WO2019238761A1 - Films multicouches hydrosolubles contenant des produits chimiques et des enzymes actifs de lavage - Google Patents

Films multicouches hydrosolubles contenant des produits chimiques et des enzymes actifs de lavage Download PDF

Info

Publication number
WO2019238761A1
WO2019238761A1 PCT/EP2019/065359 EP2019065359W WO2019238761A1 WO 2019238761 A1 WO2019238761 A1 WO 2019238761A1 EP 2019065359 W EP2019065359 W EP 2019065359W WO 2019238761 A1 WO2019238761 A1 WO 2019238761A1
Authority
WO
WIPO (PCT)
Prior art keywords
acid
enzyme
layers
salts
layer
Prior art date
Application number
PCT/EP2019/065359
Other languages
English (en)
Inventor
Benjamin SCHMIDT-HANSBERG
Andreas Schroeder
Yongqing Lan
Thomas SEYFRIED
Sonja KUEBELBECK
Grit BAIER
Yannick Fuchs
Aaron Wagner
Matthias Arndt
Juergen Detering
Original Assignee
Basf Se
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 Basf Se filed Critical Basf Se
Publication of WO2019238761A1 publication Critical patent/WO2019238761A1/fr

Links

Classifications

    • 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
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B32—LAYERED PRODUCTS
    • B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
    • B32B27/00—Layered products comprising a layer of synthetic resin
    • B32B27/18—Layered products comprising a layer of synthetic resin characterised by the use of special additives
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B32—LAYERED PRODUCTS
    • B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
    • B32B27/00—Layered products comprising a layer of synthetic resin
    • B32B27/30—Layered products comprising a layer of synthetic resin comprising vinyl (co)polymers; comprising acrylic (co)polymers
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38681—Chemically modified or immobilised enzymes
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B32—LAYERED PRODUCTS
    • B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
    • B32B2250/00—Layers arrangement
    • B32B2250/24—All layers being polymeric
    • B32B2250/246—All polymers belonging to those covered by groups B32B27/32 and B32B27/30
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B32—LAYERED PRODUCTS
    • B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
    • B32B2307/00—Properties of the layers or laminate
    • B32B2307/70—Other properties
    • B32B2307/716—Degradable
    • B32B2307/7166—Water-soluble, water-dispersible
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B32—LAYERED PRODUCTS
    • B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
    • B32B2432/00—Cleaning articles, e.g. mops, wipes

Definitions

  • the present invention relates to water soluble multilayer films containing wash active chemicals and enzymes, their production and use.
  • Multilayer films for example wash active films, as described for example in unpublished patent applications PCT/EP2017/083133 and PCT/EP2017/083127, usually comprise acidic compo- nents (as mentioned in US 20160369210 A1 ).
  • wash active films described in the above publications due to their acidic nature, offer an environment which is not suitable for enzyme integration into such films.
  • laundry products usually comprise enzymes, in order to enhance washing perfor- mance.
  • laundry products have to withstand considerable storage periods (for example when a laundry product is stored in a supermarket, and subsequently in the home of a consumer), under variable storage conditions, for example varying temperatures and humidities.
  • WO2013/148492 Use of enzymes for preparing water-soluble films, enzymes+polyol for preparation of water soluble film containing PVA, PEO, glycerol, MPG, CaCh, protease; film used for unit dose products
  • W014152547 Detergent pouch with enzymatic water-soluble film, enzyme in the film is different from enzyme in the detergent (protease or lipase in film); architecture of pouch film, compartments and ingredients; several layers are described having or not having enzyme for pro tecting enzyme from detergent
  • W014186464 Stabilized Lipase in water soluble aims, water-soluble film containing lipase (sequence claimed); lipase in in solid, particulate form; film comprises 35-90% PVA with 75-99% degree of hydrolysis and 10-50% polyols; use of film for preparing a detergent unit dose product
  • a multilayer film for example a wash active multilayer film
  • incorporation of two or more enzymes into a multilayer film may present additional challenges, since some enzymes are incompatible with each other.
  • protease in case of using protease and at least one different enzyme, such as amylase, it becomes necessary to include a protease inhibitor in order to prevent rapid decomposition of the different enzyme, (see EP2799533, W014152674) This may hold true also in case of protease alone, which also decomposes itself, in the presence of water, in particular at relatively high mass fractions of protease.
  • protease inhibitors inhibit protease’s proteolytic activity, such that protease is prevented from decomposing proteins, like for example other enzymes (and itself).
  • Common protease inhibitors include boron-containing compounds. Suitable boron-containing compounds are selected from boric acid or its derivatives and from boronic acid or its derivatives such as aryl boronic acids or its derivatives, from salts thereof, and from mixtures thereof. Furthermore, peptide aldehydes like di-, tri- or tetrapeptide aldehydes or aldehyde analogues may also be used to inhibit protease.
  • protease inhibitors for example boron-containing compounds as mentioned above, lead to environmental stress and are costly.
  • an object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least one enzyme, wherein the enzyme should be stable on storage.
  • Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least two enzymes, preferably two en zymes incompatible with each other, wherein the enzymes should be stable on storage.
  • Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing protease and at least one further enzyme, wherein the enzymes should be stable on storage.
  • Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing protease and at least one further enzyme, wherein the enzymes should be stable on storage, and wherein it is possible to refrain from using a protease inhibitor.
  • an object of the present invention was to provide a water- soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least one enzyme, wherein the enzyme should be stable on storage, and wherein at least one of the films would be wash active in itself (so that additional cost and environmental stress by adding another wash-active layer can be avoided).
  • Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least one enzyme, wherein the enzyme should be stable on storage and wherein the washing and/or cleaning performance should be at least stable compared to a comparable wash and cleaning active multilayer film without any enzyme, preferably improved compared to a comparable wash and cleaning active multilayer film without any enzyme.
  • Another object of the present invention was to provide a process for manufacturing a water- soluble multilayer film, preferably a wash and cleaning active multilayer film, as described above and below.
  • the newly found multilayer concept allows for the separation of incompatible en zymes from each other, for example separation of protease and enzymes that suffer under the presence of protease, such as lipase, into at least two discrete layers, making protease inhibi tors unnecessary.
  • At least two enzymes incompatible with each other are incorporated into two discrete layers, and in addition, the two discrete layers are spatially separated by a fur ther layer devoid of any enzyme.
  • the term“polymer film” refers to a flat structure which has an essentially two-dimensional extension.
  • the thickness of the films according to the inven tion is preferably 0.5 pm to 20 mm, particularly preferably 1 pm to 10 mm.
  • the thickness of the polymer films of the invention is small in relation to the length and width.
  • the thick ness of the polymer films is smaller by a factor of at least 2, more preferably of at least 5 and especially of at least 10 than the length of the greatest longitudinal axis.
  • the thickness of the polymer films is smaller by a factor of at least 20, more specifically at least 50, even more specifically at least 100 and very specifically at least 500 than the length of the greatest longitudinal axis.
  • the upper value for the greatest longitudinal extent of the polymer films of the invention is uncritical.
  • the polymer films of the invention can be pro-losed, for example, in the form of film rolls, where the greatest length may even be in the region of 100 m or higher.
  • the polymer films of the invention can be in form of single layer films or multilayer films.
  • multi-layered film in connection with the present invention defines a self-supporting planar construction which comprises at least two film layers.
  • a multi-layered film according to the present invention is a film composite which comprises at least two films which are perma- nently connected with a substantial part of their surface over its entire surface. Thereby, it is understood that at least two films are permanently connected with at least 50% of their surface over its entire surface. If two films of different sizes are connected to each other, at least the film with the smaller surface is permanently connected over its entire surface to at least 50% of its surface.
