-28 The Procter & Gamble Company Detergent compositions
EP0299575A1 (fr) 1987-07-14 1989-01-18 The Procter & Gamble Company Compositions détergentes
EP0305216A1 (fr) 1987-08-28 1989-03-01 Novo Nordisk A/S Lipase recombinante de humicola et procédé de production de lipases recombinantes de humicola
JPS6474492A (en) 1987-09-17 1989-03-20 Koito Kogyo Kk Road surface snowfall depth meter
EP0313146A2 (fr) 1987-10-19 1989-04-26 The Procter & Gamble Company Compositions détergentes
WO1989006270A1 (fr) 1988-01-07 1989-07-13 Novo-Nordisk A/S Detergent enzymatique
EP0331376A2 (fr) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. ADN recombinant, bactérie du genre pseudomonas le contenant et son utilisation dans un procédé de production de lipase
US4977252A (en) 1988-03-11 1990-12-11 National Starch And Chemical Investment Holding Corporation Modified starch emulsifier characterized by shelf stability
WO1990000609A1 (fr) 1988-07-08 1990-01-25 The University Of British Columbia Proteines de fusion se liant a la cellulose
WO1990009446A1 (fr) 1989-02-17 1990-08-23 Plant Genetic Systems N.V. Cutinase
WO1991000353A2 (fr) 1989-06-29 1991-01-10 Gist-Brocades N.V. α-AMYLASES MICROBIENNES MUTANTES PRESENTANT UNE MEILLEURE STABILITE THERMIQUE, AUX ACIDES ET/OU AUX ALCALINS
WO1991016422A1 (fr) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Lipases bacillaires alcalines, sequences d'adn de codage pour celles-ci et bacilles produisant ces lipases
US5354559A (en) 1990-05-29 1994-10-11 Grain Processing Corporation Encapsulation with starch hydrolyzate acid esters
WO1992006154A1 (fr) 1990-09-28 1992-04-16 The Procter & Gamble Company Tensioactifs d'amides de l'acide gras de polyhydroxy destines a ameliorer l'efficacite des enzymes
EP0495257A1 (fr) 1991-01-16 1992-07-22 The Procter & Gamble Company Compositions de détergent compactes contenant de la cellulase de haute activité
US5227084A (en) 1991-04-17 1993-07-13 Lever Brothers Company, Division Of Conopco, Inc. Concentrated detergent powder compositions
WO1992021760A1 (fr) 1991-05-29 1992-12-10 Cognis, Inc. Enzymes proteolytiques mutantes tirees de bacillus
US5340735A (en) 1991-05-29 1994-08-23 Cognis, Inc. Bacillus lentus alkaline protease variants with increased stability
US5500364A (en) 1991-05-29 1996-03-19 Cognis, Inc. Bacillus lentus alkaline protease varints with enhanced stability
WO1994002597A1 (fr) 1992-07-23 1994-02-03 Novo Nordisk A/S Alpha-amylase mutante, detergent, agent de lavage de vaisselle et de liquefaction
WO1994012621A1 (fr) 1992-12-01 1994-06-09 Novo Nordisk Amelioration de reactions enzymatiques
US5646101A (en) 1993-01-18 1997-07-08 The Procter & Gamble Company Machine dishwashing detergents containing an oxygen bleach and an anti-tarnishing mixture of a paraffin oil and sequestrant
WO1994026859A1 (fr) 1993-05-08 1994-11-24 Henkel Kommanditgesellschaft Auf Aktien Produit i de protection de l'argent contre la corrosion
WO1994026860A1 (fr) 1993-05-08 1994-11-24 Henkel Kommanditgesellschaft Auf Aktien Produits de protection de l'argent contre la corrosion ii
WO1995001426A1 (fr) 1993-06-29 1995-01-12 Novo Nordisk A/S Renforcement de reactions aux laccases
US5698504A (en) 1993-07-01 1997-12-16 The Procter & Gamble Company Machine dishwashing composition containing oxygen bleach and paraffin oil and benzotriazole compound silver tarnishing inhibitors
US5486303A (en) 1993-08-27 1996-01-23 The Procter & Gamble Company Process for making high density detergent agglomerates using an anhydrous powder additive
WO1995010603A1 (fr) 1993-10-08 1995-04-20 Novo Nordisk A/S Variants d'amylase
EP0922499A2 (fr) 1993-12-15 1999-06-16 Ing. Erich Pfeiffer GmbH Distributeur de fluides
WO1995016782A1 (fr) 1993-12-17 1995-06-22 Genencor International, Inc. Nouvelles enzymes cellulases et systemes pour leur expression
US5874276A (en) 1993-12-17 1999-02-23 Genencor International, Inc. Cellulase enzymes and systems for their expressions
WO1995023221A1 (fr) 1994-02-24 1995-08-31 Cognis, Inc. Enzymes ameliorees et detergents les contenant
US5801039A (en) 1994-02-24 1998-09-01 Cognis Gesellschaft Fuer Bio Und Umwelttechnologie Mbh Enzymes for detergents
WO1995026397A1 (fr) 1994-03-29 1995-10-05 Novo Nordisk A/S Amylase alcaline issue d'un bacille
US5686014A (en) 1994-04-07 1997-11-11 The Procter & Gamble Company Bleach compositions comprising manganese-containing bleach catalysts
WO1995035382A2 (fr) 1994-06-17 1995-12-28 Genecor International Inc. NOUVELLES ENZYMES AMYLOLYTIQUES DERIVEES DE B. LICHENIFORMIS α-AMYLASE, POSSEDANT DES CARACTERISTIQUES AMELIOREES
US6602842B2 (en) 1994-06-17 2003-08-05 Genencor International, Inc. Cleaning compositions containing plant cell wall degrading enzymes and their use in cleaning methods
WO1995035362A1 (fr) 1994-06-17 1995-12-28 Genencor International Inc. Compositions de nettoyage contenant des enzymes de degradation de parois cellulaires vegetales et leur utilisation dans des procedes de nettoyage
