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EP3898919A1 - Waschmittelbeutel mit metalloproteasen - Google Patents

Waschmittelbeutel mit metalloproteasen

Info

Publication number
EP3898919A1
EP3898919A1 EP19829560.2A EP19829560A EP3898919A1 EP 3898919 A1 EP3898919 A1 EP 3898919A1 EP 19829560 A EP19829560 A EP 19829560A EP 3898919 A1 EP3898919 A1 EP 3898919A1
Authority
EP
European Patent Office
Prior art keywords
percent
compartment
present
seq
metalloprotease
Prior art date
Legal status (The legal status 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 status listed.)
Withdrawn
Application number
EP19829560.2A
Other languages
English (en)
French (fr)
Inventor
Astrid Benie
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novozymes AS
Original Assignee
Novozymes AS
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 Novozymes AS filed Critical Novozymes AS
Publication of EP3898919A1 publication Critical patent/EP3898919A1/de
Withdrawn legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/24—Metalloendopeptidases (3.4.24)
    • 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
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/04—Detergent materials or soaps characterised by their shape or physical properties combined with or containing other objects
    • C11D17/041—Compositions releasably affixed on a substrate or incorporated into a dispensing means
    • C11D17/042—Water soluble or water disintegrable containers or substrates containing cleaning compositions or additives for cleaning compositions
    • 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
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/04—Detergent materials or soaps characterised by their shape or physical properties combined with or containing other objects
    • C11D17/041—Compositions releasably affixed on a substrate or incorporated into a dispensing means
    • C11D17/042—Water soluble or water disintegrable containers or substrates containing cleaning compositions or additives for cleaning compositions
    • C11D17/045—Multi-compartment
    • 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
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y301/00—Hydrolases acting on ester bonds (3.1)
    • C12Y301/21—Endodeoxyribonucleases producing 5'-phosphomonoesters (3.1.21)
    • C12Y301/21001—Deoxyribonuclease I (3.1.21.1)

Definitions

  • the invention relates to a multi-compartment pouch comprising a selected combination of ingredients in different compartments as well as a washing process and the use of the multi compartment pouch for laundry applications, such as for washing and cleaning of textiles, or for dishwashing applications.
  • the detergent formulators are constantly looking for new detergent forms with improved cleaning profile. Lately, products in unit dose form have become one of the preferred forms for the user due to the ease of use, particularly water-soluble pouches which present the added advantage of no need to unwrap.
  • Enzymatic detergent compositions normally contain a protease.
  • One group of proteases the metalloproteases, have not yet found widespread use in detergent industry, however, mainly due to low stability in detergent compositions as well as under the conditions during the wash process.
  • an M4 family metal loprotease from Bacillus amyloliquefaciens known as Neutrase® has been used for many years as an additive in various food and feed products.
  • Neutrase® Bacillus amyloliquefaciens
  • this and other metalloproteases have been described for use in detergent and cleaning compositions and processes, they have not been used in detergent compositions in practice.
  • a number of metalloproteases are known to have activity that in theory would make them suitable for detergent use, their instability in detergent compositions and wash conditions has in practice prevented such use.
  • the object of the present invention is to provide an improved way of delivering an enzyme such as a metalloprotease in a multi-compartment pouch.
  • the invention relates to an enzyme containing water-soluble films, and their use in detergents.
  • the present invention relates to a multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition.
  • the present invention relates to a method of releasing an enzyme in a cleaning process comprising steps of: a. providing a multicompartment pouch with at least two compartments, the first compartment comprising enzyme-containing composition and the second compartment comprising a detergent composition; b. releasing the detergent composition from the second compartment and subsequently releasing the enzyme-containing composition from the first compartment into the wash liquor.
  • the present invention also relates to a method of treating a substrate, where the method includes the step of contacting the substrate with the pouch in the presence of water, wherein the substrate is a fabric or a hard surface.
  • the present invention also relates to a method of cleaning comprising contacting a surface and/or a fabric with the pouch.
  • the present invention also relates to a method for removing and/or reducing soil and/or for reducing redeposition on a surface and/or textile comprising contacting the surface and/or textile with the pouch.
  • the present invention also relates to a method of laundering or dishwashing in a washing machine comprising the steps of placing the pouch into the product dispenser and releasing it during the wash cycle.
  • the present invention also relates to use of the pouch for cleaning of an item, wherein the item is a textile or a surface.
  • the present invention also relates to use of the pouch in a cleaning process, such as laundry, hard surface cleaning, dish wash or automated dish wash.
  • the present invention also relates to use of the pouch for removing or releasing a stain from a textile having a stain.
  • the near or approximating unrecited number may be a number which, in the context in which it is presented, provides the substantial equivalent of the specifically recited number.
  • the term“about” refers to a range of -10% to +10% of the numerical value, unless term is otherwise specifically defined in context.
  • the phrase a “pH value of about 9” refers to pH values of from 8.1 to 9.9, unless the pH value is specifically defined otherwise.
  • protease activity or“peptidase activity” is defined herein as the ability to break down the amide bond of a protein by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain.
  • Protein activity can be measured using any assay in which a substrate is employed that includes peptide bonds relevant for the specificity of the protease in question.
  • Assay-pH and assay-temperature are likewise to be adapted to the protease in question.
  • assay- pH-values are pH 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , or 12.
  • assay-temperatures are 15, 20, 25, 30, 35, 37, 40, 45, 50, 55, 60, 65, 70, 80, 90, or 95°C.
  • Examples of general protease substrates are casein, bovine serum albumin and haemoglobin.
  • protease activity was determined using assays which are described in“Materials and Methods”, such as the Protazyme OL assay.
  • metaloprotease refers to a protease having one or more metal ions in the binding/active site.
  • cleaning compositions and “cleaning formulations,” refer to compositions that find use in the removal of undesired compounds from items to be cleaned, such as fabric, carpets, dishware including glassware, contact lenses, hard surfaces such as tiles, zincs, floors, and table surfaces, hair (shampoos), skin (soaps and creams), teeth (mouthwashes, toothpastes), etc.
  • the terms encompass any materials/compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, granule, or spray compositions).
  • the specific selection of cleaning composition materials 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.
  • detergent composition e.g., liquid and/or solid laundry detergents and fine fabric detergents; hard surface cleaning formulations, such as for glass, wood, ceramic and metal counter tops and windows; carpet cleaners; oven cleaners; fabric fresheners; fabric softeners; and textile and laundry pre-spotters, as well as dishwash detergents).
  • DNase means a polypeptide with DNase activity that catalyses the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, thus degrading DNA. DNase activity may be determined according to the procedure described in the Assay I described in“Materials and Methods”.
  • detergent composition refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as hard surfaces or dishware.
  • the detergent composition may be used to e.g. clean dishware for both household cleaning and industrial cleaning.
  • the terms encompass any materials/compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, or spray compositions) and includes, but is not limited to, detergent compositions (e.g., liquid and/or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; and textile and laundry pre-spotters/pretreatment).
  • the detergent formulation may contain one or more additional enzymes (such as other proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidaes, haloperoxygenases, DNase, catalases and mannanases, or any mixture thereof), and/or detergent components such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizer
  • additional enzymes such as other protea
  • fabric encompasses any textile material. Thus, it is intended that the term encompass garments, as well as fabrics, yarns, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material.
  • the term“textile” means any textile material including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material, fabrics made of these materials and products made from fabrics (e.g., garments and other articles).
  • the textile or fabric may be in the form of knits, wovens, denims, non-wovens, felts, yarns, and toweling.
  • the textile may be cellulose based such as natural cellulosics, including cotton, flax/linen, jute, ramie, sisal or coir or manmade cellulosics (e.g. originating from wood pulp) including viscose/rayon, cellulose acetate fibers (tricell), lyocell or blends thereof.
  • the textile or fabric may also be non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non-cellulose based fibers.
  • non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non-cellulose based fibers.
  • blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fiber (e.g. polyamide fiber, acrylic fiber, polyester fiber, polyvinyl chloride fiber, polyurethane fiber, polyurea fiber, aramid fiber), and/or cellulose-containing fiber (e.g.
  • Fabric may be conventional washable laundry, for example stained household laundry.
  • fabric or garment it is intended to include the broader term textiles as well.
  • textiles as well.
  • the term“textile” also covers fabrics.
  • the term "effective amount of enzyme” refers to the quantity of enzyme necessary to achieve the enzymatic activity required in the specific application, e.g., in a defined detergent 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 enzyme used, the cleaning application, the specific composition of the detergent composition, and whether a liquid or dry (e.g., granular, bar) composition is required, and the like.
  • relevant washing conditions is used herein to indicate the conditions, particularly washing temperature, time, washing mechanics, detergent concentration, type of detergent and water hardness, actually used in households in a detergent market segment.
  • wash performance of an enzyme refers to the contribution of an enzyme to washing that provides additional cleaning performance to the detergent without the addition of the enzyme to the composition. Wash performance is compared under relevant washing conditions. Wash performance of enzymes is conveniently measured by their ability to remove certain representative stains under appropriate test conditions. In these test systems, other relevant factors, such as detergent composition, detergent concentration, water hardness, washing mechanics, time, pH, and/or temperature, can be controlled in such a way that conditions typical for household application in a certain market segment are imitated.
  • water hardness or“degree of hardness” or“dH” or“°dH” as used herein refers to German degrees of hardness. One degree is defined as 10 milligrams of calcium oxide per litre of water.
  • improved wash performance is used to indicate that a better end result is obtained in stain removal from items washed (e.g., fabrics or dishware and/or cutlery) under relevant washing conditions as compared to no enzyme or to a reference enzyme, or that less enzyme, on weight basis, is needed to obtain the same end result relative to no enzyme or to a reference enzyme.
  • Improved wash performance could in this context also be that the same effect, e.g., stain removal effect is obtained in shorter wash time, e.g., the enzymes provide their effect more quickly under the tested conditions.
  • wash cycle is defined herein as a washing operation wherein fabric is exposed to the wash liquor for a period of time by circulating the wash liquor and spraying the wash liquor onto the fabric in order to clean the fabric and finally the superfluous wash liquor is removed.
  • a wash cycle may be repeated one, two, three, four, five or even six times at the same or at different temperatures.
  • the fabric is generally rinsed and dried.
  • wash liquor is defined herein as the solution or mixture of water and detergent components optionally including enzymes used for laundrering textiles, for hard surface cleaning or for dishwashing.
  • wash time is defined herein as the time it takes for the entire washing process; i.e. the time for the wash cycle(s) and rinse cycle(s) together.
  • enzyme detergency or“detergency” or“detergency effect” is defined herein as the advantageous effect an enzyme may add to a detergent compared to the same detergent without the enzyme.
  • Important detergency benefits which can be provided by enzymes are stain removal with no or very little visible soils after washing and/or cleaning, prevention or reduction of redeposition of soils released in the washing process an effect that also is termed anti redeposition, restoring fully or partly the whiteness of textiles, which originally were white but after repeated use and wash have obtained a greyish or yellowish appearance an effect that also is termed whitening.