  • the multi-layered films used in the process of the present invention differ from films used for the production of water-soluble container known in the art in which a single film or two or more films are connected by means of a seal seam. Those films known in the art are only connected over their entire surfaces to not more than 50% of their surfaces.
  • the thickness of enzyme containing layers is usually below that of today’s single layer PVA films. Due to this reduced enzyme formulation space, the enzyme concentration in the film needs to be higher compared to state of the art. Approaches as described by Monosol/Novozymes, e. g. in W013/148492 or W014/186464, cause additional challenges to enzyme stability.
  • the resulting enzyme containing wash active multilayer films shows better wash performance than enzyme containing PVOH films according to the state of the art, due to the additional wash active polymers which could not be formulated into the liquid detergent up to now (e.g. poly acrylic acid).
  • the present invention is directed at a water-soluble multilayer film comprising at least one layer comprising or consisting of a polymer composition P1) obtainable by physical blending of at least one polymer P1 ') obtainable by by free-radical polymerization of a monomer composition M’) that comprises at least one monomer A‘) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof, and at least one polyether component PE), or by free-radical polymerization of a monomer composition M1 ) comprising at least one monomer A) selected from a,b-ethylenically unsaturated mono- and dicarboxylic acids, salts of a,b-ethylenically unsaturated mono- and dicarboxylic acids, anhydrides of a,b-ethylenically unsaturated mono- and dicarboxylic acids and mixtures
  • homo- and copolymers comprising repeat units which derive from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof,
  • homo- and copolymers comprising at least one copolymerized monomer selected from N- vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole, 2-vinylpyridine, 4-vinylpyridine, salts of the three latter monomers, vinylpyridine N-oxide, N-carboxymethyl-4-vinylpyridium halides and mixtures thereof, homo- and copolymers of acrylic acid and/or methacrylic acid, especially copolymers comprising at least one copolymerized acrylic monomer selected from acrylic acid, acrylic salts and mixtures thereof, and at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof,
  • copolymers comprising at least one copolymerized (meth)acrylic monomer selected from acrylic acid, methacrylic acid, salts thereof and mixtures thereof and at least one copoly- merized hydrophobic monomer selected from C-i-Cs-alkyl esters of (meth)acrylic acid, C2-C10 olefins, styrene and a-methylstyrene,
  • copolymers comprising at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof and at least one copolymerized C2-C8 olefin,
  • polyalkylene glycols mono- or diethers of polyalkylene glycols
  • multifunctional alkoxylated diamines preferably alkoxylated diamines with 2 to 10 methylene groups
  • cellulose derivatives preferably cellulose ethers, cellulose esters, carboxyalkyl celluloses and salts thereof, sulfoalkyl celluloses and salts thereof, acidic sulfuric ester salts of cellulose, alkyl celluloses, hydroxyalkyl celluloses, hydroxyalkyl alkyl celluloses and mixtures of two or more of these cellulose derivatives
  • amphoteric modified starch and mixtures thereof,
  • At least two of the layers preferably two of the layers, comprise at least one type of enzyme EN) each.
  • the film comprises at least one layer comprising or consisting of at least one washing- and/or cleaning active polymer or polymer blend, wherein (i) the washing- and/or cleaning active polymer or polymer blend is selected from P1 ), and/or (ii) the washing- and/or cleaning active polymer or polymer blend is selected from P2).
  • the polymer P1’) can be prepared by free-radical polymerization of a monomer composition M’) that comprises at least one monomer A‘) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof, optionally at least one monomer B’) which is selected from unsaturated sulfonic acids, salts of unsaturated sulfonic acids, unsaturated phosphonic acid, salts of unsaturated phosphonic acids and mixtures thereof, and
  • Monomer composition M’ Monomer A’):
  • the monomer composition M’) used for producing the polymer P1’) comprises at least one monomer A’) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof.
  • the monomer composition M’) consists only of a,b-ethylenically un- saturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof.
  • the a,b-ethylenically unsaturated carboxylic acid is preferably selected from acrylic acid, meth- acrylic acid, ethacrylic acid, maleic acid, fumaric acid, itaconic acid, a-chloroacrylic acid, croton- ic acid, citraconic acid, mesaconic acid, glutaconic acid and aconitic acid.
  • Suitable salts of the aforementioned acids are, in particular, the sodium, potassium and ammonium salts, and the salts with amines.
  • the monomers A’) can be used as such or as mixtures with one another. The stated weight fractions all refer to the acid form.
  • the at least one a,b-ethylenically unsaturated carboxylic acid is used for the polymerization in non-neutralized form. If the a,b-ethylenically unsaturated carboxylic acids are used for the polymerization in partially neutralized form, then the acid groups are neutralized preferably to at most 50 mol%, particularly preferably to at most 30 mol%.
  • the monomer A’ is selected from acrylic acid, methacrylic acid, maleic acid, fumaric acid, itaconic acid, salts of the aforementioned carboxylic acids and mixtures thereof.
  • the monomer A’ is selected from acrylic acid, methacrylic acid, salts of acrylic acid, salts of methacrylic acid and mixtures thereof.
  • the monomer A’ is used preferably in an amount of from 50 to 100% by weight, particularly preferably 60 to 100% by weight, based on the total weight of the monomer composition M’).
  • the monomer composition M’ consists to at least 50% by weight, preferably to at least 80% by weight, in particular to at least 90% by weight, based on the total weight of the monomer composition M’), of acrylic acid and/or acrylic acid salts.
  • the monomer composition M’) can comprise, in addition to the monomers A’), at least one monomer B’) which is selected from unsaturated sulfonic acids, salts of unsaturated sulfonic acids, unsaturated phosphonic acid, salts of unsaturated phosphonic acids and mixtures there of.
  • the monomer B’) is preferably selected from 2-acrylamido-2-methylpropanesulfonic acid, vinyl- sulfonic acid, allylsulfonic acid, sulfoethyl acrylate, sulfoethyl methacrylate, sulfopropyl acrylate, sulfopropyl methacrylate, 2-hydroxy-3-acryloxypropylsulfonic acid, 2-hydroxy-3- methacryloxypropylsulfonic acid, styrenesulfonic acid, vinylphosphonic acid, allylphosphonic acid, salts of the aforementioned acids, and mixtures thereof.
  • Suitable salts of the aforementioned acids are in particular the sodium, potassium and ammoni um salts, and the salts with amines.
  • the monomers B’) can be used as such or as mixtures with one another.
  • the stated weight fractions all refer to the acid form.
  • the monomer composition M’) then consists to at least 50% by weight, particularly preferably to at least 80% by weight, in particular to at least 90% by weight, based on the total weight of the monomer composition M’), of monomers A’) and B’). If the monomer composition M’) comprises at least one monomer B’), then this is used preferably in an amount of from 0.1 to 50% by weight, particularly preferably 1 to 25% by weight, based on the total weight of the monomer composition M’).
  • the monomer composition M’) can additionally comprise at least one further monomer different from the monomers containing acid groups and salts thereof.
  • the monomer composition M’) additionally comprises at least one comonomer C’) selected from
  • x is 0, 1 or 2
  • k and I independently of one another, are an integer from 0 to 100, where the sum of k and I is at least 2, preferably at least 5,
  • R 1 is hydrogen or methyl
  • R 2 is hydrogen, C1-C4-alkyl
  • the monomer composition M’) can comprise the further monomers C1’) to C3’) in each case preferably in an amount of from 0 to 30% by weight, particularly preferably 0 to 20% by weight, in particular 0 to 10% by weight, based on the total weight of the monomer composition M’). If the monomer composition M’) comprises at least one monomer selected from C1’) to C3’), then in each case preferably in an amount of from 0.1 to 30% by weight, particularly preferably 1 to 20% by weight, in particular 1.5 to 10% by weight, based on the total weight of the monomer composition M’). In a specific embodiment, the monomer composition M’) comprises no further comonomers apart from the monomers A’).