US5695679A (en) 1994-07-07 1997-12-09 The Procter & Gamble Company Detergent compositions containing an organic silver coating agent to minimize silver training in ADW washing methods
WO1996005295A2 (fr) 1994-08-11 1996-02-22 Genencor International, Inc. Composition de nettoyage amelioree
US5879584A (en) 1994-09-10 1999-03-09 The Procter & Gamble Company Process for manufacturing aqueous compositions comprising peracids
US5489392A (en) 1994-09-20 1996-02-06 The Procter & Gamble Company Process for making a high density detergent composition in a single mixer/densifier with selected recycle streams for improved agglomerate properties
US5516448A (en) 1994-09-20 1996-05-14 The Procter & Gamble Company Process for making a high density detergent composition which includes selected recycle streams for improved agglomerate
US5691297A (en) 1994-09-20 1997-11-25 The Procter & Gamble Company Process for making a high density detergent composition by controlling agglomeration within a dispersion index
US5710115A (en) 1994-12-09 1998-01-20 The Procter & Gamble Company Automatic dishwashing composition containing particles of diacyl peroxides
US5855625A (en) 1995-01-17 1999-01-05 Henkel Kommanditgesellschaft Auf Aktien Detergent compositions
US5595967A (en) 1995-02-03 1997-01-21 The Procter & Gamble Company Detergent compositions comprising multiperacid-forming bleach activators
WO1996023874A1 (fr) 1995-02-03 1996-08-08 Novo Nordisk A/S Technique de mise au point de mutants d'amylase-alpha dotes de proprietes predefinies
WO1996023873A1 (fr) 1995-02-03 1996-08-08 Novo Nordisk A/S Alleles d'amylase-alpha
US5574005A (en) 1995-03-07 1996-11-12 The Procter & Gamble Company Process for producing detergent agglomerates from high active surfactant pastes having non-linear viscoelastic properties
WO1996030481A1 (fr) 1995-03-24 1996-10-03 Genencor International, Inc. Composition de detergents de lessive amelioree contenant de l'amylase
US5569645A (en) 1995-04-24 1996-10-29 The Procter & Gamble Company Low dosage detergent composition containing optimum proportions of agglomerates and spray dried granules for improved flow properties
US5705464A (en) 1995-06-16 1998-01-06 The Procter & Gamble Company Automatic dishwashing compositions comprising cobalt catalysts
US5597936A (en) 1995-06-16 1997-01-28 The Procter & Gamble Company Method for manufacturing cobalt catalysts
US5565422A (en) 1995-06-23 1996-10-15 The Procter & Gamble Company Process for preparing a free-flowing particulate detergent composition having improved solubility
US5576282A (en) 1995-09-11 1996-11-19 The Procter & Gamble Company Color-safe bleach boosters, compositions and laundry methods employing same
WO1997010342A1 (fr) 1995-09-13 1997-03-20 Genencor International, Inc. Micro-organismes alcaliphiles et thermophiles et enzymes obtenues a partir de ceux-ci
WO1997011151A1 (fr) 1995-09-18 1997-03-27 The Procter & Gamble Company Systemes de liberation
WO1997041213A1 (fr) 1996-04-30 1997-11-06 Novo Nordisk A/S MUTANTS DUNE AMYLASE-$g(a)
WO1997043424A1 (fr) 1996-05-14 1997-11-20 Genencor International, Inc. α-AMYLASES MODIFIEES POSSEDANT DES PROPRIETES MODIFIEES DE FIXATION DU CALCIUM
WO1998013481A1 (fr) 1996-09-26 1998-04-02 Novo Nordisk A/S Enzyme a activite amylase
WO1998026078A1 (fr) 1996-12-09 1998-06-18 Genencor International, Inc. Enzymes alpha-amylase h-mutantes
US6225464B1 (en) 1997-03-07 2001-05-01 The Procter & Gamble Company Methods of making cross-bridged macropolycycles
WO1999002702A1 (fr) 1997-07-11 1999-01-21 Genencor International, Inc. α-AMYLASE MUTANTE COMPORTANT UNE LIAISON DISULFURE
WO1999006521A1 (fr) 1997-08-02 1999-02-11 The Procter & Gamble Company Pastille detergente
US6376445B1 (en) 1997-08-14 2002-04-23 Procter & Gamble Company Detergent compositions comprising a mannanase and a protease
WO1999009183A1 (fr) 1997-08-19 1999-02-25 Genencor International, Inc. ALPHA-AMYLASE MUTANTE COMPRENANT UNE MODIFICATION AU NIVEAU DES RESIDUS CORRESPONDANT A A210, H405 ET/OU T412 CHEZ LES $i(BACILLUS LICHENIFORMIS)
WO1999014342A1 (fr) 1997-09-15 1999-03-25 Genencor International, Inc. Proteases d'organismes gram positifs
WO1999014341A2 (fr) 1997-09-15 1999-03-25 Genencor International, Inc. Proteases extraites d'organismes gram positif
WO1999019467A1 (fr) 1997-10-13 1999-04-22 Novo Nordisk A/S MUTANTS D'α-AMYLASE
US6312936B1 (en) 1997-10-23 2001-11-06 Genencor International, Inc. Multiply-substituted protease variants
US6482628B1 (en) 1997-10-23 2002-11-19 Genencor International, Inc. Multiply-substituted protease variants
WO1999023211A1 (fr) 1997-10-30 1999-05-14 Novo Nordisk A/S Mutants d'alpha-amylase
US5935826A (en) 1997-10-31 1999-08-10 National Starch And Chemical Investment Holding Corporation Glucoamylase converted starch derivatives and their use as emulsifying and encapsulating agents