  • Textile care benefits which are not directly related to catalytic stain removal or prevention of redeposition of soils, are also important for enzyme detergency benefits.
  • Examples of such textile care benefits are prevention or reduction of dye transfer from one fabric to another fabric or another part of the same fabric an effect that is also termed dye transfer inhibition or anti- back staining, removal of protruding or broken fibers from a fabric surface to decrease pilling tendencies or remove already existing pills or fuzz an effect that also is termed anti-pilling, improvement of the fabric-softness, color clarification of the fabric and removal of particulate soils which are trapped in the fibers of the fabric or garment.
  • Enzymatic bleaching is a further enzyme detergency benefit where the catalytic activity generally is used to catalyze the formation of bleaching component such as hydrogen peroxide or other peroxides.
  • Hard surface cleaning is defined herein as cleaning of hard surfaces, such as reducing or removing biofilm from a hard surface, wherein hard surfaces may include floors, tables, walls, roofs etc. as well as surfaces of hard objects such as cars (car wash) and dishes (dish wash).
  • Hard surface cleaning also includes cleaning the interior of washing machines, such as the interior of laundry washing machines or dishwashing machines, this includes cleaning soap intake box, walls, windows, baskets, racks, nozzles, pumps, sump, filters, pipelines, tubes, joints, seals, gaskets, fittings, impellers, drums, drains, traps, coin traps inlet and outlets.
  • Dish washing includes but are not limited to cleaning of plates, cups, glasses, bowls, pots, cutlery, spoons, knives, forks, serving utensils, ceramics, plastics, cutting boards, china and glass ware.
  • laundering relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a cleaning or detergent composition of the present invention.
  • the laundering process can for example be carried out using e.g. a household or an industrial washing machine or can be carried out by hand.
  • the present invention relates to a multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition.
  • the present invention also relates to a method of releasing an enzyme in a cleaning process comprising steps of: a. providing a multi-compartment pouch with at least two compartments, the first compartment comprising enzyme-containing composition and the second compartment comprising a detergent composition; b. releasing the detergent composition from the second compartment and subsequently releasing the enzyme-containing composition from the first compartment into the wash liquor.
  • the present invention envisages a multi-compartment pouch.
  • the water-soluble multi-compartment pouch of the invention (herein referred to as pouch) comprises at least two compartments and may for example be in the form of two side-by-side compartments superposed onto another compartment.
  • the pouch is typically a closed structure, made of materials described herein, enclosing a volume space. The volume space is separated into at least two compartments.
  • the pouch can be of any form, shape and material which is suitable to hold the compositions, e.g without allowing the release of the composition from the pouch prior to contact of the pouch with water. The exact execution will depend, for example on the type and amount of the composition.
  • the multi-compartment pouch comprises at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition.
  • the multi-compartment pouch can have more than two compartments, which can be in any disposition, side-by-side, superposed or compartment-inside-compartment. Especially preferred are: i) pouches having two compartments on side-by-side disposition superposed onto a single compartment; and ii) pouches having two side-by-side compartments superposed onto two other side-by-side compartments.
  • each compartment of the multi-compartment pouch may contain a detergent composition or part thereof in any physical form, including solid (loose or densified powder, tablet, pre-formed discrete particles, etc.), liquids (gels, aqueous liquids, non-aqueous liquids, etc.), liquids with solid suspended on them, etc.
  • a detergent composition or part thereof in any physical form, including solid (loose or densified powder, tablet, pre-formed discrete particles, etc.), liquids (gels, aqueous liquids, non-aqueous liquids, etc.), liquids with solid suspended on them, etc.
  • the multi-compartment pouch is very effective in terms of separation of incompatible ingredients.
  • the invention also envisages a method of automatic dishwashing using the pouch of the invention.
  • the pouch of the invention can contain any kind of detergent composition, preferably the composition is a laundry or dishwashing composition.
  • the multi-compartment pouch may be formed by water-soluble films that form the different compartments can be the same but preferably the films have different solubility and are suitable for delivering the content of different compartments at different points in time of the wash cycle or during the wash and during the rinse cycle.
  • the pouch of the invention is very effective in terms of separation of incompatible ingredients.
  • the pouches of the invention are robust, compact and have a great flexibility in terms of ingredients separation and controlled release.
  • the inventors of the present invention have seen a surprising effect when using the multi-compartment pouch.
  • the multi-compartment pouch of the invention an advantageous wash and cleaning capacity is obtained, especially when an enzyme such as metalloprotease is sensitive in presence of detergent components.
  • the wash and cleaning capacity of a preferred multi-compartment pouch of the invention with sequential release of detergent composition followed by the release of enzyme-containing composition is significantly enhanced in comparison with multi-compartment pouches of the invention in which detergent components and enzyme such as metalloprotease on the other hand are released simultaneously.
  • water-soluble film or “water-soluble polymer” encompasses films which disintegrates when in contact with water by forming a solution and/or dispersion of polymer in water.
  • the pouch is preferably made of a film material wherein the film material is soluble in water, and has water solubility of at least 50%, at least 60%, at least 70%, preferably at least 75%, at least 80%, at least 90% or even at least 95%.
  • Preferred pouch materials are polymeric materials, preferably polymers which are formed into a film or sheet.
  • the pouch material can, for example, be obtained by casting, blow moulding, extrusion or blown extrusion of the polymeric material, as known in the art.
  • the pouch of the present invention may be made using any suitable equipment and method.
  • the multi-compartment pouch may be of such a size that it conveniently contains either a unit dose amount of the composition herein, suitable for the required operation, for example one wash, or only a partial dose, to allow the consumer greater flexibility to vary the amount used, for example depending on the size and/or degree of soiling of the wash load.
  • the pouch is made from a water-soluble film which encloses an inner volume; wherein the inner volume is divided into the compartments of the pouch.
  • the multi-compartment pouch herein defined are closed structures, made from a water-soluble film, which encloses a volume space which comprises the solid component or the liquid component of the composition. Said volume space is preferably enclosed by a water-soluble film in such a manner that the volume space is separated from the outside environment.
  • the pouches are made by a process involving stretching the material used for the pouch.
  • the enzyme-containing composition is present in the first compartment of the multi-compartment pouch.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprises a protease.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprises a metalloprotease.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprises a metalloprotease selected from a group consisitng of EC classes EC 3.4.22 or EC3.4.24.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprising the metalloprotease is selected from a group consisting of a. a thermolysin and/or variant thereof; b. a metalloprotease from M4 family, that is not a thermolysin and variant thereof; c. a metalloprotease from the M7 family; and d. a metalloprotease from the M35 metalloprotease.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprising the metalloprotease is an enzyme (E.C 3.4.24) that hydrolyse bonds within peptides and proteins, in the laundry context this leads to enhanced removal of protein or peptide containing stains.
  • Metalloproteases metallopeptidases or metalloproteinases
  • metalloproteases are found in 14 different families.
  • the protease is selected from the M4, M7 or M35 family, more preferably an M4 metalloprotease, most preferably a neutral metalloprotease.
  • the metalloproteases that may be used in this invention includes any of those which may be used in a homecare application.
  • metalloproteases are, for example, derived from bacterium selected from the group consisting of Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus stearothermophilus, and Bacillus thermoproteolyticus, and fungi selected from the group consisting of Aspergillus oryzae and Aspergillus niger.
  • Especially preferred metalloproteases for use herein belong to EC classes EC 3.4.22 or EC3.4.24, more preferably they belong to EC classes EC3.4.22.2, EC3.4.24.28 or EC3.4.24.27.
  • M4 Metalloprotease Family or“M4 Metalloprotease” or“M4” as used herein means a polypeptide falling into the M4 metalloprotease family according to Rawlings et al., Biochem. J., 290, 205-218 (1993) and as further described in MEROPS - (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270-272, 2006).
  • the M4 metalloproteases are neutral metalloproteases containing mainly endopeptidases. All peptidases in the family bind a single, catalytic zinc ion.
  • M4 metalloprotease family members include the common HEXXH motif, where the histidine residues serve as zinc ligands and glutamate is an active site residue. M4 metalloproteases have a pH optimum mainly at neutral pH.
  • the M4 metalloprotease family includes, e.g., Neutrase® (classified as MEROPS subclass M04.014), Thermolysin, Bacillolysin, vibriolysin, pseudolysin, Msp peptidase, coccolysin, aureolysin, vimelysin, lambda toxin neutral peptidase B, PA peptidase (Aeromonas-type), griselysin, stearolysin, Mprlll ( Alteromonas sp.
  • strain 0-7 pap6 peptidase, neutral peptidase ( Thermoactinomyces-type ), ZmpA peptidase ( Burkholderia sp.), zpx peptidase, PrtS peptidase (Photorhabdus luminescens), protealysin, ZmpB peptidase ( Burkholderia sp.).
  • the M4 metalloprotease family of polypeptides have been further characterized and presently includes, according to MEROPS, at least twenty-two subclasses for which a distinct MEROPS ID (i.e., an identifier of the formula M04.xxx) has been assigned, as well as non-peptidase homologues and unassigned peptidases.
  • MEROPS a distinct MEROPS ID (i.e., an identifier of the formula M04.xxx) has been assigned, as well as non-peptidase homologues and unassigned peptidases.
  • Thermolysin-Like Metalloprotease as used herein means (a) an M4 metalloprotease of the MEROPS subclass M04.001 ; (b) an M4 metalloprotease of the MEROPS subclass M04.018; (c) an M4 metalloprotease of the MEROPS subclass M04.021 ; (d) an M4 metalloprotease having an active cleft motif TG[TS][QS]DNGGVH[TI] as shown in SEQ ID NO: 65; (e) an M4 metalloprotease having an active cleft motif
  • the amino acid sequences of several TLPs have been determined, and the three-dimensional structures of several TLPs have been solved. Focus has been on increasing the thermostability of the TLP and a number of publications describe the thermostability of Bacillus TLPs, e.g., Veltman et al., (1998) Biochemistry 37(15):5312-9.
  • the TLPs consist of an alpha-helical C-terminal domain and an N- terminal domain mainly consisting of beta-strands. The domains are connected by a central alpha- helix.
  • This helix is located at the bottom of the active site cleft and contains several of the catalytically important residues such as four substrate binding pockets S2, S1 , ST and S2' have been identified (Hangauer et al. (1984) Biochemistry 23:5730-5741).
  • M7 Metalloprotease Family or“M7 Metalloprotease” or“M7” or“snapalysin family” as used herein means a polypeptide falling into the M7 metalloprotease family according to Rawlings et al., Biochem. J., 290, 205-218 (1993) and as further described in MEROPS - (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270- 272, 2006).
  • the protease family M7 contains a metalloendopeptidase, snapalysin. Snapalysin is active at neutral pH.
  • the only known activity is cleavage of proteins of skimmed milk to form clear plaques around the growing bacterial colonies.
  • the Zinc is bound by two histidines and an aspartate in an HEXXHXXGXXD sequence motif as shown in SEQ ID NO: 68; the glutamate is a catalytic residue.
  • the M7 proteases have clear signal peptides recognized by the SignalP prediction program. They also all have a propeptide that is cleaved off.