  • Preferred nitrogen heterocycles with a free-radically polymerizable a,b-ethylenically unsaturated double bond C1’) are selected from 1-vinylimidazole (N-vinylimidazole), vinyl- and allyl-substitu- ted nitrogen heterocycles different from 1 -vinylimidazole, and mixtures thereof.
  • Suitable monomers C1’) are also the compounds obtained by protonation or quaternization of 1 - vinylimidazole and vinyl- and allyl-substituted nitrogen heterocycles different therefrom.
  • Acids suitable for the protonation are e.g. carboxylic acids, such as lactic acid, or mineral acids, such as phosphoric acid, sulfuric acid and hydrochloric acid.
  • Alkylating agents suitable for the quaternization are Ci-C4-alkyl halides or di(Ci-C4-alkyl) sulfates, such as ethyl chloride, ethyl bromide, methyl chloride, methyl bromide, dimethyl sulfate and diethyl sulfate.
  • a protonation or quaternization can generally take place either before or after the polymerization.
  • a protonation or quaternization takes place after the polymerization.
  • Examples of such charged monomers C1’) are quaternized vinylimidazoles, in particular 3-methyl-1 -vinylimidazolium chloride, methosulfate and ethosulfate.
  • Preferred monomers C1’) are furthermore vinyl- and allyl-substituted nitrogen heterocycles different from vinylimidazoles selected from 2-vinylpyridine, 4-vinylpyridine, 2-allylpyridine, 4-allyl- pyridine and the salts thereof obtained by protonation or by quaternization.
  • the monomer composition M’) comprises at least one comonomer C1’) selected from 1-vinylimidazole, 2-vinylpyridine, 4-vinylpyridine, 2-allylpyridine, 4-allylpyridine and the salts thereof obtained by protonation or by quaternization.
  • the monomer composition M’) comprises 1 -vinylimidazole as comonomer C1’).
  • Suitable amide-group-containing monomers C2’ are compounds of the general formula (II)
  • R 3 and R 4 together with the amide group to which they are bonded, can also be a lactam having 5 to 8 ring atoms,
  • R 4 and R 5 together with the nitrogen atom to which they are bonded, can also be a five- to seven-membered heterocycle.
  • the monomers C2’) are selected from primary amides of a,b-ethylenically unsaturat ed monocarboxylic acids, N-vinylamides of saturated monocarboxylic acids, N-vinyllactams, N-alkyl- and N,N-dialkylamides, a,b-ethylenically unsaturated monocarboxylic acids and mixtures thereof.
  • Preferred monomers C2’ are N-vinyllactams and derivatives thereof, which can have, e.g., one or more C1-C6-alkyl substituents, such as methyl, ethyl, n-propyl, isopropyl, n-butyl, sec-butyl, tert-butyl, etc.
  • N-vinylpyrrolidone N-vinylpiperidone, N-vinylcaprolactam
  • N-vinyl-5-methyl-2-pyrrolidone N-vinyl-5-ethyl-2-pyrrolidone
  • N-vinyl-6-methyl-2-piperidone N-vinyl-6-ethyl-2-piperidone
  • N-vinyl-7-methyl-2 -caprolactam N-vinyl-7-ethyl-2-caprolactam.
  • N-vinylpyrrolidone and/or N-vinylcaprolactam are particularly preferred.
  • Suitable monomers C2’) are furthermore acrylamide and methacrylamide.
  • N-Alkyl- and N,N-dialkylamides of a,b-ethylenically unsaturated monocarboxylic acids suitable as monomers C2’) are, for example, methyl(meth)acrylamide, methylethacrylamide, ethyl(meth)acrylamide, ethylethacrylamide, n-propyl(meth)acrylamide, isopropyl(meth)acryl- amide, n-butyl(meth)acrylamide, tert-butyl(meth)acrylamide, tert-butylethacrylamide, and mixtures thereof.
  • Open-chain N-vinylamide compounds suitable as monomers C2’ are, for example, N-vinylfor- mamide, N-vinyl-N-methylformamide, N-vinylacetamide, N-vinyl-N-methylacetamide, N-vinyl-N- ethylacetamide, N-vinylpropionamide, N-vinyl-N-methylpropionamide, N-vinylbutyramide and mixtures thereof. Preference is given to using N-vinylformamide.
  • the monomer composition M’) can additionally comprise at least one monomer C3’) selected from compounds of the general formulae (I. a) and (l.b), as defined above.
  • k is preferably an integer from 1 to 100, particularly preferably 2 to 50, in particular 3 to 30.
  • I is an integer from 0 to 50.
  • R 2 in the formulae I. a) and l.b) is hydrogen, methyl, ethyl, n-propyl, isopropyl, n- butyl, sec-butyl or tert-butyl.
  • x is preferably 1 or 2.
  • the polymer P1’ comprises less than 15% by weight, preferably less than 10% by weight, polymerized units of monomers different from monomers A’).
  • the polymer P1’) is essentially uncrosslinked.
  • the monomer composition M’) used for producing the polymer P1’) thus comprises in particular no added crosslinking monomers.
  • crosslinking monomers are compounds with two or more than two polymerizable ethylenically unsaturated double bonds per molecule.
  • the monomer composition M’ comprises, based on the total weight, less than 0.5% by weight, even more specifically less than 0.1 % by weight, of crosslinking monomers which have two or more than two free-radical ly polymerizable a,b-ethylenically unsaturated double bonds per molecule.
  • the monomer composition M’ comprises no crosslinking monomers having two or more than two polymerizable a,b-ethylenically unsaturated double bonds per molecule.
  • the polymer P1’ can be prepared by free-radical polymerization of a monomer composition M’). It is possible to work by any known free-radical polymerization process. In addition to polymerization in bulk, mention should be made especially of the processes of solution polymerization and emulsion polymerization, preference being given to solution polymerization.
  • the polymerization is preferably performed in water as a solvent. However, it can also be undertaken in alcoholic solvents, especially Ci-C4-alcohols, such as methanol, ethanol and isopropanol, or mixtures of these solvents with water.
  • alcoholic solvents especially Ci-C4-alcohols, such as methanol, ethanol and isopropanol, or mixtures of these solvents with water.
  • the free-radical polymerization of the monomer composition M’) is preferably carried out in the feed procedure.
  • at least the monomers are metered into the reaction mixture in liquid form.
  • Monomers that are liquid under the addition conditions can be introduced into the reaction mixture without adding a solvent. Otherwise the monomers are used as solution in a suitable solvent.
  • Suitable polymerization initiators are compounds which decompose thermally, by a redox mechanism or photochemically (photo initiators) to form free radicals.
  • thermal initiators having a decomposition temperature in the range from 20 to 180°C, especially from 50 to 90°C.
  • suitable thermal initiators are inorganic peroxo compounds such as perox- odisulfates (ammonium peroxodisulfate and preferably sodium peroxodisulfate), peroxosulfates, percarbonates and hydrogen peroxide; organic peroxo compounds such as diacetyl peroxide, di-tert-butyl peroxide, diamyl peroxide, 5-dioctanoyl peroxide, didecanoyl peroxide, dilauroyl peroxide, dibenzoyl peroxide, tert-butyl perneodecanoate, tert-butyl perbenzoate, tert-butyl perisobutyrate, tert-butyl perpivalate, tert-butyl
  • initiators can be used in combination with reducing compounds as initiator/regulator sys- tems.
  • reducing compounds include phosphorus compounds such as phosphorous acid, hypophosphites and phosphinates, sulfur compounds such as sodium hydrogen- sulfite, sodium sulfite and sodium formaldehyde- sulfoxylate, and hydrazine.
  • redox initiator systems which consist of a peroxo compound, a metal salt and a reducing agent.