US6605458B1 (en) 1997-11-21 2003-08-12 Novozymes A/S Protease variants and compositions
WO1999029876A2 (fr) 1997-12-09 1999-06-17 Genencor International, Inc. Alpha-amylases mutantes de bacillus licheniformis
WO1999034011A2 (fr) 1997-12-24 1999-07-08 Genencor International, Inc. Methode amelioree pour tester une enzyme preferee et/ou une composition detergente preferee
WO1999033960A2 (fr) 1997-12-30 1999-07-08 Genencor International, Inc. Proteases de germes gram positifs
WO1999034003A2 (fr) 1997-12-30 1999-07-08 Genencor International, Inc. Proteases provenant d'organismes a gram positif
WO1999042567A1 (fr) 1998-02-18 1999-08-26 Novo Nordisk A/S Amylase bacillaire alcaline
WO1999043793A1 (fr) 1998-02-27 1999-09-02 Novo Nordisk A/S Variantes d'enzymes amylolytiques
WO1999043794A1 (fr) 1998-02-27 1999-09-02 Novo Nordisk A/S Variantes d'alpha-amylase maltogene
WO1999046399A1 (fr) 1998-03-09 1999-09-16 Novo Nordisk A/S Preparation enzymatique de sirop de glucose a partir d'amidon
US6566114B1 (en) 1998-06-10 2003-05-20 Novozymes, A/S Mannanases
US6060299A (en) 1998-06-10 2000-05-09 Novo Nordisk A/S Enzyme exhibiting mannase activity, cleaning compositions, and methods of use
WO1999064619A2 (fr) 1998-06-10 1999-12-16 Novozymes A/S Nouvelles mannanases
WO1999064573A1 (fr) 1998-06-10 1999-12-16 Novozymes A/S Nouvelles mannanases
US6376450B1 (en) 1998-10-23 2002-04-23 Chanchal Kumar Ghosh Cleaning compositions containing multiply-substituted protease variants
WO2000029560A1 (fr) 1998-11-16 2000-05-25 Novozymes A/S VARIANTES DE α-AMYLASE
WO2000032601A2 (fr) 1998-11-30 2000-06-08 The Procter & Gamble Company Procede de preparation de tetraaza macrocycles pontes transversalement
WO2000060059A2 (fr) 1999-03-30 2000-10-12 NovozymesA/S Variantes d'alpha amylase
WO2000060060A2 (fr) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides presentant une activite alcaline alpha-amylase et acides nucleiques les codant
WO2000060058A2 (fr) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides possedant une activite alcaline alpha-amylase et acides nucleiques codant pour ces polypeptides
WO2001014532A2 (fr) 1999-08-20 2001-03-01 Novozymes A/S Amylase alcaline de bacillus
WO2001034784A1 (fr) 1999-11-10 2001-05-17 Novozymes A/S Variants alpha-amylase du type fungamyle
WO2001064852A1 (fr) 2000-03-03 2001-09-07 Novozymes A/S Polypeptides possedant une activite de l'alpha-amylase et acides nucleiques codant pour ces polypeptides
WO2001066712A2 (fr) 2000-03-08 2001-09-13 Novozymes A/S Variants possedant des proprietes modifiees
US6610642B2 (en) 2000-04-20 2003-08-26 The Procter And Gamble Company Cleaning compositions containing multiply-substituted protease variants
WO2001088107A2 (fr) 2000-05-12 2001-11-22 Novozymes A/S Variantes d'alpha-amylase avec une activite 1,6 alteree
WO2001096537A2 (fr) 2000-06-14 2001-12-20 Novozymes A/S Alpha-amylase pre-oxydee
WO2002010355A2 (fr) 2000-08-01 2002-02-07 Novozymes A/S Mutants d'alpha-amylase a proprietes modifiees
WO2002031124A2 (fr) 2000-10-13 2002-04-18 Novozymes A/S Variant de l'alpha-amylase possedant des proprietes modifiees
WO2002092797A2 (fr) 2001-05-15 2002-11-21 Novozymes A/S Variant d'alpha-amylases ayant des proprietes modifiees
WO2002102955A1 (fr) 2001-06-18 2002-12-27 Unilever Plc Conditionnement soluble dans l'eau et liquides contenus dans ce conditionnement
WO2004055178A1 (fr) 2002-12-17 2004-07-01 Novozymes A/S Alpha-amylases thermostables
US7833773B2 (en) 2003-04-30 2010-11-16 Danisco Us Inc. Bacillus mHKcel cellulase
US7449318B2 (en) 2003-04-30 2008-11-11 Danisco A/S, Genencor Division Bacillus mHKcel cellulase
WO2004111178A1 (fr) 2003-05-23 2004-12-23 The Procter & Gamble Company Composition de nettoyage destinee a etre utilisee dans un lave-linge ou un lave-vaisselle
WO2004113551A1 (fr) 2003-06-25 2004-12-29 Novozymes A/S Procede d'hydrolyse de l'amidon
WO2005001064A2 (fr) 2003-06-25 2005-01-06 Novozymes A/S Polypeptides a activite alpha-amylase et polynucleotides codant pour ceux-ci
WO2005003311A2 (fr) 2003-06-25 2005-01-13 Novozymes A/S Enzymes de traitement d'amidon
WO2005018336A1 (fr) 2003-08-22 2005-03-03 Novozymes A/S Processus de preparation d'une pate contenant une exo-amylase glucogenique de degradation de l'amidon de famille 13
WO2005019443A2 (fr) 2003-08-22 2005-03-03 Novozymes A/S Variants d'alpha-amylases fongiques
WO2005056782A2 (fr) 2003-12-03 2005-06-23 Genencor International, Inc. Perhydrolase
WO2005054475A1 (fr) 2003-12-03 2005-06-16 Meiji Seika Kaisha, Ltd. Stce d'endoglucanase et preparation de cellulase le contenant
WO2005056787A1 (fr) 2003-12-08 2005-06-23 Meiji Seika Kaisha, Ltd. Cellulase supportant les tensioactifs et procede de transformation associe
WO2005066338A1 (fr) 2004-01-08 2005-07-21 Novozymes A/S Amylase
WO2006002643A2 (fr) 2004-07-05 2006-01-12 Novozymes A/S Variants d'alpha-amylases presentant des proprietes modifiees
WO2006012902A2 (fr) 2004-08-02 2006-02-09 Novozymes A/S Creation de diversite dans des polypeptides