  • M35 Metalloprotease Family or “M35 Metalloprotease” or “M35” or “deuterolysin family” as used herein means a polypeptide falling into the M35 metalloprotease family according to Proteolysis in Cell Function, pp13-21 , IOS Press, Amsterdam (1997), Rawlings et al., Biochem. J., 290, 205-218 (1993) and as further described in MEROPS - (Rawlings et al., MEROPS: the peptidase database, Nucl Acids Res, 34 Database issue, D270- 272, 2006).
  • Family M35 members contain two zinc binding histidine’s and a catalytic glutamate in an HEXXH motif as shown in SEQ ID NO: 69. There is a third zinc ligand, an Asp, found in a GTXDXXYG motif as shown in SEQ ID NO: 70 C-terminal to the His zinc ligands (see the Alignment). For this reason, the peptidases in this family are sometimes termed“aspzincins”, although peptidases in which the third ligand of zinc is Asp also occur in families M6, M7 and M64.
  • Metalloproteases can be derived from animals, plants, bacteria or fungi. Suitable metalloprotease can be selected from the group of neutral metalloproteases and Myxobacter metalloproteases. Suitable metalloproteases can include collagenases, hemorrhagic toxins from snake venoms and thermolysin from bacteria. Preferred thermolysin enzyme variants include an M4 peptidase, more preferably the thermolysin enzyme variant is a member of the PepSY ⁇ Peptidase_M4 ⁇ Peptidase_M4_C family.
  • thermolysin enzyme variant is from a genus selected from the group consisting of Bacillus, Geobacillus, Alicyclobacillus, Lactobacillus, Exiguobacterium, Brevibacillus, Paenibacillus, Herpetosiphon, Oceanobacillus, Shewanella, Clostridium, Staphylococcus, Flavobacterium, Stigmatella, Myxococcus, Vibrio, Methanosarcina, Chryseobacterium, Streptomyces, Kribbella, Janibacter, Nocardioides, Xanthamonas, Micromonospora, Burkholderia, Dehalococcoides, Croceibacter, Kordia, Microscilla, Thermoactinomyces, Chloroflexus, Listeria, Plesiocystis, Haliscomenobacter, Cytophaga, Hahella, Arthrobacter, Brachybacterium, Clavibacter, Micro
  • thermolysin enzyme variant is from a genus selected from the group consisting of Bacillus, Geobacillus, Alicyclobacillus, Lactobacillus, Exiguobacterium, Brevibacillus, Paenibacillus, Herpetosiphon, Oceanobacillus, Shewanella, Clostridium, Staphylococcus, Flavobacterium, Stigmatella, Myxococcus, Vibrio, Methanosarcina, Chryseobacterium, and Pseudoalteromonas.
  • the metalloprotease comprises of amino acid sequence having at least 60% at least 65%, e.g., at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, but less than 100% sequence identity to a polypeptide
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 1.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 2.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 3.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 4.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 5.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 6.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 7.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 8.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 9.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 10.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 1 1.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 12.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 13.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 14.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 15.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 16.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 17.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 18.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 19.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 20.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 21.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 22.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 23.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 24.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 25.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 26.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 27.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 28.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 29.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 30.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 31.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 32.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 33.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 34
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 35.
  • the present invention relates to a metalloprotease wherein the metalloprotease comprises or consists of amino acid sequence as set forth in SEQ ID NO: 36.
  • Suitable commercially available metalloproteases enzymes include those sold under the trade names Neutrase ® by Novozymes A/S (Denmark), the Corolase ® range including Corolase ® 2TS, Corolase ® N, Corolase ® L10, Corolase ® LAP and Corolase ® 7089 from AB Enzymes, Protex 14L and Protex 15L from DuPont (Palo Alto, California), those sold as thermolysin from Sigma and the Thermoase range (PC10F and CIOO) and thermolysin enzyme from Amano enzymes.
  • the enzyme-containing composition is present in the first compartment of the multi-compartment pouch comprises a metalloprotease and further comprises one or more additional enzymes.
  • the metalloprotease comprises of amino acid sequence having at least 60% at least 65%, e.g., at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, but less
  • the enzyme-containing composition in the first compartment of the pouch is present in a liquid, solid or gel form.
  • the enzyme of the present invention in particular a metalloprotease, may be added in an amount corresponding to 0.001-100 mg of protein, such as 0.01-100 mg of protein, preferably 0.005-50 mg of protein, more preferably 0.01- 25 mg of protein, even more preferably 0.05-10 mg of protein, most preferably 0.05-5 mg of protein, and even most preferably 0.01-1 mg of protein per liter of wash liquor.
  • the detergent composition is present in the second compartment of the multi-compartment pouch.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises at least one enzyme.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprising the enzyme is preferably a DNase.
  • the detergent composition is present in the second compartment of the multi-compartment pouch comprises at least one DNase.
  • DNase means a polypeptide with DNase (deoxyribonuclease) activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in a DNA backbone, thus degrading DNA. Exodeoxyribonuclease cut or cleaves residues at the end of the DNA back bone where endo-deoxyribonucleases cleaves or cut within the DNA backbone. A DNase may cleave only double-stranded DNA or may cleave double stranded and single stranded DNA.
  • DNases and the expression “a polypeptide with DNase activity” are used interchangeably throughout the application. For purposes of the present invention, DNase activity is determined according to the procedure described in the Assay I.
  • the polypeptide having DNase activity is obtained from a microorganism and the DNase is a microbial enzyme.
  • the DNase is preferably of fungal or bacterial origin.
  • the DNase may be obtainable from Bacillus e.g. such as a Bacillus licheniformis, Bacillus subtilis, Bacillus horikoshii, Bacillus horneckiae, Bacillus cibi, Bacillus idriensis, Bacillus algicola, Bacillus vietnamensis, Bacillus hwajinpoensis, Bacillus indicus, Bacillus marisflavi or Bacillus luciferensis.
  • Bacillus e.g. such as a Bacillus licheniformis, Bacillus subtilis, Bacillus horikoshii, Bacillus horneckiae, Bacillus cibi, Bacillus idriensis, Bacillus algicola, Bacillus vietnamensis, Bacillus hwajinpoensis, Bacillus indicus, Bacillus marisflavi or Bacillus luciferensis.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises a DNase having at least 60%, at least 65%, at least 70%, at least 75% at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 60.
  • DNases obtained from Bacillus includes a polypeptide having DNase activity, wherein the polypeptide comprises an amino acid sequence having at least 60%, at least 65%, at least 70%, at least 75% at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID No: 61 and 62.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises a DNase having at least 60%, at least 65%, at least 70%, at least 75% at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 61.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises a DNase having at least 60%, at least 65%, at least 70%, at least 75% at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 62.
  • the DNase may also be fungal, preferably obtained from Aspergillus e.g. Aspergillus oryzae.
  • the pouch comprises a polypeptide having DNase activity, wherein the polypeptide comprises an amino acid sequence having at least 60%, at least 65%, at least 70%, at least 75% at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 63.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises a DNase having at least 60%, at least 65%, at least 70%, at least 75% at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 63.
  • the fungal DNase may also be obtained from Trichoderma e.g. Trichoderma Harzianum e.g.
  • the pouch comprises a polypeptide having DNase activity, wherein the polypeptide comprises an amino acid sequence having at least 60%, at least 65%, at least 70%, at least 75% at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the polypeptide shown in SEQ ID NO: 64.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises a DNase having at least 60%, at least 65%, at least 70%, at least 75% at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 64.
  • the enzyme-containing composition present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition is present in a second compartment of a multi-compartment pouch comprises at least one DNase.
  • the enzyme-containing composition present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi-compartment pouch comprises at least one DNase, wherein the metalloprotease is classified in EC 3.4.22 or EC3.4.24.
  • the enzyme-containing composition present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi-compartment pouch comprises at least one DNase and wherein the metalloprotease is an M4, M7 or M35.
  • the enzyme-containing composition is present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi compartment pouch comprises at least one DNase, wherein the DNase is obtained from Bacillus.
  • the enzyme-containing composition is present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi compartment pouch comprises at least one DNase, wherein the DNase is obtained from Aspergillus.
  • the enzyme-containing composition is present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi compartment pouch comprises at least one DNase, wherein the DNase is obtained from Trichoderma.
  • the detergent composition is present in the second compartment of the multi-compartment pouch further comprises one or more detergent components selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric hueing agents, anti-foaming agents, dispersants, processing aids, and/or pigments.
  • surfactants selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises a surfactant.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises a surfactant and wherein the surfactant is an anionic and/or a nonionic surfactant.
  • LAS linear alkylbenzenesulfonates
  • AEO alcohol ether sulfate
  • AEOS alcohol ether sulfate
  • SLES sodium lauryl ether sulfate
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises a nonionic surfactant is selected from alcohol ethoxylates (AE or AEO), alcohol propoxylates, alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, /V-acyl N- alkyl derivatives of glucosamine (glucamides, GA, or
  • the detergent composition present in the second compartment of the multi-compartment pouch may comprise one or more surfactants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic, or a mixture thereof.
  • the detergent composition includes a mixture of one or more nonionic surfactants and one or more anionic surfactants.
  • the surfactant(s) is typically present at a level of from about 0.1 % to 60% by weight, such as about 1 % to about 40%, or about 3% to about 20%, or about 3% to about 10%.
  • the surfactant(s) is chosen based on the desired cleaning application, and may include any conventional surfactant(s) known in the art.
  • the detergent When included therein the detergent will usually contain from about 1 % to about 40% by weight of an anionic surfactant, such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant.
  • an anionic surfactant such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant.
  • Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular, linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane- 2, 3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates), secondary alkanesulfonates (S
  • the detergent When included therein the detergent will usually contain from about 1 % to about 40% by weigh of a cationic surfactant, for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%.
  • a cationic surfactant for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%.
  • Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and combinations thereof.
  • ADMEAQ alkyldimethylethanolamine quat
  • CAB cetyltrimethylammonium bromide
  • DMDMAC dimethyldistearylammonium chloride
  • AQA alkoxylated quaternary ammonium
  • the detergent When included therein the detergent will usually contain from about 0.2% to about 40% by weight of a nonionic surfactant, for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%.
  • a nonionic surfactant for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%.
  • Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof
  • the detergent When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a semipolar surfactant.
  • semipolar surfactants include amine oxides (AO) such as alkyldimethylamineoxide, N-(coco alkyl)-N,N-dimethylamine oxide and N- (tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide and combinations thereof.
  • AO amine oxides
  • the detergent When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a zwitterionic surfactant.
  • zwitterionic surfactants include betaines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.
  • the detergent composition present in the second compartment of the multi-compartment pouch preferably comprises surfactant in an amount to provide from 0.001 ppm to 5,000 ppm surfactant in the wash liquor during the laundering process.
  • the detergent composition is present in the second compartment of the multi-compartment pouch comprises a builder.
  • the etergent composition present in the second compartment of the multi-compartment pouch comprises a builder, wherein the builder is selected from a group consisting of phosphates, sodium citrate builders, sodium carbonate, sodium silicate, sodium and zeolites.