  • peroxo compounds are hydrogen peroxide, peroxodisulfate (as the ammonium, sodium or potassium salt), peroxosulfates, and organic peroxo compounds such as tert-butyl hydroperoxide, cumene hydroperoxide or dibenzoyl per oxide.
  • Suitable metal salts are in particular iron(ll) salts such as iron(ll) sulfate heptahydrate.
  • Suitable reducing agents are sodium sulfite, the disodium salt of 2-hydroxy-2-sulfinatoacetic acid, the disodium salt of 2-hydroxy-2-sulfonatoacetic acid, sodium hydroxymethanesulfinate, ascorbic acid, isoascorbic acid or mixtures thereof.
  • photoinitiators examples include benzophenone, acetophenone, benzyl dialkyl ketones and derivatives thereof.
  • thermal initiators preferably inorganic peroxo compounds, espe cially sodium peroxodisulfate.
  • the peroxo compounds are advantageously used in combination with sulfur-containing reducing agents, especially sodium hydrogensulfite, as the redox initiator system.
  • sulfur-containing reducing agents especially sodium hydrogensulfite
  • copolymers comprising sulfonate and/or sulfate as end groups are obtained, which are notable for exceptional cleaning power and scale- inhibiting action.
  • phosphorus-containing regulator systems for example sodium hypophosphite and phosphinates.
  • initiator/regulator system should be matched to the substances used in each case. If, for example, the peroxodisulfate/ hydrogensulfite system is used, typically 1 to 7% by weight, preferably 2 to 6% by weight, of peroxodisulfate and generally 3 to 25% by weight, preferably 4 to 15% by weight, of hydrogensulfite are used, based in each case on monomer com position M’).
  • organic polymerization regulators are sulfur compounds such as mercaptoethanol, 2-ethylhexyl thioglycolate, thioglycolic acid and dodecyl mercaptan.
  • sulfur compounds such as mercaptoethanol, 2-ethylhexyl thioglycolate, thioglycolic acid and dodecyl mercaptan.
  • the amount thereof is generally 0.1 to 25% by weight, preferably 0.5 to 20% by weight and more preferably 1.0 to 15% by weight, based in each case on monomer composition M’).
  • the polymerization temperature is generally 20 to 200°C, preferably 20 to 150°C and more preferably 20 to 120°C.
  • the polymerization can be performed under atmospheric pressure, but is preferably undertaken in a closed system under the autogenous pressure which evolves.
  • the polymerization can take place in the absence or in the presence of an inert gas.
  • the polymerization is carried out in the presence of an inert gas, e.g. nitrogen.
  • the weight-average molecular weight Mw of the polymer P1’ can be determined by means of gel permeation chromatography (GPC) in aqueous solution using neutralized polyacrylic acid as polymer standard.
  • the polymer P1’) preferably has a weight-average molecular weight of from 1000 to 100 000 g/mol, more preferably 1500 to 50 000 g/mol, in particular 2000 to 20 000 g /mol.
  • polymer P1’ has a polydispersity index (PDI) of from 1.2 to 6.0, more preferably 1.4 to 4.0, in particular 1.6 to 3.5.
  • PDI polydispersity index
  • the polymer P1’) can be obtained in the acidic state, but it can also, if desired be partly neutralized by addition of bases.
  • bases are alkali metal hydroxides, like NaOH and KOH, alka line earth metal hydroxides, like Ca(OH)2 and Mg(OH)2, ammonia and amine bases, like mono- ethanol amine.
  • bases are alkali metal hydroxides, like NaOH and KOH, alka line earth metal hydroxides, like Ca(OH)2 and Mg(OH)2, ammonia and amine bases, like mono- ethanol amine.
  • sodium hydroxide is especially preferred. Neutralization can be performed as early as during the polymerization or after the polymerization has ended.
  • step i) for providing the aqueous composition Prior to its use in step i) for providing the aqueous composition, at the most 30 mol% of the car- boxy groups of the polymer P1’) are in the deprotonated form. Preferably, at the most 25 mol%, more preferably at the most 15 mol%, of the carboxy groups of the polymer P1’) are in the deprotonated form. In a special embodiment, the acid groups of the polymer composition according to the invention are present in non-neutralized form.
  • the polymer P1’) used in accordance with the invention can be used directly in the form of the aqueous solutions obtained in the course of preparation by means of solvent polymerization, or in dried form (obtained, for example, by spray drying, spray granulation such as fluid bed spray granulation or spouted bed spray granulation, roller drying or freeze drying).
  • Suitable polymers P1’) are commercially available or are intermediates of commercially availa ble products.
  • a commercially available polyacrylic acid is employed that is not crosslinked and not neutralized or only to a low extend neutralized.
  • Suitable products are Sokalan ® CP 10 S, Sokalan ® CP 12 S, Sokalan ® CP 13 S, Sokalan ® PA 25 XS, Sokalan ® PA 80 S and Sokalan ® NR 2530 from BASF SE.
  • the monomer composition M1) consists only of a, b-ethylenically un saturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof.
  • the a,b-ethylenically unsaturated carboxylic acid is preferably selected from acrylic acid, meth- acrylic acid, ethacrylic acid maleic acid, fumaric acid, itaconic acid, a-chloroacrylic acid, crotonic acid, citraconic acid, mesaconic acid, glutaconic acid and aconitic acid.
  • Suitable salts of the abovementioned acids are, in particular, the sodium, potassium and ammonium salts and the salts with amines or aminoalcohols.
  • the monomers A) can be used as such or as mixtures with one another. The stated proportions by weight are all based on the acid form.
  • the at least one a, b-ethylenically unsaturated carboxylic acid is preferably used in unneutral ized form for the polymerization. If the a, b-ethylenically unsaturated carboxylic acids are used in partially neutralized form for the polymerization, the acid groups are preferably neutralized to at most 50 mol%, more preferably to at most 30 mol%.
  • the monomer A) is particularly preferably selected from acrylic acid, methacrylic acid, maleic acid, fumaric acid, itaconic acid, salts of the abovementioned carboxylic acids and mixtures thereof.
  • the monomer A) is selected from acrylic acid, methacrylic acid, salts of acrylic acid, salts of methacrylic acid and mixtures thereof.
  • the monomer A) is preferably used in an amount of 50 to 100 wt .-%, particularly preferably 60 to 100 wt .-%, based on the total weight of the monomer composition M1.
  • the monomer composition M1 comprises at least 50% by weight, preferably at least 80% by weight, in particular at least 90% by weight, based on the total weight of the monomer composition M1 ), of acrylic acid and / or acrylic acid salts
  • the monomer composition M1) may comprise, in addition to the at least one monomer A), at least one monomer B) selected from olefinically unsaturated sulfonic acids, salts of olefinically unsaturated sulfonic acids, olefinically unsaturated phosphonic acids, salts of olefinically unsaturated phosphonic acids and mixtures thereof.
  • the monomer composition M1 ) may comprise, in addition to the monomers A), at least one monomer B selected from unsaturated sulfonic acids, salts of unsaturated sulfonic acids, un saturated phosphonic acid, salts of unsaturated phosphonic acids and mixtures thereof.
  • the monomer B) is preferably selected from 2-acrylamido-2-methylpropane-sulfonic acid, vinyl- sulfonic acid, allylsulfonic acid, sulfoethyl acrylate, sulfoethyl methacrylate, sulfopropyl acrylate, sulfopropyl methacrylate, 2-hydroxy-3-acryloxypropylsulfonic acid, 2-hydroxy-3-methacryloxy- propylsulfonic acid, styrenesulfonic acid, vinylphosphonic acid, allylphosphonic acid, salts of the aforementioned acids and mixtures thereof.
  • Preferred monomer B) is 2-acrylamido-2-methylpropanesulfonic acid.