WO2006012899A1 (fr) 2004-08-02 2006-02-09 Novozymes A/S Variants d'alpha-amylase maltogene
WO2006031554A2 (fr) 2004-09-10 2006-03-23 Novozymes North America, Inc. Procedes permettant de detruire, de reduire, d'eliminer ou d'empecher la formation d'un film biologique
WO2006063594A1 (fr) 2004-12-15 2006-06-22 Novozymes A/S Amylase de bacille alcaline
WO2006066596A2 (fr) 2004-12-22 2006-06-29 Novozymes A/S Enzymes hybrides
WO2006066594A2 (fr) 2004-12-23 2006-06-29 Novozymes A/S Variantes de l'alpha-amylase
WO2006136161A2 (fr) 2005-06-24 2006-12-28 Novozymes A/S Amylases a usage pharmaceutique
WO2007044993A2 (fr) 2005-10-12 2007-04-19 Genencor International, Inc. Utilisation et production d'une metalloprotease neutre stable au stockage
WO2007145964A2 (fr) 2006-06-05 2007-12-21 The Procter & Gamble Company Stabilisateur d'enzymes
WO2008000825A1 (fr) 2006-06-30 2008-01-03 Novozymes A/S Variantes d'alpha-amylases bactériennes
WO2008010925A2 (fr) 2006-07-18 2008-01-24 Danisco Us, Inc., Genencor Division Variantes de protéases actives sur une large plage de températures
WO2008088493A2 (fr) 2006-12-21 2008-07-24 Danisco Us, Inc., Genencor Division Compositions et utilisations pour un polypeptide alpha-amylase de l'espèce de bacille 195
WO2008092919A1 (fr) 2007-02-01 2008-08-07 Novozymes A/S Alpha-amylase et son utilisation
WO2008101894A1 (fr) 2007-02-19 2008-08-28 Novozymes A/S Polypeptides possédant une activité débranchante de l'amidon
WO2008112459A2 (fr) 2007-03-09 2008-09-18 Danisco Us Inc., Genencor Division Variants de l'α-amylase d'une espèce de bacillus alcaliphile, compositions comprenant des variants de l'α-amylase, et procédés d'utilisation
WO2009058661A1 (fr) 2007-10-31 2009-05-07 Danisco Us Inc., Genencor Division Utilisation et production de métalloprotéases neutres stables vis-à-vis des citrates
WO2009058303A2 (fr) 2007-11-01 2009-05-07 Danisco Us Inc., Genencor Division Production de thermolysine et de ses variants et utilisation dans des détergents liquides
WO2009061380A2 (fr) 2007-11-05 2009-05-14 Danisco Us Inc., Genencor Division Variants de bacillus sp. ts-23 alpha-amylase à propriétés modifiées
WO2009061381A2 (fr) 2007-11-05 2009-05-14 Danisco Us Inc., Genencor Division Variants d'alpha-amylase à propriétés modifiées
WO2009100102A2 (fr) 2008-02-04 2009-08-13 Danisco Us Inc., Genencor Division Variants ts23 de l’alpha-amylase à propriétés modifiées
EP2100947A1 (fr) 2008-03-14 2009-09-16 The Procter and Gamble Company Composition détergente de lave-vaisselle automatique
EP2100949A1 (fr) 2008-03-14 2009-09-16 The Procter and Gamble Company Composition de détergent de lave-vaisselle automatique
US9181296B2 (en) 2008-03-26 2015-11-10 Novozymes A/S Stabilized liquid enzyme compositions
WO2009140504A1 (fr) 2008-05-16 2009-11-19 Novozymes A/S Polypeptides présentant une activité alpha-amylase et polynucléotides codant pour ces polypeptides
WO2009149200A2 (fr) 2008-06-06 2009-12-10 Danisco Us Inc. Compositions et procédés comprenant des protéases microbiennes variantes
WO2009149145A2 (fr) 2008-06-06 2009-12-10 Danisco Us Inc., Genencor Division Compositions et procédés comprenant des protéases microbiennes variantes
WO2009149144A2 (fr) 2008-06-06 2009-12-10 Danisco Us Inc. Compositions et procédés comprenant des protéases microbiennes variantes
WO2009149419A2 (fr) 2008-06-06 2009-12-10 Danisco Us Inc. Alpha amylases variantes de bacillus subtilis et leurs procédés d’utilisation
WO2010044786A1 (fr) 2008-10-15 2010-04-22 Danisco Us Inc., Genencor Division Variant modifié d’inhibiteurs de la protéase bowman-birk
WO2010056640A2 (fr) 2008-11-11 2010-05-20 Danisco Us Inc. Compositions et méthodes comportant des variantes de protéase à serine
WO2010056653A2 (fr) 2008-11-11 2010-05-20 Danisco Us Inc. Protéases comprenant une ou plusieurs mutations combinables
US8530219B2 (en) 2008-11-11 2013-09-10 Danisco Us Inc. Compositions and methods comprising a subtilisin variant
WO2010059413A2 (fr) 2008-11-20 2010-05-27 Novozymes, Inc. Polypeptides ayant une activité amylolytique renforcée et polynucléotides codant pour ceux-ci
WO2010088447A1 (fr) 2009-01-30 2010-08-05 Novozymes A/S Polypeptides ayant une activité alpha-amylase et polynucléotides codant pour ceux-ci
WO2010091221A1 (fr) 2009-02-06 2010-08-12 Novozymes A/S Polypeptides ayant une activité alpha-amylase et polynucléotides codant pour ceux-ci
WO2010104675A1 (fr) 2009-03-10 2010-09-16 Danisco Us Inc. Alpha-amylases associées à la souche bacillus megaterium dsm90, et leurs procédés d'utilisation
WO2010115021A2 (fr) 2009-04-01 2010-10-07 Danisco Us Inc. Compositions et procédés comprenant des variantes alpha-amylases qui possèdent des propriétés modifiées
WO2010115028A2 (fr) 2009-04-01 2010-10-07 Danisco Us Inc. Système de lavage comprenant une alpha-amylase et une protéase