  • the detergent composition present in the second compartment of the multi-compartment pouch may contain about 0-65% by weight, such as about 5% to about 50% of a detergent builder or co-builder, or a mixture thereof.
  • the level of builder is typically 40-65%, particularly 50-65%.
  • the builder and/or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and/or co-builder known in the art for use in laundry/ADW/hard surface cleaning detergents may be utilized.
  • Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Hoechst), ethanolamines such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2’-iminodiethan-1-ol), triethanolamine (TEA, also known as 2,2’,2”-nitrilotriethan-1-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.
  • zeolites such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2’-iminodiethan-1-ol), triethanolamine (TEA, also known as 2,2’,2”-nitrilotriethan-1-ol), and (carboxymethyl)inulin (
  • the detergent composition present in the second compartment of the multi-compartment pouch may also contain 0-50% by weight, such as about 5% to about 30%, of a detergent co-builder.
  • the detergent composition may comprise a co-builder alone, or in combination with a builder, for example a zeolite builder.
  • co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA).
  • PAA/PMA poly(acrylic acid)
  • Further non-limiting examples include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid.
  • NTA 2,2’,2”-nitrilotriacetic acid
  • EDTA ethylenediaminetetraacetic acid
  • DTPA diethylenetriaminepentaacetic acid
  • IDS iminodisuccinic acid
  • EDDS ethylenediamine-N,N’-disuccinic acid
  • MGDA methylglycinediacetic acid
  • GLDA glutamic acid- N,N-diacetic acid
  • HEDP 1-hydroxyethane-1 ,1-diphosphonic acid
  • EDTMPA ethylenediaminetetra(methylenephosphonic acid)
  • DTMPA or DTPMPA diethylenetriaminepentakis(methylenephosphonic acid)
  • EDG N-(2- hydroxyethyl)iminodiacetic acid
  • ASMA aspartic acid-N-monoacetic acid
  • ASDA aspartic acid-N,N- diacetic acid
  • ASMP aspartic acid-N-monopropionic
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more hydrotrope.
  • a hydrotrope is a compound that solubilises hydrophobic compounds in aqueous solutions (or oppositely, polar substances in a non-polar environment).
  • hydrotropes typically have both hydrophilic and a hydrophobic character (so-called amphiphilic properties as known from surfactants); however the molecular structure of hydrotropes generally do not favor spontaneous self-aggregation, see e.g., review by Hodgdon and Kaler (2007), Current Opinion in Colloid & Interface Science 12: 121-128. Hydrotropes do not display a critical concentration above which self-aggregation occurs as found for surfactants and lipids forming miceller, lamellar or other well defined meso-phases.
  • hydrotropes show a continuous-type aggregation process where the sizes of aggregates grow as concentration increases.
  • many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing substances of polar and non-polar character, including mixtures of water, oil, surfactants, and polymers.
  • Hydrotropes are classically used across industries from pharma, personal care, food, to technical applications.
  • Use of hydrotropes in detergent compositions allow for example more concentrated formulations of surfactants (as in the process of compacting liquid detergents by removing water) without inducing undesired phenomena such as phase separation or high viscosity.
  • the detergent present in the second compartment of the multi-compartment pouch may contain 0-10% by weight, such as about 0.5 to about 5%, or about 3% to about 5%, of a hydrotrope. Any hydrotrope known in the art for use in detergents may be utilized.
  • Non-limiting examples of hydrotropes include sodium benzene sulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more bleaching system.
  • the detergent composition present in the second compartment of the multi-compartment pouch may contain 0-30% by weight, such as about 1 % to about 20%, of a bleaching system.
  • a bleaching system Any bleaching system known in the art for use in laundry/ADW/hard surface cleaning detergents may be utilized. Suitable bleaching system components include sources of hydrogen peroxide; sources of peracids; and bleach catalysts or boosters.
  • Suitable sources of hydrogen peroxide are inorganic persalts, including alkali metal salts such as sodium percarbonate and sodium perborates (usually mono- or tetra hydrate), and hydrogen peroxide— urea (1/1).
  • Peracids may be (a) incorporated directly as preformed peracids or (b) formed in situ in the wash liquor from hydrogen peroxide and a bleach activator (perhydrolysis) or (c) formed in situ in the wash liquor from hydrogen peroxide and a perhydrolase and a suitable substrate for the latter, e.g., an ester.
  • Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids such as peroxybenzoic acid and its ring-substituted derivatives, peroxy-a-naphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, e-phthalimidoperoxycaproic acid [phthalimidoperoxyhexanoic acid (PAP)], and o-carboxybenzamidoperoxycaproic acid; aliphatic and aromatic diperoxydicarboxylic acids such as diperoxydodecanedioic acid, diperoxyazelaic acid, diperoxysebacic acid, diperoxybrassylic acid, 2-decyldiperoxybutanedioic acid, and diperoxyphthalic, -isophthalic and -terephthalic acids; perimidic acids; peroxymonosulfuric acid; peroxydisulfuric acid; peroxyphosphoric acid
  • Suitable bleach activators include those belonging to the class of esters, amides, imides, nitriles or anhydrides and, where applicable, salts thereof. Suitable examples are tetraacetylethylenediamine (TAED), sodium 4-[(3, 5, 5-trimethylhexanoyl)oxy]benzene-1 -sulfonate (ISONOBS), sodium 4-(dodecanoyloxy)benzene-1 -sulfonate (LOBS), sodium 4- (decanoyloxy) benzene- 1 -sulfonate, 4-(decanoyloxy)benzoic acid (DOBA), sodium 4- (nonanoyloxy)benzene-l-sulfonate (NOBS), and/or those disclosed in W098/17767.
  • TAED tetraacetylethylenediamine
  • ISONOBS sodium 4-[(3, 5, 5-trimethylhexanoyl)oxy]benzene-1 -sulfonate
  • ATC acetyl triethyl citrate
  • ATC or a short chain triglyceride like triacetin has the advantage that they are environmentally friendly.
  • acetyl triethyl citrate and triacetin have good hydrolytical stability in the product upon storage and are efficient bleach activators.
  • ATC is multifunctional, as the citrate released in the perhydrolysis reaction may function as a builder.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more bleach catalyst and/or booster.
  • the bleaching system may also include a bleach catalyst or booster.
  • bleach catalysts that may be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese-collagen, cobalt-amine catalysts and manganese triazacyclononane (MnTACN) catalysts; particularly preferred are complexes of manganese with 1 ,4,7-trimethyl-1 ,4,7-triazacyclononane (Me3- TACN) or 1 ,2,4,7-tetramethyl-1 ,4,7-triazacyclononane (Me4-TACN), in particular Me3-TACN, such as the dinuclear manganese complex [(Me3-TACN)Mn(0)3Mn(Me3-TACN)](PF6)2, and [2,2',2"-nitrilotris(ethane-1 ,2-diylazanylylidene-KN-methanylylidene)triphenolato- K30]manganese(lll).
  • an organic bleach catalyst or bleach booster may be used having one of the following formulae:
  • each R1 is independently a branched alkyl group containing from 9 to 24 carbons or linear alkyl group containing from 11 to 24 carbons, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbons or linear alkyl group containing from 11 to 18 carbons, more preferably each R1 is independently selected from the group consisting of 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl.
  • Suitable bleaching systems are described, e.g. in W02007/087258, W02007/087244, W02007/087259, EP1867708 (Vitamin K) and W02007/087242.
  • Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more metal care agents.
  • Metal care agents may prevent or reduce the tarnishing, corrosion or oxidation of metals, including aluminium, stainless steel and non-ferrous metals, such as silver and copper. Suitable examples include one or more of the following:
  • benzatriazoles including benzotriazole or bis-benzotriazole and substituted derivatives thereof.
  • Benzotriazole derivatives are those compounds in which the available substitution sites on the aromatic ring are partially or completely substituted.
  • Suitable substituents include linear or branch-chain Ci-C20- alkyl groups (e.g., C1-C20- alkyl groups) and hydroxyl, thio, phenyl or halogen such as fluorine, chlorine, bromine and iodine.
  • metal salts and complexes chosen from the group consisting of zinc, manganese, titanium, zirconium, hafnium, vanadium, cobalt, gallium and cerium salts and/or complexes, the metals being in one of the oxidation states II , III, IV, V or VI.
  • suitable metal salts and/or metal complexes may be chosen from the group consisting of Mn(ll) sulphate, Mn(ll) citrate, Mn(ll) stearate, Mn(ll) acetylacetonate, K A TiF6 (e.g., K2T 6), K A ZrF6 (e.g., K2ZrF6), CoS04, Co(NOs)2 and Ce(NOs)3, zinc salts, for example zinc sulphate, hydrozincite or zinc acetate.;
  • silicates including sodium or potassium silicate, sodium disilicate, sodium metasilicate, crystalline phyllosilicate and mixtures thereof.
  • composition of the invention comprises from 0.1 to 5% by weight of the composition of a metal care agent, preferably the metal care agent is a zinc salt.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more polymers.
  • the detergent composition may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1 % of a polymer. Any polymer known in the art for use in detergents may be utilized.
  • the polymer may function as a co-builder as mentioned above, or may provide antiredeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties. Some polymers may have more than one of the above-mentioned properties and/or more than one of the below- mentioned motifs.
  • Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone- vinylimidazole (P
  • exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate.
  • PEO-PPO polypropylene oxide
  • diquaternium ethoxy sulfate diquaternium ethoxy sulfate.
  • Other exemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of the above-mentioned polymers are also contemplated.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more fabric hueing agent.
  • the detergent composition may also comprise fabric hueing agents such as dyes or pigments, which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liquor comprising said detergent compositions and thus altering the tint of said fabric through absorption/reflection of visible light.
  • fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum.
  • Suitable fabric hueing agents comprise dyes and dye- clay conjugates, and may also comprise pigments.
  • Suitable dyes comprise small molecule dyes and polymeric dyes.
  • Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.l.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in W02005/03274, W02005/03275, W02005/03276 and EP1876226 (hereby incorporated by reference).
  • the detergent composition present in the second compartment of the multi-compartment pouch preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.0001 wt% to about 0.04 wt% fabric hueing agent.
  • the detergent composition present in the second compartment of the multi compartment pouch may comprise from 0.0001 wt% to 0.2 wt% fabric hueing agent, this may be especially preferred when the composition is in the form of a unit dose pouch.
  • Suitable hueing agents are also disclosed in, e.g. WO 2007/087257 and W02007/087243.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more adjunct material.
  • any detergent components known in the art for use in laundry/ADW/hard surface cleaning detergents may also be utilized.
  • Other optional detergent components include anti-corrosion agents, anti-shrink agents, anti-soil redeposition agents, anti-wrinkling agents, bactericides, binders, corrosion inhibitors, disintegrants/disintegration agents, dyes, enzyme stabilizers (including boric acid, borates, CMC, and/or polyols such as propylene glycol), fabric conditioners including clays, fillers/processing aids, fluorescent whitening agents/optical brighteners, foam boosters, foam (suds) regulators, perfumes, soil-suspending agents, softeners, suds suppressors, tarnish inhibitors, and wicking agents, either alone or in combination.