  • Suitable salts of the abovementioned acids are in particular the sodium, potassium and ammo nium salts and the salts with amines.
  • the monomers B) can be used as such or as mixtures with one another. The stated proportions by weight are all based on the acid form
  • the monomer composition M1) additionally comprises at least one comonomer C) selected from
  • x is 0, 1 or 2
  • k and I are independently an integer from 0 to 100, where the sum of k and I is at least 2, preferably at least 5,
  • R 1 is hydrogen or methyl
  • R 2 is hydrogen or Ci-C 4 -alkyl, and mixtures of two or more than two of the aforementioned monomers C1 ) to C3).
  • the monomer composition M1 based on the total weight, comprises less than 0.1 % by weight, preferably less than 0.05% by weight, especially less than 0.001 % by weight, of crosslinking monomers having two or more than two free-radically polymerizable a,b-ethylenically unsaturated double bonds per molecule.
  • the monomer composition M1 does not comprise any crosslinking monomers having two or more than two free-radically polymerizable a,b-ethylenically unsaturated double bonds per molecule.
  • the monomer composition M1 ) used for free-radical polymerization comprises or consists of acrylic acid and/or acrylic acid salts.
  • the free-radical polymerization of the monomer composition M1 is conducted in the presence of at least one Ce-C-is-alkyl polyoxy- alkylene ether incorporating exclusively ethylene oxide units as alkylene oxide units and/or also in the presence of a polymer.
  • the Ce-C-ie-alkyl polyoxyalkylene ethers mentioned above comprise an average of 3 to 10 ethylene oxide units per molecule, preferably an average of 5 to 9 ethylene oxide units per molecule.
  • the polymer composition P1) is provided by
  • step a) subjecting the monomer composition M1) provided in step a) to a free-radical polymerization in the presence of at least one Ce-Cie-alkyl polyoxyalkylene ether having 3 to 12 alkylene oxide units per molecule and optionally in the presence of at least one additive.
  • the free-radical polymerization in step B) is effected in feed mode, wherein at least a portion of the Cs-Cis-alkyl polyoxyalkylene ether having 3 to 12 alkylene oxide units per molecule and optionally, if present, at least a portion of a solvent are initially charged, and at least a portion of the monomer composition M) provided in step a) and at least one free-radical initiator are fed into the initial charge.
  • Suitable as polyether component PE are polyetherols having a number average molecular weight of at least 200 g/mol and their mono- and di-(Ci-C 6 -alkyl ethers).
  • Suitable polyetherols and their mono- and di-(CrC 6 -alkyl ethers) may be linear or branched, preferably linear.
  • Suitable polyetherols and their mono- and di-(C1-C6-alkyl ethers) generally have a number-average molecular weight in the range from about 200 to 100,000, preferably from 300 to 50,000, particularly preferably from 500 to 40,000.
  • Suitable polyetherols are, for example, water-soluble or water-dispersible nonionic polymers which comprise alkylene oxide repeat units.
  • the proportion of alkylene oxide repeating units is at least 30 % by weight, based on the total weight of the compound.
  • Suitable polyetherols are polyalkylene gly cols, such as polyethylene glycols, polypropylene glycols, polytetrahydrofurans and alkylene oxide copolymers.
  • Suitable alkylene oxides for the preparation of alkylene oxide copolymers are e.g. ethylene oxide, propylene oxide, epichlorohydrine, 1 ,2- and 2,3-butylene oxide.
  • Suitable examples are copolymers of ethylene oxide and propylene oxide, copolymers of ethylene oxide and butylene oxide and copolymers of ethylene oxide, propylene oxide and at least one butylene oxide.
  • the alkylene oxide copolymers may comprise randomly distributed alkylene oxide units or in copolymerized form in the form of blocks.
  • the proportion of repeating units derived from ethylene oxide is 40 to 99% by weight.
  • Particularly preferred as the polyether component PE are ethylene oxide homopolymers and ethylene oxide / propylene oxide copolymers.
  • polyether component PE Also suitable as polyether component PE are the mono- and di-(Ci-C 6 -alkyl ethers) of the polyetherols described above. Preference is given to polyalkylene glycol monomethyl ether and pol yalkylene glycol dimethyl ether.
  • polyether component PE Also suitable as polyether component PE are polyether-containing surfactants. Generally suit able are nonionic and ionic surfactants which have at least one nonpolar and at least one polar group and which comprise a polyether group.
  • the polyether groups-containing surfactants PE are preferably selected from alkylpolyoxy- alkylenether, arylpolyoxyalkylenether, alkylarylpolyoxyalkylenether, alkoxylated animal and/or vegetable fats and/or oils, fatty amine alkoxylates, fatty acid amide alkoxylates, fatty acid dieth- anolamide alkoxylates, polyoxyethylenesorbitan fatty acid esters, alkylpolyethersulfates, ar- ylpolyethersulfates, alkylarylpolyethersulfates, alkylpolyethersulfonates, arylpolyethersulfonates, alkylarylpolyethersulfonates, alkylpolyether phosphateates, aryl polyether phosphates, alkylaryl polyether phosphates, glycerol ether sulfonates, glycerol ether sulfates, monogly
  • the preferred nonionic polyether group-containing surfactants PE include, for example:
  • Alkyl polyoxyalkylene ethers derived from C3-C6 low molecular weight alcohols or C7-C30 fatty alcohols.
  • the ether component may be derived from ethylene oxide units, propylene oxide units, 1 ,2-butylene oxide units, 1 ,4-butylene oxide units, and random copolymers and block copolymers thereof.
  • Suitable nonionic surfactants include, inter alia, surfactants of the general formula (VI)
  • R 10 is a linear or branched alkyl radical having 6 to 22 C atoms
  • R 11 and R 12 independently of one another are hydrogen or a linear or branched alkyl radical having 1 to 10 C atoms or H, wherein R 12 is preferably methyl, and
  • x and y are independently 0 to 300.
  • fatty alcohol alkoxylates and oxo alcohol alkoxylates such as iso- tridecyl alcohol and oleyl alcohol polyoxyethylene ethers.
  • the sequence of the alkylene oxide units is arbitrary, s, t, u and v independently represent an integer from 0 to 500, the sum of s, t, u and v being > 0, R 13 and R 15 independently of one another represent a linear or branched, saturated Ci-C4o-alkyl radical or a mono- or polyunsaturated C 2 -C4o-alkenyl radical, and
  • R 14 is selected from methyl, ethyl, n-propyl, isopropyl or n-butyl.
  • the sum of s, t, u and v is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
  • t and u are 0.
  • the sum of s and v is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
  • R 13 and R 15 are preferably, independently of one another, a linear or branched, saturated C 2 -C3o-alkyl radical.
  • R 13 and R 15 may also be mixtures of different alkyl radicals.
  • R 14 is preferably methyl or ethyl, in particular methyl.
  • a preferred embodiment are hydroxyl-containing surfactants of the general formula
  • s and v are independently an integer from 0 to 500, the sum of s and v being > 0, and
  • R 13 and R 15 independently of one another represent a linear, saturated Ci-C3o-alkyl radical or a branched, saturated C3-C3o-alkyl radical or mono- or polyunsaturated C2-C3o-alkenyl radical.
  • the sum of s and v is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
  • nonionic surfactants include e.g. hydroxy mixed ethers of the general formula (C 6 -22-alkyl)-CH(OH)CH 2 O-(EO)20-i20-(C2-26-alkyl).
  • R 16 and R 18 independently of one another represent a linear or branched, saturated Ci-C4o-alkyl radical or a mono- or polyunsaturated C2-C4o-alkenyl radical, and
  • R 17 is selected from methyl, ethyl, n-propyl, isopropyl or n-butyl.
  • the sum of p and q is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
  • R 16 and R 18 independently of one another represent a linear or branched, saturated C 4 -C3o-alkyl radical.