WO2010117511A1 (fr) 2009-04-08 2010-10-14 Danisco Us Inc. Alpha-amylases liées à la souche halomonas wdg195 et procédés d'utilisation
WO2011013022A1 (fr) 2009-07-28 2011-02-03 Koninklijke Philips Electronics N.V. Unité de lavage et de stérilisation
WO2011072099A2 (fr) 2009-12-09 2011-06-16 Danisco Us Inc. Compositions et procédés comprenant des variants de protéase
WO2011076897A1 (fr) 2009-12-22 2011-06-30 Novozymes A/S Utilisation de variants d'amylase à basse température
WO2011076123A1 (fr) 2009-12-22 2011-06-30 Novozymes A/S Compositions comprenant un polypeptide renforçateur et un enzyme dégradant l'amidon, et utilisations correspondantes
WO2011087836A2 (fr) 2009-12-22 2011-07-21 Novozymes A/S Variants de pullulanase et utilisations de ceux-ci
WO2011080352A1 (fr) 2010-01-04 2011-07-07 Novozymes A/S Alpha-amylases
WO2011080353A1 (fr) 2010-01-04 2011-07-07 Novozymes A/S Stabilisation des alpha-amylases en présence d'une déplétion en calcium et d'un ph acide
WO2011082425A2 (fr) 2010-01-04 2011-07-07 Novozymes A/S Variants d'alpha-amylase et polynucleotides les codant
WO2011080354A1 (fr) 2010-01-04 2011-07-07 Novozymes A/S Alpha-amylases
WO2011082429A1 (fr) 2010-01-04 2011-07-07 Novozymes A/S Alpha-amylases
WO2011098531A1 (fr) 2010-02-10 2011-08-18 Novozymes A/S Variants et compositions contenant des variants à stabilité élevée en présence d'un agent chélateur
WO2011140364A1 (fr) 2010-05-06 2011-11-10 Danisco Us Inc. Compositions et procédés comprenant des variants de la subtilisine
WO2012112718A1 (fr) 2011-02-15 2012-08-23 Novozymes Biologicals, Inc. Réduction des odeurs dans les machines de nettoyage et les procédés de nettoyage
WO2012151534A1 (fr) 2011-05-05 2012-11-08 Danisco Us Inc. Procédés et compositions comprenant des variants de la sérine protéase
WO2013063460A2 (fr) 2011-10-28 2013-05-02 Danisco Us Inc. Variants d'alpha-amylase pour obtention de maltohexaose variant
WO2013087286A1 (fr) 2011-12-12 2013-06-20 Unilever Plc Compositions pour lessiver
WO2013165725A1 (fr) 2012-04-30 2013-11-07 Danisco Us Inc. Systèmes de perhydrolase à format de dosage unitaire
WO2013184577A1 (fr) 2012-06-08 2013-12-12 Danisco Us Inc. Variants d'alpha-amylase dérivés de l'alpha-amylase de cytophaga sp. amylase/ (cspamy2)
WO2014059360A1 (fr) 2012-10-12 2014-04-17 Danisco Us Inc. Compositions comprenant un variant d'enzyme lipolytique et procédés associés
WO2014071410A1 (fr) 2012-11-05 2014-05-08 Danisco Us Inc. Compositions et procédés comportant des variants de thermolysine protéase
WO2014099523A1 (fr) 2012-12-21 2014-06-26 Danisco Us Inc. Variants d'alpha-amylase
WO2014164777A1 (fr) 2013-03-11 2014-10-09 Danisco Us Inc. Variantes combinatoires d'alpha-amylases
WO2014194054A1 (fr) 2013-05-29 2014-12-04 Danisco Us Inc. Métalloprotéases inédites
WO2014194034A2 (fr) 2013-05-29 2014-12-04 Danisco Us Inc. Métalloprotéases inédites
WO2014194117A2 (fr) 2013-05-29 2014-12-04 Danisco Us Inc. Métalloprotéases inédites
WO2014194032A1 (fr) 2013-05-29 2014-12-04 Danisco Us Inc. Métalloprotéases inédites
WO2015010009A2 (fr) 2013-07-19 2015-01-22 Danisco Us Inc. Compositions et méthodes comprenant un variant d'enzyme lipolytique
WO2015022428A1 (fr) 2013-08-15 2015-02-19 Novozymes A/S Procédé de production d'un extrait de café à l'aide d'enzymes ayant une activité bêta-1,3-galactanase
WO2015038792A1 (fr) 2013-09-12 2015-03-19 Danisco Us Inc. Compositions et procédés comprenant des variants de protéase lg12-clade
WO2015077126A1 (fr) 2013-11-20 2015-05-28 Danisco Us Inc. Variants d'alpha-amylases ayant une sensibilité réduite au clivage protéasique, et leurs procédés d'utilisation
WO2015089441A1 (fr) 2013-12-13 2015-06-18 Danisco Us Inc. Sérine protéases d'espèce de bacillus
WO2015089447A1 (fr) 2013-12-13 2015-06-18 Danisco Us Inc. Sérines protéases du clade du bacillus gibsonii
WO2015143360A2 (fr) 2014-03-21 2015-09-24 Danisco Us Inc. Sérine-protéases de l'espèce bacillus
WO2016061438A1 (fr) 2014-10-17 2016-04-21 Danisco Us Inc. Sérines protéases de l'espèce bacillus
WO2016069552A1 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérines protéases
WO2016069563A1 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérine protéases
WO2016069548A2 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérine-protéases
WO2016069544A1 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérines protéases
WO2016069569A2 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérine protéases
WO2016069557A1 (fr) 2014-10-27 2016-05-06 Danisco Us Inc. Sérine-protéases de l'espèce bacillus
WO2016145428A1 (fr) 2015-03-12 2016-09-15 Danisco Us Inc Compositions et procédés comprenant des variants de protéase lg12-clade
US10683474B2 (en) 2015-06-05 2020-06-16 The Procter & Gamble Company Compacted liquid laundry detergent composition
WO2017054983A1 (fr) 2015-10-01 2017-04-06 Unilever Plc Composition de détergent à lessive liquide
WO2017079751A1 (fr) * 2015-11-05 2017-05-11 Danisco Us Inc Mannanases de paenibacillus sp.