  • Any ingredient known in the art for use in laundry/ADW/hard surface cleaning detergents may be utilized. The choice of such ingredients is well within the skill of the artisan.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more dispersants.
  • the detergent composition can also contain dispersants.
  • powdered detergents may comprise dispersants.
  • Suitable water-soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.
  • Suitable dispersants are for example described in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises 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 dye transfer inhibiting agents may be present at levels from about 0.0001 % to about 10%, from about 0.01 % to about 5% or even from about 0.1 % to about 3% by weight of the composition.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more fluorescent whitening agent.
  • the detergent composition present in the second compartment of the multi-compartment pouch will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent or optical brighterners.
  • fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention.
  • the most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulphonic acid derivatives, diarylpyrazoline derivatives and bisphenyl- distyryl derivatives. Examples of the diaminostilbene-sulphonic acid derivative type of fluorescent whitening agents include the sodium salts of:
  • Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba-Geigy AG, Basel, Switzerland.
  • Tinopal DMS is the disodium salt of 4,4'-bis-(2-morpholino-4 anilino-s-triazin-6- ylamino) stilbene disulphonate.
  • Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl) disulphonate. Also preferred are fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India. Other fluorescers suitable for use in the invention include the 1-3-diaryl pyrazolines and the 7- alkylaminocoumarins.
  • Suitable fluorescent brightener levels include lower levels of from about 0.01 , from 0.05, from about 0.1 or even from about 0.2 wt% to upper levels of 0.5 or even 0.75 wt%.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more soil release polymer.
  • the detergent composition present in the second compartment of the multi-compartment pouch may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics.
  • the soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series, volume 71 , Marcel Dekker, Inc.
  • Another type of soil release polymers is amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure.
  • the core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523.
  • random graft co-polymers are suitable soil release polymers Suitable graft co-polymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/113314.
  • Other soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose deriviatives such as those described in EP 1 867 808 or WO 2003/040279.
  • Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides and mixtures thereof.
  • Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cationically modified cellulose, zwitterionically modified cellulose, and mixtures thereof.
  • Suitable cellulosic polymers include methyl cellulose, carboxy methyl cellulose, ethyl cellulose, hydroxyl ethyl cellulose, hydroxyl propyl methyl cellulose, ester carboxy methyl cellulose, and mixtures thereof.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more anti-redeposition agents.
  • the detergent composition present in the second compartment of the multi-compartment pouch may also include one or more anti-redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and/or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimines.
  • CMC carboxymethylcellulose
  • PVA polyvinyl alcohol
  • PVP polyvinylpyrrolidone
  • PEG polyethyleneglycol
  • homopolymers of acrylic acid copolymers of acrylic acid and maleic acid
  • ethoxylated polyethyleneimines ethoxylated polyethyleneimines.
  • the cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents.
  • adjunct materials include, but are not limited to, anti-shrink agents, anti wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, structurants for liquid detergents and/or structure elasticizing agents.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more rheology modifiers.
  • the detergent composition present in the second compartment of the multi-compartment pouch may also comprise one or more rheology modifiers, structurants or thickeners, as distinct from viscosity reducing agents.
  • the rheology modifiers are selected from the group consisting of non polymeric crystalline, hydroxy-functional materials, polymeric rheology modifiers which impart shear thinning characteristics to the aqueous liquid matrix of a liquid detergent composition.
  • the rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example as shown in EP 2169040.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises one or more other suitable adjunct material.
  • suitable adjunct materials include, but are not limited to, anti-shrink agents, anti-wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and/or structure elasticizing agents.
  • the enzyme-containing present in the first compartment of the multi compartment pouch further comprises one or more additional enzymes.
  • the detergent composition present in the second compartment of the multi-compartment pouch further comprises one or more additional enzymes.
  • the enzyme-containing present in the first compartment of the multi compartment pouch further comprises one or more additional enzymes and/or the detergent composition present in the second compartment of the multi-compartment pouch further comprises one or more additional enzymes.
  • the enzyme-containing present in the first compartment of the multi compartment pouch and/or the detergent composition present in the second compartment of the multi-compartment pouch comprises an additional enzyme selected from the group consisting of an alpha-amylase, a beta-amylase, a protease, a pullulanase, a lipase, a cellulase, an oxidase, a phospholipase, a perhydrolase, a xylanase, a pectate lyase, a pectinase, a galacturanase, a hemicellulase, a xyloglucanase, a nuclease, a mannanase and mixtures thereof.
  • an additional enzyme selected from the group consisting of an alpha-amylase, a beta-amylase, a protease, a pullulanase, a lipase, a cellula
  • the properties of the selected enzyme(s) should be compatible with the selected detergent, (i.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.
  • Suitable cellulases comprise those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691 , 178, US 5,776,757 and WO 89/09259.
  • cellulases are the alkaline or neutral cellulases having colour care benefits.
  • Examples of such cellulases are cellulases described in EP 0 495 257, EP 0 531 372, WO 96/1 1262, WO 96/29397, WO 98/08940.
  • Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471 , WO 98/12307 and W099/001544.
  • cellulases are endo-beta-1 ,4-glucanase enzyme having a sequence of at least 97% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO:2 of WO 2002/099091 or a family 44 xyloglucanase, which a xyloglucanase enzyme having a sequence of at least 60% identity to positions 40-559 of SEQ ID NO: 2 of WO 2001/062903.
  • cellulases include CelluzymeTM, and CarezymeTM (Novozymes A/S) Carezyme PremiumTM (Novozymes A/S), Celluclean TM (Novozymes A/S), Celluclean ClassicTM (Novozymes A/S), CellusoftTM (Novozymes A/S), WhitezymeTM (Novozymes A/S), ClazinaseTM, and Puradax HATM (Genencor International Inc.), and KAC-500(B)TM (Kao Corporation).
  • Cellulase in particular an enzyme exhibiting endo-beta-1 ,4-glucanase activity.
  • Cellulose is a polymer of glucose linked by beta-1 ,4-glucosidic bonds. Cellulose chains form numerous intra- and intermolecular hydrogen bonds, which results in the formation of insoluble cellulose micro-fibrils.
  • Microbial hydrolysis of cellulose to glucose involve three major classes of cellulases: (i) endo-glucanases (EC 3.2.1.4) which cleave beta-1 , 4-glucosidic links randomly throughout cellulose molecules, also called endo-beta-1 ,4-glucanases; (ii) cellobiohydrolases (EC 3.2.1.91) which digest cellulose from the non-reducing end, releasing cellobiose; and (iii) beta-glucosidases (EC 3.2.1.21) which hydrolyse cellobiose and low molecular-weight cellodextrins to release glucose.
  • endo-glucanases EC 3.2.1.4
  • cellobiohydrolases EC 3.2.1.91
  • beta-glucosidases EC 3.2.1.21 which hydrolyse cellobiose and low molecular-weight cellodextrins to release glucose.
  • the cellulases useful in the cleaning composition of the invention are preferably endo- glucanases (EC 3.2.1.4). Beta-1 , 4-glucosidic bonds are also present beta-glucans from plants such as barley and oats. In some cases, endo-glucanases also provide hydrolysis of such non cellulose polymers.
  • the cellulases are placed into different families of glycosyl hydrolases; fungal and bacterial glycosyl hydrolases have been grouped into 35 families (Henrissat, B.: A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 (1991), 309-316.
  • Cellulases are synthesized by a large number of microorganisms which include fungi, actinomycetes, myxobacteria and true bacteria but also by plants. Especially endo-beta-1 ,4-glucanases of a wide variety of specificities have been identified. Many bacterial endo-glucanases have been described (Gilbert, H.J. and Hazlewood, G.P. (1993) J. Gen. Microbiol. 139:187-194. Henrissat, B., and Bairoch, A.: New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293 (1993), 781 - 788.).
  • One preferred cellulase includes endo-beta-1 ,4-glucanase activity (EC 3.2.1.4), preferably obtained from Bacillus sp. AA349 (DSM 12648), as described in W02002/099091.
  • Other preferred cellulases include those described in W01996/029397, which discloses family 45 endoglucanases e.g. cellulases from Thielavia in particular a strain of Thielavia terrestris and the cellulases described in WO1991/017243, which discloses endoglucanases from e.g. of Humicola such as Humicola insolens.
  • the detergent composition in the second compartment of the pouch comprises a cellulase selected from the group consisting of:
  • Bacillus subtilis c) a cellulase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 47, preferably obtained from Humicola insolens ; and d) a cellulase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 48, preferably obtained from Thielavia terrestris.
  • Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • the mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens.
  • Suitable mannanases are described in WO 1999/064619.
  • the detergent composition in the second compartment of the pouch comprises a mannanase selected from the group consisting of:
  • a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 50, preferably from Bacillus e.g. Bacillus bogoriensis ;
  • mannanase wherein the mannanase belongs to the Glycoside Hydrolase Family 26 mannanases;
  • a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 51 , preferably obtained from Paenibacillus woosongensis;
  • a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 52, preferably obtained from Paenibacillus illinoisensis ⁇ ,
  • a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 53, preferably obtained from Neobulgaria sp.;
  • a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 54, preferably obtained from Preussia aemulans ;
  • a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 56, preferably obtained from Myrothecium roridunr,
  • a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 57, preferably obtained from Chaetomium brasiliense ;
  • a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 58, preferably obtained from Ascobolus stictoideus ;
  • a mannanase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 59, preferably obtained from Chaetomium virescens.
  • mannanase A commercially available mannanase is Mannaway (Novozymes A/S). Lipases and Cutinases:
  • Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96/13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp.
  • Thermomyces e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216
  • cutinase from Humicola e.g. H
  • strain SD705 (W095/06720 & W096/27002), P. wisconsinensis (WO96/12012), GDSL-type Streptomyces lipases (W010/065455), cutinase from Magnaporthe grisea (W010/107560), cutinase from Pseudomonas mendocina (US5,389,536), lipase from Thermobifida fusca (W011/084412), Geobacillus stearothermophilus lipase (W011/084417), lipase from Bacillus subtilis (W011/084599), and lipase from Streptomyces griseus (WO11/150157) and S. pristinaespiralis (W012/137147).
  • lipase variants such as those described in EP407225, WO92/05249, WO94/01541 , WO 94/25578, W095/14783, WO95/30744, W095/35381 , W095/22615,
  • the detergent composition in the second compartment of the pouch comprises a lipase selected from the group consisting of:
  • a lipase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 49, wherein the lipase comprises one or both the substitutions T231 R and/or N233R, wherein the position corresponds to the positions of SEQ ID NO 49.
  • Preferred commercial lipase products include LipolaseTM, LipexTM; LipolexTM and LipocleanTM (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades).
  • lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10/1 11 143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (W010/100028).
  • Suitable proteases include those of bacterial, fungal, plant, viral or animal origin e.g. vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease. A serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as subtilisin.
  • subtilases refers to a sub-group of serine protease according to Siezen et al., Protein Engng. 4 (1991) 719-737 and Siezen et al. Protein Science 6 (1997) 501-523.
  • Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate.
  • the subtilases may be divided into 6 sub-divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
  • subtilases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and W009/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN’, subtilisin 309, subtilisin 147 and subtilisin 168 described in WO89/06279 and protease PD138 described in (WO93/18140).
  • Bacillus lentus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and W009/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniform
  • proteases may be those described in WO 92/175177, WO 01/016285, WO 02/026024 and WO 02/016547.
  • trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270, WO 94/25583 and WO 05/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 05/052161 and WO 05/052146.
  • a further preferred protease is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO 95/23221 , and variants thereof which are described in WO 92/21760, WO 95/23221 , EP 1921147 and EP 1921148.
  • WO 92/19729 examples include the variants described in: WO 92/19729, WO 96/034946, WO 98/201 15, WO 98/201 16, WO 99/011768, WO 01/44452, WO 03/006602, WO 04/03186, WO 04/041979, WO 07/006305, WO 1 1/036263, WO 11/036264, especially the variants with substitutions in one or more of the following positions: 3, 4, 9, 15, 24, 27, 42, 55, 59, 60, 66, 74, 85, 96, 97, 98, 99, 100, 101 , 102, 104, 1 16, 1 18, 121 , 126, 127, 128, 154, 156, 157, 158, 161 , 164, 176, 179, 182, 185, 188, 189, 193, 198, 199, 200, 203, 206, 211 , 212, 216, 218, 226, 229, 230
  • subtilase variants may comprise the mutations: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, N85S, N85R, , G96S, G96A, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V102I, V102Y, V102N, S104A, G1 16V, G1 16R, H118D, H118N, N120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M
  • the protease variants are preferably variants of the Bacillus lentus protease (Savinase®) shown in SEQ ID NO 1 of WO 2016/001449, the Bacillus amyloliquefaciens protease (BPN’) shown in SEQ ID NO 2 of W02016/001449.
  • the protease variants preferably have at least 80 % sequence identity to SEQ ID NO 1 or SEQ ID NO 2 of WO 2016/001449.
  • a protease variant comprising a substitution at one or more positions corresponding to positions 171 , 173, 175, 179, or 180 of SEQ ID NO: 1 of W02004/067737, wherein said protease variant has a sequence identity of at least 75% but less than 100% to SEQ ID NO: 1 of WO 2004/067737.
  • Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, Duralase Tm , Durazym Tm , Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Everlase® and Esperase® (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect Ox®, Purafect OxP®, Puramax®, FN2®, FN3®, FN4®, Excellase®, Excellenz P1000TM, Excellenz P1250TM, Eraser®, Preferenz P100TM, Pur
  • amylases include alpha-amylases and/or glucoamylases and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1 ,296,839.
  • Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 211 , 243, 264, 304, 305, 391 , 408, and 444.
  • amylases having SEQ ID NO: 6 in WO 02/010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6.
  • Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.
  • amylases which are suitable are hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90% sequence identity thereof.
  • Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181 , N 190, M197, 1201 , A209 and Q264.
  • hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36- 483 of SEQ ID NO: 4 are those having the substitutions:
  • amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99/019467 or variants thereof having 90% sequence identity to SEQ ID NO: 6.
  • Preferred variants of SEQ ID NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181 , G182, H183, G184, N195, I206, E212, E216 and K269.
  • Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184.
  • Additional amylases which can be used are those having SEQ ID NO: 1 , SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96/023873 or variants thereof having 90% sequence identity to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7.
  • Preferred variants of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181 , 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96/023873 for numbering. More preferred variants are those having a deletion in two positions selected from 181 , 182, 183 and 184, such as 181 and 182, 182 and 183, or positions 183 and 184.
  • amylase variants of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.
  • Other amylases which can be used are amylases having SEQ ID NO: 2 of WO 08/153815, SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01/66712.
  • Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201 , 207, 21 1 and 264.
  • amylases having SEQ ID NO: 2 of WO 09/061380 or variants having 90% sequence identity to SEQ ID NO: 2 thereof.
  • Preferred variants of SEQ ID NO: 2 are those having a truncation of the C-terminus and/or a substitution, a deletion or an insertion in one of more of the following positions: Q87, Q98, S125, N128, T131 , T165, K178, R180, S181 , T182, G183, M201 , F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475.
  • More preferred variants of SEQ ID NO: 2 are those having the substitution in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131 I, T165I, K178L, T182G, M201 L, F202Y, N225E.R, N272E.R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/or deletion in position R180 and/or S181 or of T182 and/or G183.
  • Most preferred amylase variants of SEQ ID NO: 2 are those having the substitutions:
  • variants are C-terminally truncated and optionally further comprises a substitution at position 243 and/or a deletion at position 180 and/or position 181.
  • amylases having SEQ ID NO: 1 of W013184577 or variants having 90% sequence identity to SEQ ID NO: 1 thereof.
  • Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: K176, R178, G179, T180, G181 , E187, N 192, M199, I203, S241 , R458, T459, D460, G476 and G477.
  • More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241 QADN, R458N, T459S, D460T, G476K and G477K and/or deletion in position R178 and/or S179 or of T180 and/or G181.
  • Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
  • variants optionally further comprise a substitution at position 241 and/or a deletion at position 178 and/or position 179.
  • amylases having SEQ ID NO: 1 of W010104675 or variants having 90% sequence identity to SEQ ID NO: 1 thereof.
  • Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: N21 , D97, V128 K177, R179, S180, 1181 , G182, M200, L204, E242, G477 and G478.
  • SEQ ID NO: 1 More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: N21 D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K and G478K and/or deletion in position R179 and/or S180 or of 1181 and/or G182. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
  • variants optionally further comprise a substitution at position 200 and/or a deletion at position 180 and/or position 181.
  • amylases are the alpha-amylase having SEQ ID NO: 12 in WO01/66712 or a variant having at least 90% sequence identity to SEQ ID NO: 12.
  • Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO: 12 in WO01/66712: R28, R1 18, N174; R181 , G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471 , N484.
  • Particular preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R1 18K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions.
  • amylase variants such as those described in WO2011/098531 , WO2013/001078 and WO2013/001087.
  • the detergent composition in the second compartment of the pouch comprises an amylase selected from the group consisting of:
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 39, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 39, comprising a two amino acid deletion in the sequence region R181 , G182, D183, G184 compared to SEQ ID NO:
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 39, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 39 comprising an alteration at one or more, preferably at all of the position(s) selected from 3, 4, 5, 1 18, 167, 170, 177, 195, 202, 204, 271 , 320, 330, 377, 385, 445, 458, 475, 476, 314, 315 or 316, compared to SEQ ID NO: 39, wherein each position corresponds to the position in SEQ ID NO: 39;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 41 , or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 41 , comprising a two amino acid deletion in the sequence region R181 , G182, D183, G184, compared to SEQ ID NO:
  • each position corresponds to the position in SEQ ID NO: 41 ;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 41 , or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 41 , comprising one or more, preferably all of the alterations selected from the group consisting of
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 42, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 42, comprising one or more, preferably all of the alterations selected from the group consisting of
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 43, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 43, comprising a two amino acid deletion in the sequence region R181 , G182, H183, G184, compared to SEQ ID NO: 43, wherein each position corresponds to the position in SEQ ID NO: 43;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 43, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 43, comprising one or more, preferably all of the alterations selected from the group consisting of
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 44, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 44, comprising a two amino acid deletion in the sequence region R181 , G182, G182, D183, compared to SEQ ID NO: 44, wherein each position corresponds to the position in SEQ ID NO: 44;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 44, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 44, comprising one or more, preferably all of the alterations selected from the group consisting of
  • amylases are DuramylTM, TermamylTM, FungamylTM, Stainzyme TM, Stainzyme PlusTM, NatalaseTM, Liquozyme X and BANTM (from Novozymes A/S), and RapidaseTM, PurastarTM/EffectenzTM, Powerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Genencor International Inc./DuPont).
  • Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinopsis, e.g., from C. cinerea (EP 179,486), and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.
  • a suitable peroxidase includes a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions.
  • Chloroperoxidases (E.C. 1.1 1.1.10) catalyze formation of hypochlorite from chloride ions.
  • the haloperoxidase is a vanadium haloperoxidase, i.e. , a vanadate-containing haloperoxidase.
  • Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
  • Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.
  • a suitable oxidase includes in particular, any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1), an o- aminophenol oxidase (EC 1.10.3.4), or a bilirubin oxidase (EC 1.3.3.5).
  • Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N.
  • thermophilum Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2238885).
  • Suitable examples from bacteria include a laccase derivable from a strain of Bacillus.
  • a laccase derived from Coprinopsis or Myceliophthora is preferred; in particular, a laccase derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora thermophila, as disclosed in WO 95/33836.
  • Suitable nucleases include deoxyribonucleases (DNases) and ribonucleases (RNases) which are any enzyme that catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA or RNA backbone respectively, thus degrading DNA and RNA.
  • DNases deoxyribonucleases
  • RNases ribonucleases
  • Exonucleases digest nucleic acids from the ends. Endonucleases act on regions in the middle of target molecules.
  • the detergent composition present in the second compartment of the multi-compartment pouch is a solid or liquid detergent composition.
  • the detergent composition present in the second compartment of the multi-compartment pouch is selected from a group comprising: liquid detergents, gel detergents, powder detergents, granule detergents.
  • the detergent composition present in the second compartment of the multi-compartment pouch is an anionic detergent composition, cationic detergent composition or non-ionic composition and zwitterionic detergent composition.
  • the detergent composition present in the second compartment of the multi-compartment pouch provided herein are typically formulated such that, during use in aqueous cleaning operations, the wash water has a pH of from about 5.0 to about 1 1.5, or in alternative embodiments, even from about 6.0 to about 10.5, such as from about 5 to about 11 , from about 5 to about 10, from about 5 to about 9, from about 5 to about 8, from about 5 to about 7, from about 6 to about 1 1 , from about 6 to about 10, from about 6 to about 9, from about 6 to about 8, from about 6 to about 7, from about 7 to about 11 , from about 7 to about 10, from about 7 to about 9, or from about 7 to about 8.
  • granular or liquid laundry products are formulated such that the wash water has a pH from about 5.5 to about 1 1.
  • 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.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch and detergent composition present in the second compartment of the multi-compartment pouch may comprise low amount of water.
  • composition present in the first compartment of the multi compartment pouch contains no water or only traces of water.
  • Enzyme components weights are based on total active protein. All percentages and ratios are calculated by weight unless otherwise indicated. All percentages and ratios are calculated based on the total composition unless otherwise indicated. In the exemplified detergent composition, the enzymes levels are expressed by pure enzyme by weight of the total composition and unless otherwise specified, the detergent ingredients are expressed by weight of the total composition.
  • the enzyme(s) of the invention may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in, for example, WO92/19709 and WO92/19708.
  • a polyol such as propylene glycol or glycerol
  • a sugar or sugar alcohol lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid
  • Non-limiting examples of useful compositions in the multi-compartment pouch include light duty and heavy-duty liquid detergent compositions, hard surface cleaning compositions, fabric enhancers, detergent gels commonly used for laundry, and bleach and laundry additives, shampoos, body washes, and other personal care compositions.