  • R 16 and R 18 may also be mixtures of different alkyl radicals.
  • R 17 is preferably methyl or ethyl, in particular methyl.
  • These include e.g. lauryl alcohol polyoxyethylene acetate. alkylarylalkoholpolyoxyethylenether, e.g. Octylphenol polyoxyethylene ether,
  • alkoxylated animal and/or vegetable fats and/or oils e.g. corn oil ethoxylates, castor oil ethoxylates, tallow fat ethoxylates,
  • alkyl phenol alkoxylates such as ethoxylated isooctyl-, octyl- or nonylphenol, tributylphe- nol polyoxyethylene ethers,
  • fatty amine alkoxylates fatty acid amide- and fatty acid diethanolamide alkoxylates, especially their ethoxylates
  • alkylpolyethersulfate sodium dodecylpoly (oxyethylene) sulfate (sodium lauryl ether sulfate, SLES).
  • the polyether component PE is selected from Ce-C-ie-alkyl polyoxyalkylene ethers having an average of 3 to 12 alkylene oxide units per molecule.
  • the polymer composition P1 may be prepared by free-radical polymerization of the monomer composition M1) in the presence of at least one Cs-C-is-alkyl polyoxyalkylene ether having an average of 3 to 12 alkylene oxide units per molecule. This affords specific polymer compositions P1 ) having advantageous properties. Without being bound to a theory, hydrogen bonds are able to form between the growing polymer and the alkylene oxide units, and these influence the properties of the resultant polymer composition.
  • polymer compositions P1) having a high content of the Ce-C-ia-alkyl polyoxyalkylene ether can be attained; these cannot be prepared by mixing the separately prepared polymer with the C 8 -Ci 8 -alkyl polyoxyalkylene ether. Free- radical surfactant degradation advantageously does not take place here.
  • the polymer compositions P1 For production of a washing- and cleaning-active multilayer films according to the invention, preference is given to using polymer compositions P1 ) having a low glass transition temperature T G .
  • the polymer compositions P1) used for production of the washing- and cleaning- active multilayer films of the invention have a glass transition temperature T G in the range from 0 to 80°C, preferably from 0 to 60°C, especially 0 to 30°C.
  • Tg glass transition temperatures described in the context of this application can be determined by means of differential scanning calorimetry (DSC).
  • the polymer compositions P1) used for production of the washing- and cleaning-active multilayer films of the invention take the form of a transparent film.
  • the multi-layered film further comprises at least one other layer which comprises at least one polymer P2) which is different from polymer composition P1 ) and is selected from
  • homo- or copolymers comprising monomer units derivable from vinyl alcohol, vinylesters, alkoxylated vinyl alcohols, or mixtures thereof;
  • homo-or copolymers comprising at least one monomer selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole, 2-vinylpyridine, 4-vinyl-pyridine, salts of N- vinylimidazole, salts of 2-vinylpyridine, salts of 4-vinyl-pyridine, vinylpyridine-N-oxide, N- carboxymethyl-4-vinylpyridine halogenides or mixtures thereof;
  • homo- or copolymers of acrylic acid and /or methacrylic acid preferably copolymers corn- prising at least one acrylic acid monomer selected from acrylic acid, salts of acrylic acid or mixtures thereof and at least one maleic acid monomer selected from maleic acid, maleic acid anhydride, salts of maleic acid or mixtures thereof;
  • copolymer comprising at least a (meth)acrylic acid monomer selected from acrylic acid, methacrylic acid, salts of acrylic acid, salts of methacrylic acid or mixtures thereof and at least one hydrophobic monomer selected from CrCs alkylesters of (meth) acrylic acid, C2-
  • polyalkyleneglycols mono-or diethers of polyalkyleneglycols
  • polyalkyleneoxide such as polyethyleneoxide
  • multifunctional alkoxylated diamines preferably alkoxylated diamines with 2 to 10 meth ylene groups, and
  • the multi-layered film particularly preferably comprises at least one further layer which compris es at least one polymer P2) or consists of at least one polymer P2) which is selected from Cellulose ethers and cellulose esters,
  • the multi-layered film comprises in particular at least one further layer which comprises at least one polymer P2) or consists of at least one polymer P2) selected from cellulose derivatives, preferably carboxyalkylcelluloses and salts thereof, sulfoalkylcelluloses and salts thereof, acidic sulfuric ester salts of cellulose, alkylcelluloses, hydroxyalkylcelluloses, (hydroxyalkyl) alkylcellu- loses and mixtures of two or more of these cellulose derivatives.
  • Polysaccharides suitable as polymers P2 are natural polysaccharides, e.g.
  • cellulose hemicellu- lose, glycogen, starch (amylose and amylopectin), dextran, pectins, inulin, xanthan, chitin, cal- lose, thermally, hydrolytically or enzymatically degraded starch, e.g. maltodextrin etc
  • Preferred modified polysaccharides are e.g. cellulose ethers, cellulose esters, cellulose amides, etc.
  • Cellulose ethers are derivatives of cellulose that result from partial or total substitution of the hydrogen atoms in the hydroxy groups of the cellulose. Cellulose ethers from the reaction of cellulose with more than one etherifying agent are also referred to as cellulose mixed ethers.
  • Preferred cellulose ethers are selected from alkylcelluloses, hydroxyalkylcelluloses, (hydroxy- alkyl) alkylcelluloses, carboxyalkylcelluloses and salts thereof, (carboxyalkyl) alkylcelluloses and salts thereof, (carboxyalkyl) (hydroxyalkyl) celluloses and salts thereof, (carboxyalkyl) (hydroxy- alkyl) alkylcelluloses and salts thereof, sulfoalkylcelluloses and salts thereof.
  • Preferred carboxyalkyl radicals are the carboxymethyl radical and the carboxyethyl radical. Particularly preferred as carboxyalkyl radical is the carboxymethyl radical.
  • Preferred as sulfoalkyl radical are the sulfomethyl radical and the sulfoethyl radical. Particularly preferred as sulfoalkyl radical is the sulfomethyl radical.
  • Preferred salts are the sodium, potassium, calcium and ammonium salts.
  • Particularly preferred cellulose ethers are selected from carboxymethylcellulose, carboxyethyl- cellulose, methylcellulose, ethylcellulose, n-propylcellulose, ethylmethylcellulose, hydroxyethyl- cellulose, hydroxypropylcellulose, hydroxybutylcellulose, hydroxyethylmethylcellulose, hydroxy- propylmethylcellulose, hydroxyethylethylcellulose, hydroxypropylethylcellulose, carboxymethyl- methylcellulose, carboxymethylethylcellulose, carboxymethylhydroxyethylcellulose, carbox- ymethylhydroxyethylmethylcellulose, carboxymethylhydroxyethylethylcellulose, sulfomethylcellu- lose and sulfoethylcellulose.
  • the carboxyalkyl radicals and the sulfoalkyl radicals may also be present as salts.
  • Cellulose esters are derivatives of cellulose which are formed by esterification of the hydroxy groups with acids.
  • Preferred are the sulfuric acid esters of cellulose.
  • the sulfuric acid is only subjected to a partial esterification, so that the resulting sulfuric acid es ters still have free acid groups or their salts.
  • Particular preferred are sulfuric ester salts of cellulose. These are distinguished by their graying-inhibiting effect.
  • Preferred modified polysaccharides are selected from methyl cellulose, ethyl cellulose, propyl cellulose, methyl/ethyl cellulose, ethyl/propyl cellulose, carboxymethyl cellulose, salts of carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, hydroxyethylmethyl cellulose, hydroxyethylethyl cellulose, hydroxypropylmethyl cellulose, hydroxypropylethyl cellulose, etc.
  • the polymers P2) are selected from homo- and copolymers comprising repeating units derived from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof.