WO2019032257A1 (fr) 2017-08-11 2019-02-14 The Procter & Gamble Company Article formant dose unitaire soluble dans l'eau, comprenant un polymère greffé amphiphile et un polyester téréphtalate
WO2019185726A1 (fr) * 2018-03-29 2019-10-03 Novozymes A/S Variants de mannanase et polynucléotides codant pour ceux-ci
US11046919B2 (en) 2018-06-26 2021-06-29 The Procter & Gamble Company Liquid laundry detergent composition
WO2020223959A1 (fr) 2019-05-09 2020-11-12 The Procter & Gamble Company Composition de détergent à lessive liquide anti-acarien stable comprenant du benzoate de benzyle
WO2020264077A1 (fr) 2019-06-28 2020-12-30 The Procter & Gamble Company Composition nettoyante
US11208619B2 (en) 2019-08-22 2021-12-28 Henkel IP & Holding GmbH Unit dose detergent products with effect on protein stains
WO2021037895A1 (fr) 2019-08-27 2021-03-04 Novozymes A/S Composition détergente
WO2021041685A1 (fr) 2019-08-28 2021-03-04 Henkel IP & Holding GmbH Compositions détergentes contenant du polyéthylène glycol et un acide organique
WO2021108307A1 (fr) 2019-11-27 2021-06-03 The Procter & Gamble Company Tensioactifs alkylbenzènesulfonate améliorés
WO2021127662A1 (fr) 2019-12-19 2021-06-24 Henkel IP & Holding GmbH Détergents de faible densité en dose unitaire avec parfum encapsulé
WO2021123184A2 (fr) 2019-12-19 2021-06-24 Novozymes A/S Variants d'alpha-amylase
US20210317387A1 (en) 2020-04-06 2021-10-14 Henkel Ag & Co. Kgaa Cleaning compositions comprising dispersin variants
WO2021219296A1 (fr) 2020-04-29 2021-11-04 Henkel Ag & Co. Kgaa Détergent pour textiles fortement alcalin contenant une protéase
WO2021223552A1 (fr) 2020-05-08 2021-11-11 The Procter & Gamble Company Composition de détergent à lessive liquide
WO2021247801A1 (fr) 2020-06-05 2021-12-09 The Procter & Gamble Company Compositions détergentes contenant un tensioactif ramifié
WO2022010372A1 (fr) 2020-07-10 2022-01-13 Institut Biosens-Istrazivacko Razvojni Institut Za Informacione Tehnologije Biosistema Système et procédé de prélèvement intelligent d'échantillons de sol
WO2022074037A2 (fr) 2020-10-07 2022-04-14 Novozymes A/S Variants d'alpha-amylase
WO2022106404A1 (fr) 2020-11-18 2022-05-27 Novozymes A/S Combinaison de protéases
US20220162523A1 (en) 2020-11-20 2022-05-26 The Procter & Gamble Company Water-soluble unit dose article comprising a fatty alkyl ester alkoxylate non-ionic surfactant and an alkoxylated alcohol non-ionic surfactant
US20220186144A1 (en) 2020-12-15 2022-06-16 Henkel IP & Holding GmbH Unit Dose Laundry Detergent Compositions Containing Soil Release Polymers
WO2022157311A1 (fr) 2021-01-22 2022-07-28 Novozymes A/S Composition d'enzyme liquide avec piégeur de sulfite
WO2022167251A1 (fr) 2021-02-04 2022-08-11 Henkel Ag & Co. Kgaa Composition détergente comprenant des variants de xanthane lyase et d'endoglucanase ayant une stabilité améliorée

Non-Patent Citations (81)

* Cited by examiner, † Cited by third party
Title
ADEMARK ET AL., J. BIOTECHNOL, vol. 63, 1998, pages 199 - 210
AGR. BIOL. CHEM., vol. 36, no. 2, 1972, pages 285 - 93
AKINO ET AL., ARCH. MICROBIOL, vol. 152, 1989, pages 10 - 15
ALTSCHUL ET AL., J. MOL. BIOL., vol. 215, 1990, pages 403 - 410
ARAUJOWARD, J. APPL. BACTERIOL, vol. 68, 1990, pages 253 - 261
ARAUJOWARD, J. APPL. BACTERIOL., vol. 68, 1990, pages 253 - 261
ARCAND ET AL., J.BIOCHEM., vol. 290, 1993, pages 857 - 863
ASPEBORG ET AL.: "Evolution, substrate specificity and subfamily classification of glycosyl hydrolase family 5 (GH5", BMC EVOLUTIONARY BIOLOGY, vol. 12, 2012, pages 186, XP021127883, DOI: 10.1186/1471-2148-12-186