  • Compositions of use in the present pouches may take the form of a liquid, solid or a powder.
  • Liquid compositions may comprise a solid.
  • Solids may include powder or agglomerates, such as micro-capsules, beads, noodles or one or more pearlized balls or mixtures thereof. Such a solid element may provide a technical benefit, through the wash or as a pre-treat, delayed or sequential release component.
  • the choice of additional components is within the skill of the artisan and includes conventional ingredients, including the exemplary non-limiting components set forth below.
  • the choice of components may include, for fabric care, the consideration of the type of fabric to be cleaned, the type and/or degree of soiling, the temperature at which cleaning is to take place, and the formulation of the detergent product.
  • the present invention also relates to a method of releasing enzyme in a cleaning process.
  • the present invention relates to a method of releasing enzymes in a cleaning process comprising steps of: a. providing a multicompartment pouch with at least two compartments the first comprising at least one enzyme containing composition and the second at least one detergent composition, b. releasing of the detergent composition from the second compartment during the main-wash cycle and subsequently releasing the enzyme from the first compartment into the wash liquor.
  • the multicompartment pouch with at least two compartments the first comprising an enzyme-containing composition and the second compartment comprising a detergent composition.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprises a protease.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprises a metal loprotease.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprises a metalloprotease selected from a group consisitng of EC classes EC 3.4.22 or EC3.4.24.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprising the metalloprotease is selected from a group consisting of a. a thermolysin and/or variant thereof; b. a metalloprotease from M4 family, that is not a thermolysin and variant thereof; c. a metalloprotease from the M7 family; and d. a metalloprotease from the M35 metalloprotease.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprises of at least one metalloprotease having amino acid sequence having at least 60% at least 65%, e.g., at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, but less than 100% sequence identity to a polypeptide selected from the group consisting of SEQ
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch comprises or consists of metalloprotease having amino acid sequence having at least 60% at least 65%, e.g., at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, but less than 100% sequence identity to a polypeptide selected from the group consisting of SEQ
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch further comprises one or more additional enzymes.
  • the detergent composition is present in the second compartment of the multi-compartment pouch.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises at least one enzyme.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprising the enzyme is preferably a DNase.
  • the detergent composition present in the second compartment of the multi-compartment pouch comprises at least one DNase.
  • the enzyme-containing composition present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition is present in a second compartment of a multi-compartment pouch comprises at least one DNase.
  • the enzyme-containing composition present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and further one or more additional enzymes and the detergent composition is present in a second compartment of a multi-compartment pouch comprises at least one DNase.
  • the enzyme-containing composition present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition is present in a second compartment of a multi-compartment pouch comprises at least one DNase and further one or more additional enzymes.
  • the enzyme-containing composition present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and further one or more additional enzymes and the detergent composition is present in a second compartment of a multi-compartment pouch comprises at least one DNase and further one or more additional enzymes.
  • the enzyme-containing composition present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi-compartment pouch comprises at least one DNase, wherein the metalloprotease is classified in EC 3.4.22 or EC3.4.24.
  • the enzyme-containing composition present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi-compartment pouch comprises at least one DNase and wherein the metalloprotease is an M4, M7 or M35.
  • the enzyme-containing composition is present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi compartment pouch comprises at least one DNase, wherein the DNase is obtained from Bacillus.
  • the enzyme-containing composition is present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi compartment pouch comprises at least one DNase, wherein the DNase is obtained from Aspergillus.
  • the enzyme-containing composition is present in a first compartment of a multi-compartment pouch comprises at least one metalloprotease and the detergent composition present in a second compartment of a multi compartment pouch comprises at least one DNase, wherein the DNase is obtained from Trichoderma.
  • the multi-compartment pouch is suitable for delivering different compositions at different points in time of the wash-cycle of a laundry or automatic dishwashing machine. Difference in solubility can be achieved by means of films of different thickness or films which solubility is temperature dependent.
  • the detergent composition present in the second compartment of the multi-compartment pouch is first released into the water containing in the washing machine or in the dishwashing machine to form a washing liquor/a dishwashing liquor comprising water and the laundry to be washed and cleaned or the dishes to be cleaned to said washing liquor or dishwashing liquor.
  • the enzyme-containing composition in the first compartment of the multi-compartment pouch is subsequently released i.e after the release of the detergent composition in the second compartment of the multi-compartment pouch into washing liquor contained in the washing machine together with the laundry to be washed and cleaned or into the dishwashing liquor contained in the dishwashing machine together with the dishes to be cleaned.
  • the films enclosing the enzyme-containing composition dissolves after to the films enclosing the detergent composition in the multi compartment pouch during the main-wash cycle of a washing machine, thereby releasing the enzyme-containing composition into the wash liquor after the delivery of the detergent composition.
  • the pouch provides excellent cleaning.
  • the detergent composition in the multi compartment pouch will react in water to release its contents before the enzyme-containing composition in the multi-compartment pouch.
  • the detergent composition may be more water-soluble than the enzyme-containing composition. This can for example be achieved by using different type of material for the detergent compartment and enzyme compartment of the pouch, for example, the detergent compartment is made of a material having a different type of polymer, different plasticizer, different levels components in the material, different coating of the film material, different thickness of the film material.
  • the multi-compartment pouch according to the invention can be used advantageously for washing and cleaning of textiles or for automatic dishwashing and preferably for removing enzyme-sensitive and bleachable soiling’s on textiles.
  • the enzyme-containing composition present in the first compartment of the multi-compartment pouch is at a concentration of 0.01 to 100 ppm, preferably 0.05 to 80 ppm, most preferably 0.05 to 20 ppm.
  • the present invention relates to a method of cleaning a fabric, a dishware or hard surface with a multi-compartment pouch comprising enzyme and detergent composition.
  • a preferred embodiment concerns a method of cleaning, said method comprising the steps of: contacting a fabric or object with a composition comprising a metalloprotease under conditions suitable for cleaning said fabric or object.
  • a method for removing stains from fabric which comprises contacting said a fabric with a composition comprising a metalloprotease under conditions suitable for cleaning said object.
  • the detergent pouch of the present invention is ideally suited for use in laundry applications. Accordingly, the present invention includes a method for laundering a fabric. The method comprises the steps of contacting a fabric to be laundered with the detergent pouch according to the invention.
  • the method of the present invention comprises a step of contacting the fabric with an aqueous wash liquor.
  • the aqueous wash liquor is formed by the addition of a detergent composition to water.
  • the detergent composition added to water to form the aqueous wash liquor.
  • the fabric may be contacted with the composition in a hand washing step or even a wash liquor in a machine wash cycle.
  • step (b) the enzyme is delivered during the main wash cycle wherein the fabric may be washed in a conventional wash step in which an aqueous wash liquor is formed by the addition of a detergent composition to water.
  • wash cycle settings for automatic washing machines generally have somewhat similar parameters of wash time and wash temperature.
  • "Regular” wash cycle settings in the United States are generally between about 12 minutes to about 18 minutes at about 33 C to about 43 C ("Warm” setting), while those in European washing machines generally are between about 100 minutes to about 140 minutes (“Normal” setting) at about 40 ° C to about 60 C.
  • Wash settings in Asia generally are about 15 minutes at about 25 C.
  • the enzyme-containing composition in first compartment of the multi-compartment pouch is released at least 30 seconds later than the detergent composition present in the second compartment releases of the multi-compartment pouch.
  • the method of cleaning comprising contacting a surface and/or a fabric with the multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition.
  • the method for removing and/or reducing soil and/or for reducing redeposition on a surface and/or textile comprising contacting the surface and/or textile with multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition.
  • the method of dishwashing in an automatic dishwashing machine comprising the steps of placing the multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition into the product dispenser and releasing it during the wash cycle.
  • the method of treating a fabric and/or textile comprising contacting the fabric and/or textile with the multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition.
  • the present invention relates to a method of treating a substrate, where the method includes the step of contacting the substrate with the multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme- containing composition and a second compartment comprises a detergent composition in the presence of water, wherein the substrate is a fabric or a hard surface.
  • a method of cleaning comprising contacting a surface and/or a fabric with the multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition.
  • the present invention relates to a method for removing and/or reducing soil and/or for reducing redeposition on a surface and/or textile comprising contacting the surface and/or textile with the pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition.
  • a method of laundering or dishwashing in a washing machine comprising the steps of placing the multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme- containing composition and a second compartment comprises a detergent composition into the product dispenser and releasing it during the wash cycle.
  • the present invention relates to a use of a multi-compartment pouch in a cleaning process.
  • the soils and stains that are important for detergent formulators are composed of many different substances, and a range of different enzymes, all with different substrate specificities have been developed for use in detergents both in relation to laundry and hard surface cleaning. These enzymes are considered to provide an enzyme detergency benefit, since they specifically improve stain removal in the cleaning process they are applied in as compared to the same process without enzymes.
  • a multi-compartment pouch in a cleaning process, such as laundry, hard surface cleaning, dish wash or automated dish wash.
  • a multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition for cleaning of an item, wherein the item is a textile or a surface.
  • a multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition for removing or releasing a stain from a textile having a stain.
  • the present invention concerns the use of metalloproteases in detergent compositions and cleaning processes, such as laundry and hard surface cleaning.
  • the present invention demonstrates the detergency effect of a variety of exemplary metalloproteases on various stains and under various conditions.
  • the cleaning process or the textile care process may for example be a laundry process, a dishwashing process or cleaning of hard surfaces such as bathroom tiles, floors, table tops, drains, sinks and washbasins.
  • Laundry processes can for example be household laundering, but it may also be industrial laundering.
  • the invention relates to a process for laundering of fabrics and/or garments where the process comprises treating fabrics with a washing solution containing a detergent composition, and at least one metalloprotease.
  • the cleaning process or a textile care process can for example be carried out in a machine-washing process or in a manual washing process.
  • the washing solution can for example be an aqueous washing solution containing a detergent composition.
  • the fabrics and/or garments subjected to a washing, cleaning or textile care process of the present invention may be conventional washable laundry, for example household laundry.
  • the major part of the laundry is garments and fabrics, including knits, woven, denims, non-woven, felts, yarns, and towelling.
  • the fabrics may be cellulose based such as natural cellulosics, including cotton, flax, linen, jute, ramie, sisal or coir or manmade cellulosics (e.g., originating from wood pulp) including viscose/rayon, ramie, cellulose acetate fibers (tricell), lyocell or blends thereof.
  • the fabrics may also be non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymer such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blend of cellulose based and non-cellulose based fibers.
  • non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymer such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blend of cellulose based and non-cellulose based fibers.
  • blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl alcohol fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and cellulose-containing fibers (e.g., rayon/viscose, ramie, flax, linen, jute, cellulose acetate fibers, lyocell).
  • companion material such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl alcohol fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and cellulose-containing fibers (e.g., rayon/viscose, ramie, flax, linen, jute, cellulose acetate fibers, lyocell).
  • the invention further concerns the use of multicompartment pouch in a proteinaceous stain removing processes.