  • Suitable vinyl esters are generally the esters of vinyl alcohol with C1-C15- carboxylic acids, preferably Ci-C8-carboxylic acids, more preferably Ci-C4-carboxylic acids.
  • Preferred vinyl acylates are vinyl acetate, vinyl n-propionate, vinyl n-butyrate, vinyl 2-ethyl- hexanoate, vinyl laurate, etc. Particularly preferred is vinyl acetate.
  • Partially or completely saponified (hydrolyzed) polyvinyl acetates are generally referred to as "polyvinyl alcohol (PVOH)".
  • Partially hydrolysed polyvinyl acetates are obtained by incomplete hydrolysis of polyvinyl acetates, i.e. the partially hydrolyzed polymer has both ester groups and hydroxyl groups.
  • the saponification of the polyvinyl acetates can be carried out in a manner known per se in alkaline or acidic, i.e. with the addition of acid or base.
  • polyvinyl alcohols are determined inter alia by the degree of polymerization and the degree of hydrolysis (degree of saponification). As the degree of saponification increases, the solubility in water decreases. Polyvinyl alcohols with degrees of hydrolysis of up to about 90 mol% are generally soluble in cold water. Polyvinyl alcohols with degrees of hydrolysis of about 90 to about 99.9 mol% are generally no longer soluble in cold water, but are soluble in hot water.
  • Polyvinyl alcohols suitable as polymers P2) preferably have a saponification degree of from 50 to 99.9 mol%, particularly preferably from 70 to 99 mol%, in particular from 80 to 98 mol%.
  • polyvinyl alcohols can further be modified by the incorporation of additional monomers such as the sodium salts of 2-acrylamido-2-methylpropane sulfonic acid, vinyl- sulfonic acid or allylsulfonic acid.
  • Polyvinyl alcohols suitable as polymers P2) preferably have a weight-average molecular weight of from 10,000 to 300,000 g/mol, more preferably from 15,000 to 250,000 g/mol.
  • Polyvinylalcohol that can typically be used as polymers P2) are known under the tradename PovalTM from Kuraray company. Non limited examples are PovalTM 8-88, PovalTM 18-88, PovalTM 26-88, PovalTM 30-92, PovalTM 10-98, PovalTM 20-98 or PovalTM 28-99.
  • blends comprising polyvinylalcohols of different molecular weight and degree of hydrolysis can be used.
  • Non limited examples are a blend of PovalTM 26-88 (three parts) and PovalTM 20-98 (one part) or a blend of PovalTM 30-92 (two parts) and PovalTM 10-98 (one part).
  • Polyvinyl alcohols suitable as polymers P2) preferably have a viscosity of 2 to 120 mPa s, more preferably of 7 to 70 mPa s and in particular of 15 to 60 mPa s, measured according to DIN 53015 on a 4% solution in water.
  • the polymers P2) are selected from homopolymers and copolymers which comprise at least one monomer in copolymerized form, which is selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole, 2-vinylpyridine, 4-vinylpyridine, salts thereof three latter monomers, vinylpyridine-N-oxide, N-carboxymethyl-4-vinylpyridium halides and mixtures thereof.
  • N-vinylimidazole, 2-vinylpyridine and 4-vinylpyridine can be converted by protonation or quater- nization into the corresponding salts.
  • Suitable acids are e.g. mineral acids such as sulfuric acid, hydrochloric acid and phosphoric acid, and carboxylic acids.
  • Alkylating agents suitable for quaternization are C1-C4 alkyl halides or C1-C4 alkyl sulfates such as ethyl chloride, ethyl bromide, methyl chloride, methyl bromide, dimethyl sulfate and diethyl sulfate.
  • polyvinylpyrrolidone homopolymers and copolymers which comprise copolymerized N-vinylpyrrolidone and another ethylenically unsaturated monomer different therefrom.
  • Suitable N-vinylpyrrolidone copolymers are generally neutral, anionic, cationic and amphoteric polymers.
  • N-vinylpyrrolidone copolymers are selected from
  • the polymers P2) are selected from homopolymers and copolymers of acrylic acid and/or methacrylic acid.
  • the polymer P2) used is an acrylic acid homopolymer.
  • Acrylic acid homopolymers P2) preferably have a number-average molecular weight in the range from 800 to 70,000 g/mol, more preferably from 900 to 50,000 g/mol, in particular from 1000 to 20,000 g/mol, especially from 1000 to 10,000 g/mol.
  • the term acrylic acid homopolymer also encompasses polymers in which the carboxylic acid groups are partially or completely neutralized. These include acrylic acid homopolymers in which the carboxylic acid groups are present partially or completely in the form of alkali metal salts or ammonium salts.
  • acrylic acid homopolymers in which the carboxylic acid groups are protonated or in which the carboxylic acid groups are present partially or completely in the form of sodium salts.
  • Homopolymers of acrylic acid which are particularly suitable as polymers P2) are the Sokalan ® PA grades from BASF SE.
  • the polymer P2) used is a copolymer comprising at least one acrylic acid monomer selected from acrylic acid, acrylic acid salts and mixtures thereof and at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, in copolymerized form.
  • acrylic acid monomer selected from acrylic acid, acrylic acid salts and mixtures thereof
  • maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, in copolymerized form.
  • These preferably have a number-average molecular weight in the range from 2500 to 150,000 g/mol, more preferably from 2800 to 70,000 g/mol, in particular from 2900 to 50,000 g/mol, more particularly from 3000 to 30,000 g/mol.
  • copoly-mers in which the carboxylic acid groups are partially or completely neutralized.
  • monomers in salt form either for the polymerization or the resulting copolymer is subjected to a partial or complete neutralization.
  • copolymers in which the carboxylic acid groups are protonated or partially or completely present in the form of alkali metal salts or ammonium salts.
  • Preferred alkali metal salts are the sodium or potassium salts, especially the sodium salts.
  • Preferred polymers P2) are copolymers of maleic acid (or maleic acid monomers) and acrylic acid (or acrylic acid monomers) in a weight ratio of 10:90 to 95: 5, particularly preferably in a weight ratio of 30:70 to 90:10.
  • Preferred polymers P2) are also terpolymers of maleic acid (or maleic acid monomers), acrylic acid (or acrylic acid monomers) and a vinyl ester of a C1-C3 carboxylic acid in a weight ratio of 10 (maleic acid) : 90 (acrylic acid + vinyl ester) to 95 (maleic acid) : 10 (acrylic acid + vinyl ester).
  • the weight ratio of acrylic acid to vinyl ester is preferably in a range of 30:70 to 70:30.
  • Particularly suitable polymers P2) based on acrylic acid monomers and maleic acid monomers are the corresponding Sokalan ® CP grades from BASF SE.
  • the polymer P2) is a copolymer, which comprises at least one (meth) acrylic acid monomer selected from (meth) acrylic acid, (meth) acrylic acid salts and mixtures thereof and at least one hydrophobic monomer.
  • the hydrophobic monomer is especially selected from Ci-Cs alkyl esters of (meth) acrylic acid such as e.g. the methyl, ethyl, n- and iso-propyl, n-butyl and 2-ethylhexyl esters of (meth) acrylic acid and C 2 -Cio-olefins, e.g. ethene, propene, 1 ,2-butene, isobutene, disobutene, styrene and a-methylstyrene.
  • the polymer P2) used is a copolymer of at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof with at least one C 2 -C 8 -olefin.
  • copolymers which comprise at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, in copolymerized form at least one C2-Cs-olefin and at least one other comonomer which is different therefrom.