BICHO ET AL., APPL. MICROBIOL. BIOTECHNOL., vol. 36, 1991, pages 337 - 343
BORASTON ET AL., BIOCHEM J, vol. 382, 2004, pages 769 - 81
BRAITHWAITE ET AL., BIOCHEM J., vol. 305, January 1999 (1999-01-01), pages 1005 - 1010
CANN ET AL., J. BACTERIOL., vol. 181, 1999, pages 1643 - 1651
CHANGCOHEN, MOL. GEN. GENET, vol. 168, 1979, pages 111 - 115
CHARRIERROULAND, J. EXPT. ZOOL., vol. 290, 2001, pages 125 - 135
CHEN ET AL., J. BIOTECHNOL, vol. 128, no. 3, 2007, pages 452 - 461
CHEN ET AL., WEI SHENG WU XUE BAO, vol. 40, 2000, pages 62 - 68
CHRISTGAU ET AL., BIOCHEM. MOL. BIOL. INT., vol. 33, 1994, pages 917 - 925
CIVAS ET AL., BIOCHEM. J., vol. 219, 1984, pages 857 - 863
CUI ET AL., WEI SHENG WU XUE BAO, vol. 39, no. 1, 1999, pages 60 - 63
DARTOIS ET AL., BIOCHEM. BIOPHYS. ACTA, vol. 1131, 1993, pages 253 - 260
DATABASE Geneseq [online] 13 July 2017 (2017-07-13), "Paenibacillus sp. mannanase protein SEQ 29.", XP002810577, retrieved from EBI accession no. GSP:BDW54903 Database accession no. BDW54903 *
DATABASE UniProt [online] 20 January 2016 (2016-01-20), "Endoglucanase from Paenibacillus sp.", XP002810576, retrieved from EBI accession no. UNIPROT:A0A0Q7TE94 Database accession no. A0A0Q7TE94 *
DUFFAUD ET AL., APPL. ENVIRON. MICROBIOL., vol. 63, 1997, pages 169 - 177
ERIKSSONWINELL: "Acta Chem. Scand.", vol. 22, 1968, pages: 1924
EUR J BIOCHEM, vol. 170, 1988, pages 575 - 581
FANUTTI ET AL., J. BIOL. CHEM., vol. 270, no. 49, 1995, pages 29314 - 29322
FILICHKIN ET AL., PLANT PHYSIOL., vol. 134, 2000, pages 1080 - 1087
FRANCO ET AL., BIOTECHNOL APPL. BIOCHEM., vol. 40, 2004, pages 255 - 259
GHERARDINI ET AL., J. BACTERIOL., vol. 169, 1987, pages 2038 - 2043
GIBBS ET AL., CURR. MICROBIOL., vol. 39, no. 6, 1999, pages 351 - 357
GILKES ET AL., JBIOL CHEM, vol. 263, 1988, pages 10401 - 10407
HALSTEAD ET AL., MICROBIOL., vol. 145, 1999, pages 3101 - 3108
HAN ET AL., APPL. MICROBIOL BIOTECHNOL., vol. 73, no. 3, 2006, pages 618 - 630
HATADA ET AL., EXTREMOPHILES, vol. 9, 2005, pages 497 - 500
HAYASHI ET AL., ANNU. REV. PLANT. PHYSIOL. PLANT MOL. BIOL.,, vol. 40, 1989, pages 139 - 168
HELOW AND KHATTAB, ACTA MICROBIOL. IMMUNOL. HUNG., vol. 43, 1996, pages 289 - 299
HIGGINS ET AL., GENE, vol. 73, 1988, pages 237 - 244
HILGE ET AL., STRUCTURE, vol. 6, 1998, pages 1433 - 1444
HUANG ET AL., WEI SHENG WU XUE BAO, vol. 47, no. 2, 2007, pages 280 - 284
KANSOHNAGIEB, ANTON. VAN. LEEUWENHOEK., vol. 85, 2004, pages 103 - 114
KARIN ET AL., PROC. NATL. ACAD. SCI. USA, vol. 90, 1993, pages 5873
KATAOKATOKIWA, J. APPL. MICROBIOL., vol. 84, 1998, pages 357 - 367
KUGIMIYA ET AL., BIOSCI. BIOTECH. BIOCHEM., vol. 56, 1992, pages 716 - 719
LI ET AL., Z. NATURFORSCH (C), vol. 61, 2006, pages 840 - 846
MATSUSHITA, J. BACTERIOL., vol. 173, 1991, pages 6919 - 6926
MENDOZA, WORLD J. MICROBIOL. BIOTECHNOL, vol. 10, 1994, pages 51 - 54
MOREIRAFILHO, APPL MICROBIOL BIOTECHNOL, vol. 79, 2008, pages 165
MORRIS, APPL. ENVIRON. MICROBIOL., vol. 61, 1995, pages 2262 - 2269
MUNI RAMMANNAGARI SUBHOSH CHANDRA: "Isolation, Purification and Characterization of a Thermostable β-Mannanase from Paenibacillus sp. DZ3", HAN'GUG EUNG'YONG SAENGMYEONG HWA HAGHOEJI - JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY, vol. 54, no. 3, 30 June 2011 (2011-06-30), Seoul, Korea, pages 325 - 331, XP055335373, ISSN: 1738-2203, DOI: 10.3839/jksabc.2011.052 *
NAKAJIMA AND MATSUURA, BIOSCI. BIOTECHNOL. BIOCHEM., vol. 61, 1997, pages 1739 - 1742