  • the proteinaceous stains may be stains such as food stains, e.g., baby food, sebum, cocoa, egg, blood, milk, ink, grass, or a combination thereof.
  • a multi-compartment pouch comprising at least two compartments, wherein said first compartment comprises an enzyme-containing composition and a second compartment comprises a detergent composition.
  • protease is a metalloprotease, preferably selected from a group consisting of:
  • thermolysin variant a thermolysin variant
  • the metalloprotease comprises of amino acid sequence having at least 60%, at least 65%, e.g., at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, but less than 100% sequence identity to a polypeptide selected from the group consisting of SEQ ID Nos: 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 34, 35 and 36.
  • the metalloprotease comprises or consists of amino acid sequence as shown in SEQ ID Nos: 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 ,
  • the enzyme is preferably a DNase having at least 60 %, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 60 or SEQ ID NO:61 or SEQ ID NO:62 or SEQ ID NO:63 or SEQ ID NO:64.
  • the detergent composition further comprises one or more detergent components which is selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric hueing agents, anti-foaming agents, dispersants, processing aids, pigments and mixtures thereof.
  • detergent components which is selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents,
  • the builder is selected from a group consisting of phosphates, sodium citrate builders, sodium carbonate, sodium silicate, sodium and zeolites.
  • the surfactant is anionic and/or nonionic.
  • the anionic surfactant is selected from linear alkylbenzenesulfonates (LAS) isomers of LAS, alcohol ether sulfate (AEO, AEOS) and sodium lauryl ether sulfate and sodium laureth sulfate (SLES).
  • nonionic surfactant is selected from alcohol ethoxylates (AE or AEO), alcohol propoxylates, alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, /V-acyl /V-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FA
  • alkoxylated fatty acid alkyl esters
  • the enzyme is selected from the group consisting of an alpha-amylase, a beta-amylase, a pullulanase, a lipase, a cellulase, an oxidase, another protease, a phospholipase, a perhydrolase, a xylanase, a pectate lyase, a pectinase, a galacturanase, a hemicellulase, a xyloglucanase, a nuclease, a mannanase and mixtures thereof.
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 38, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 38, comprising a two amino acid deletion in the sequence region R178, G179, T180, G181 compared to SEQ ID NO 38, wherein each position corresponds to the position in SEQ ID NO 38;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 39 or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 39, comprising a two amino acid deletion in the sequence region R181 , G182, D183, G184 compared to SEQ ID NO 39, wherein each position corresponds to the position in SEQ ID NO 39;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 39, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 39 comprising an alteration at one or more, preferably at all of the position(s) selected from 3, 4, 5, 118, 167, 170, 177, 195, 202, 204, 271 , 320, 330, 377, 385, 445, 458, 475, 476, 314, 315 or 316, compared to SEQ ID NO 35, wherein each position corresponds to the position in SEQ ID NO 39;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 40, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 40 preferably comprising a two amino acid deletion in the sequence region R181 , G182, D183, G184, compared to SEQ ID NO 40, wherein each position corresponds to the position in SEQ ID NO 40;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 41 , or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 41 , comprising one or more, preferably all of the alterations selected from the group consisting of
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 43, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 43, comprising a two amino acid deletion in the sequence region R181 , G182, H183, G184, compared to SEQ ID NO 43, wherein each position corresponds to the position in SEQ ID NO 43;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 44, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 44, comprising one or more, preferably all of the alterations selected from the group consisting of
  • the detergent composition is selected from a group comprising: liquid detergents, solid detergents, gel detergents, powder detergents and granule detergents.
  • a method of releasing an enzyme in a cleaning process comprising steps of: a. providing a multicompartment pouch with at least two compartments, the first compartment comprising enzyme-containing composition and the second compartment comprising a detergent composition; b. releasing the detergent composition from the second compartment and subsequently releasing the enzyme-containing composition from the first compartment into the wash liquor.
  • thermolysin variant a thermolysin variant
  • metalloprotease comprises or consists of amino acid sequence as shown in SEQ ID Nos: 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 21 , 22, 23, 24, 25, 26, 27, 28, 29, 30, 31 , 32, 33, 34, 35 and 36.
  • the detergent composition comprises at least one enzyme, preferably a DNase.
  • the detergent composition further comprises one or more detergent components selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric hueing agents, anti-foaming agents, dispersants, processing aids, and/or pigments.
  • one or more detergent components selected from the group consisting of surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighten
  • anionic surfactant is selected from linear alkylbenzenesulfonates (LAS) isomers of LAS, alcohol ether sulfate (AEO, AEOS) and sodium lauryl ether sulfate and sodium laureth sulfate (SLES).
  • LAS linear alkylbenzenesulfonates
  • AEO alcohol ether sulfate
  • AEOS alcohol ether sulfate
  • SLES sodium lauryl ether sulfate and sodium laureth sulfate
  • nonionic surfactant is selected from alcohol ethoxylates (AE or AEO), alcohol propoxylates, alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA) and
  • the additional enzyme is selected from the group consisting of an alpha-amylase, a beta-amylase, a pullulanase, a lipase, a cellulase, an oxidase, another protease, a phospholipase, a perhydrolase, a xylanase, a pectate lyase, a pectinase, a galacturanase, a hemicellulase, a xyloglucanase, a nuclease, a mannanase and mixtures thereof.
  • the additional enzyme is selected from the group consisting of an alpha-amylase, a beta-amylase, a pullulanase, a lipase, a cellulase, an oxidase, another protease, a phospholipase, a perhydrolase, a xylanas
  • the enzyme is an amylase selected from the group consisting of: a) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 37, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 37 comprising a two amino acid deletion in the sequence region R180, S181 , T182, G183, compared to SEQ ID NO:
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 37, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO: 37 comprising one or preferably all the alterations sets selected from the group consisting of:
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO: 38, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 38, comprising a two amino acid deletion in the sequence region R178, G179, T180, G181 compared to SEQ ID NO
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 38, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 38, comprising one or more, preferably all of the alterations sets selected from the group consisting of:
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 39, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 39, comprising a two amino acid deletion in the sequence region R181 , G182, D183, G184 compared to SEQ ID NO 39, wherein each position corresponds to the position in SEQ ID NO 39;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 39, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 39 comprising an alteration at one or more, preferably at all of the position(s) selected from 3, 4, 5, 118, 167, 170, 177, 195, 202, 204, 271 , 320, 330, 377, 385, 445, 458, 475, 476, 314, 315 or 316, compared to SEQ ID NO 35, wherein each position corresponds to the position in SEQ ID NO 39; g) an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 40, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 40 comprising one or more, preferably all of the alterations selected from the group consisting of
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 41 , or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 41 , comprising a two amino acid deletion in the sequence region R181 , G182, D183, G184, compared to SEQ ID NO 41 , wherein each position corresponds to the position in SEQ ID NO 41 ;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 41 , or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 41 , comprising one or more, preferably all of the alterations selected from the group consisting of
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 42, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 42, comprising one or more, preferably all of the alterations selected from the group consisting of
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 43, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 43, comprising a two amino acid deletion in the sequence region R181 , G182, H 183, G184, compared to SEQ ID NO
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 43, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 43, comprising one or more, preferably all of the alterations selected from the group consisting of
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 44, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 44, comprising a two amino acid deletion in the sequence region R181 , G182, G182, D183, compared to SEQ ID NO 44, wherein each position corresponds to the position in SEQ ID NO 44;
  • an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% or 100% sequence identity to SEQ ID NO 44, or an amylase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98% but less than 100% sequence identity to SEQ ID NO 44, comprising one or more, preferably all of the alterations selected from the group consisting of
  • the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 60.
  • the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 61.
  • the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 62.
  • the DNase is fungal, preferably obtained from Aspergillus and even more preferably from Aspergillus oryzae and wherein the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 63.
  • the DNase is fungal, preferably obtained from Trichoderma and even more preferably from Trichoderma harzianum and wherein the DNase comprises a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 64.
  • a method of treating a substrate includes the step of contacting the substrate with the multi-compartment pouch of paragraphs 1-27 in the presence of water, wherein the substrate is a fabric or a hard surface.
  • a method of cleaning comprising contacting a surface and/or a fabric with the multi compartment pouch of any of the paragraphs 1-27.
  • a method for removing and/or reducing soil and/or for reducing redeposition on a surface and/or textile comprising contacting the surface and/or textile with the pouch of any of paragraphs 1-27.
  • a method of laundering or dishwashing in a washing machine comprising the steps of placing the multi-compartment pouch of any of the paragraphs 1-27 into the product dispenser and releasing it during the wash cycle.
  • 62. Use of a multi-compartment pouch according to paragraphs 1-27 for cleaning of an item, wherein the item is a textile or a surface.
  • Substrate Protazyme OL tablet (AZCL-collagen, Megazyme T-PROL 1000).
  • Assay buffers 100mM succinic acid, 100mM HEPES, 100mM CHES, 100mM CABS,
  • a Protazyme OL tablet is suspended in 2.0 ml 0.01 % Triton X-100 by gentle stirring.
  • 500 mI of this suspension and 500 mI assay buffer are dispensed in an Eppendorf tube and placed on ice.
  • 20 mI protease sample (diluted in 0.01 % Triton X-100) is added to the ice cold tube.
  • the assay is initiated by transferring the Eppendorf tube to an Eppendorf thermomixer, which is set to the assay temperature.
  • the tube is incubated for 15 minutes on the Eppendorf thermomixer at its highest shaking rate (1400 rpm). The incubation is stopped by transferring the tube back to the ice bath.
  • OD650 is read as a measure of protease activity.
  • a buffer blind is included in the assay (instead of enzyme).
  • the AMSA plate has a number of slots for test solutions and a lid firmly squeezing the laundry sample, the textile to be washed against all the slot openings. During the washing time, the plate, test solutions, textile and lid are vigorously shaken to bring the test solution in contact with the textile and apply mechanical stress in a regular, periodic oscillating manner.
  • W002/42740 especially the paragraph "Special method embodiments" at page 23-24.
  • test materials are obtained from EMPA Testmaterials AG Movenstrasse 12, CH-9015 St. Gallen, Switzerland or from Center For Testmaterials BV, P.O. Box 120, 3133 KT Vlaardingen, the Netherlands.
  • Color measurements are made with a professional flatbed scanner (Kodak iQsmart, Kodak, Midtager 29, DK-2605 Brondby, Denmark), which is used to capture an image of the washed textile.
  • RGB red, green and blue
  • Example 1 Relative wash performance of different metalloproteases
  • wash liquor a diluted detergent solution
  • a drastic performance drop is observed as only a small metalloprotease performance is detectable. It may be observed that the metalloprotease must be kept separated from the undiluted/undissolved detergent. Further, the metalloprotease should get into the wash liquor when the detergent is already diluted.
  • Table 1 shows the wash performance of the different metalloproteases from setup 1 (metalloproteases added to detergent and then after 30 min diluted with water hardness according to detergent dosage) relative to setup 2 (detergent first diluted with water hardness according to detergent dosage and then metalloproteases added) in percent.
  • Table 1 Relative wash performance of different metalloproteases

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