PARKER ET AL., BIOTECHNOL. BIOENG., vol. 75, no. 3, 2001, pages 322 - 333
PASONRATANAKHANOKCHAI, APPL. ENVIRON. MICROBIOL., vol. 72, 2006, pages 2483 - 2490
PEARSON ET AL., PROC. NATL. ACAD. SCI. USA, vol. 85, 1988, pages 2444 - 2448
PERRET ET AL., BIOTECHNOL. APPL. BIOCHEM., vol. 40, 2004, pages 255 - 259
POLITZ, APPL. MICROBIOL. BIOTECHNOL., vol. 53, no. 6, 2000, pages 715 - 721
PROC. NATL. ACAD. SCI. USA, vol. 89, 1989, pages 10915
PUCHART ET AL., BIOCHIMICA ET BIOPHYSICA ACTA, vol. 1674, 2004, pages 239 - 250
REGALADO ET AL., J. SCI. FOOD AGRIC, vol. 80, 2000, pages 1343 - 1350
ROBERT C. EDGAR: "MUSCLE: multiple sequence alignment with high accuracy and high throughput", NUCL. ACIDS RES, vol. 32, no. 5, 2004, pages 1792 - 1797, XP008137003, DOI: 10.1093/nar/gkh340
SACHSLEHNER ET AL., J. BIOTECHNOL., vol. 80, 2000, pages 127 - 134
SCHIMADA ET AL., BIOCHEM., vol. 106, 1989, pages 383 - 388
SETATI ET AL., PROTEIN EXPRESS PURIF, vol. 21, 2001, pages 105 - 114
SMITH, APPL. ENV. MICROBIOL, vol. 51, 1986, pages 634
STALBRAND ET AL., J. BIOTECHNOL., vol. 29, 1993, pages 229 - 242
STOL, APPL. ENVIRON. MICROBIOL., vol. 65, no. 6, 1999, pages 2598 - 2605
SUN ET AL., SHENG WU GONG CHENGXUE BAO., vol. 19, no. 3, 2003, pages 327 - 330
SUNNA ET AL., APPL. ENVIRON. MICROBIOL., vol. 66, 2000, pages 664 - 670
TALBOTSYGUSCH, APPL. ENVIRON. MICROBIOL, vol. 56, 1990, pages 3505 - 3510
TAMARU ET AL., J. FERMENT. BIOENG., vol. 83, 1997, pages 201 - 205
TANG ET AL., APPL. ENVIRON. MICROBIOL, vol. 67, 2001, pages 2298 - 2303
TOMME ET AL.: "Enzymatic Degradation of Insoluble Polysaccharides", 1995, AMERICAN CHEMICAL SOCIETY, article "Cellulose-binding domains: classification and properties", pages: 142 - 163
VINCKEN ET AL., PLANT PHYSIOL., vol. 104, 1994, pages 99 - 107
VINCKEN ET AL., TRICHODERMA VIRIDE
WORLD J. MICROBIOL. BIOTECHNOL., vol. 8, no. 2, 1992, pages 115 - 120
WYMELENBERG ET AL., J. BIOTECHNOL., vol. 118, 2005, pages 17 - 34
YAMAGUCHI ET AL., GENE, vol. 109, 1991, pages 117 - 113
YAMAMURA ET AL., BIOSCI. BIOTECHNOL. BIOCHEM., vol. 60, 1996, pages 674 - 676
YAMAMURA ET AL., BIOSCI. BIOTECHNOL. BIOCHEM., vol. 7, 1993, pages 1316 - 1319
YANHE ET AL., EXTREMOPHILES, vol. 8, 2004, pages 447 - 454
YEOMAN ET AL.: "Adv Appl Microbiol", vol. 70, 2010, ELSEVIER, pages: 1
ZAKARIA ET AL., BIOSCI. BIOTECHNOL. BIOCHEM., vol. 62, no. 3, 1998, pages 655 - 660

Similar Documents

Publication Publication Date Title
JP7269907B2 (ja) パエニバチルス（Ｐａｅｎｉｂａｃｉｌｌｕｓ）及びバチルス（Ｂａｃｉｌｌｕｓ）種のマンナナーゼ
JP7364330B2 (ja) パエニバチルス（Ｐａｅｎｉｂａｃｉｌｌｕｓ）属種及びバチルス（Ｂａｃｉｌｌｕｓ）属種のマンナナーゼ
US20200362324A1 (en) Paenibacillus sp. mannanases
US8986970B2 (en) Detergent compositions containing Bacillus agaradhaerens mannanase and methods of use thereof
US20140135252A1 (en) Detergent compositions containing geobacillus tepidamans mannanase and methods of use thereof
US11866748B2 (en) Compositions comprising polypeptides having mannanase activity
US20150344858A1 (en) Novel mannanase, compositions and methods of use thereof
US20140073548A1 (en) Detergent compositions containing bacillus sp. mannanase and methods of use thereof
CN111373036A (zh) 具有甘露聚糖酶活性的多肽和编码它们的多核苷酸
CN103608356A (zh) 包含黏琼脂芽孢杆菌(Bacillus agaradhaerens)甘露聚糖酶的洗涤剂组合物及其使用方法
CN103502445A (zh) 包含芽孢杆菌甘露聚糖酶的洗涤剂组合物及其使用方法
CN103534266A (zh) 包含喜温地芽孢杆菌(geobacillus tepidamans)甘露聚糖酶的洗涤剂组合物及其使用方法
WO2024050339A1 (fr) Variants de mannanases et procédés d'utilisation

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 23773141

Country of ref document: EP

Kind code of ref document: A1