  • copolymers which comprise at least one maleic acid monomer select ed from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof and at least one C 2 -C 8 -olefin copolymerized as sole monomers. These preferably have a number average molecular weight in the range from 3000 to 150,000 g/mol, particularly preferably from 5000 to 70,000 g/mol, in particular from 8000 to 50,000 g/mol, more particularly from 10,000 to 30,000 g/mol. Included therein are also copolymers in which the carboxylic acid groups are partially or completely neutralized.
  • maleic acid salts can be used for the polymerization or the resulting copolymer is subjected to a partial or complete neutralization.
  • Preferred alkali metal salts are the sodium or potassium salts, especially the sodium salts.
  • a specific embodiment are copolymers of maleic acid with C2-C8 olefins in a molar ratio of 40:60 to 80:20, whereby copolymers of maleic acid with ethylene, propylene, isobutene, diisobutene or styrene are particularly preferred.
  • Particularly suitable polymeric carboxylic acid group- containing compounds based on olefins and maleic acid are likewise the corresponding Soka- lan ® CP grades from BASF SE.
  • copolymers comprising at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, at least one C2-C8 olefin and at least one acrylic acid monomer selected from acrylic acid, acrylic acid salts and mixtures thereof, in copolymerized form.
  • a further preferred embodiment is copolymers which comprise at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, at least one C2-C8 olefin and at least one ester of (meth) acrylic acid in copolymerized form.
  • the ester of (meth) acrylic acid is then in particular selected from C2-Cs-alkyl esters of (meth) acrylic acid, e.g. the methyl, ethyl, n- and iso-propyl, n-butyl and 2-ethylhexyl esters of (meth) acrylic acid.
  • the polymers P2) are selected from homopolymers and co polymers which comprise, in polymerized form, at least one monomer selected from acrylamide, methacrylamide and mixtures thereof. These polymers P2) are preferably water-soluble or water-dispersible. In particular, these polymers P2) are water-soluble.
  • the polymers P2) are selected from homopolymers of acrylamide or methacrylamide.
  • the polymers P2) are selected from copolymers of acrylamide and/or methacrylamide. These comprise at least one comonomer in copolymerized form, which is selected from acrylamide and methacrylamide different hydrophilic monomers (A1 ), monoeth- ylenically unsaturated, amphiphilic monomers (A2) and other ethylenically unsaturated monomers (A3).
  • Suitable hydrophilic, monoethylenically unsaturated monomers (A1 ) are neutral monomers, such as N-methyl (meth) acrylamide, N, N'-dimethyl (meth) acrylamide or N-methylol (meth) acrylamide, monomers comprising hydroxyl and/or ether groups, such as e.g.
  • N-vinyl derivatives can be hydrolyzed after polymerization to vinylamine units, vinyl esters to vinyl alcohol units.
  • Suitable hydrophilic, monoethylenically unsaturated monomers (A1 ) are furthermore monomers which comprise at least one acidic group or salts thereof. These include acrylic acid, methacrylic acid, crotonic acid, itaconic acid, maleic acid, fumaric acid, vinylsulfonic acid, allylsulfonic acid, 2-acrylamido-2-methylpropanesulfonic acid, 2-methacrylamido-2-methylpropanesulfonic acid, 2-acrylamidobutanesulfonic acid, 3-acryl- amido-3-methylbutanesulfonic acid, 2-acrylamido-2,4,4-trimethylpentanesulfonic acid, vi- nylphosphonic acid, allylphosphonic acid, N-(meth) acrylamidoalkylphosphonic acids, (meth) acryloyloxyalkylphosphonic acids and salts and mixtures thereof.
  • the other monoethylenically unsaturated hydrophilic monomers may be hydrophilic cationic monomers.
  • Suitable cationic monomers (A1 c) include, in particular, ammonium-group containing monomers, in particular ammonium derivatives of N-(u)-aminoalkyl) (meth) acrylamides or w-aminoalkyl (meth) acrylic esters.
  • amphiphilic monomers (A2) are preferably monoethylenically unsaturated monomers which have at least one hydrophilic group and at least one, preferably terminal, hydrophobic group.
  • the monomers (A3) may be e.g. monoethylenically unsaturated monomers which have a more hydrophobic character than the hydrophilic monomers (A1) and which accordingly are only slightly water-soluble.
  • monomers include N-alkyl and N, N'-dialkyl (meth) acrylamides wherein the number of carbon atoms in the alkyl groups together is at least 3, preferably at least 4.
  • monomers include N-butyl (meth) acrylamide, N-cyclohexyl (meth) acrylamide or N-benzyl (meth) acrylamide.
  • the polymers P2) are selected from polyamino acids.
  • Suita ble polyamino acids are in principle compounds, which comprise at least one amino acid, such as aspartic acid, glutamic acid, lysine, glycine, etc. in copolymerized form.
  • the polyamino acids also include the derivatives obtainable by polymer-analogous reaction, such as esterification, amidation, etc.
  • Preferred polyamino acids are polyaspartic acid, polyaspartic acid derivatives, polyglutamic acid, polyglutamic acid derivatives and mixtures thereof.
  • Polyaspartic acid may e.g. by alkaline hydrolysis of polysuccinimide (PSI, anhydropolyaspartic acid).
  • PSI polysuccinimide
  • Polysuccinimide can be prepared by thermal condensation of aspartic acid or from ammonia and maleic acid.
  • Polyaspartic acid may e.g. be used as a biodegradable complexing agent and cobuilder in detergents and cleaners.
  • Polyamino acids having surfactant properties can be obtained by at least partially converting the free carboxylic acid groups of polyaspartic acid or polyglutamic acid into N-alkylamides and/or into esters.
  • Polyaspartic acid amides can also be prepared by reacting polysuccinimide with amines.
  • hydroxyethylaspartamides the ring opening of polysuccinimide can be carried out with ethanolamine.
  • DE 37 00 128 A and EP 0 458 079 A describe the subsequent esterification of such hydroxyethyl derivatives with carboxylic acid derivatives.
  • Copolymers of polyaspartic ester are, as described in DE 195 45 678 A, obtainable by condensation of monoalkyl esters of maleic or fumaric acid with addition of ammonia.
  • copolymeric polyaspartic esters are accessible by reaction of polysuccin- imide with alcohols and optionally subsequent hydrolysis.
  • polyaspartic esters in addition to their bio degradability, are distinguished by excellent properties as stabilizers for O / W and W / O emulsions, foam-stabilizing and foam-enhancing cosurfactants in detergents and cleaners and as complexing agents for metal cations.
  • the polymers P2) are selected from polyalkylene glycols and mono- or diethers of polyalkylene glycols.
  • Preferred polyalkylene glycols have a number aver age molecular weight in the range from 1000 to 4,000,000 g/mol, particularly preferably from 1 ,500 to 1 ,000,000 g/mol
  • Suitable polyalkylene glycols and their mono- or diethers may be linear or branched, preferably linear.
  • Suitable polyalkylene glycols are e.g. water-soluble or water-dispersible nonionic polymers, which comprise alkylene oxide repeat units. The proportion of alkylene oxide repeating units is preferably at least 30% by weight, preferably at least 50% by weight, in particular at least 75% by weight, based on the total weight of the compound.
  • Suitable polyalkylene glycols are polyethylene glycols, polypropylene glycols, polytetrahydrofurans and alkylene oxide copolymers.
  • Suitable alkylene oxides for the preparation of alkylene oxide copolymers are, for.
  • ethylene oxide, propylene oxide, epichlorohydrin, 1 ,2- and 2,3-butylene oxide Suitable examples are copolymers of ethylene oxide and propylene oxide, copolymers of ethylene oxide and butylene oxide and copolymers of ethylene oxide, propylene oxide and at least one butylene oxide.
  • the alkylene oxide copolymers may comprise randomly distributed alkylene oxide units or in copolymerized form in the form of blocks.
  • the proportion of repeating units derived from ethylene oxide is 40 to 99% by weight.
  • Particularly preferred are ethylene oxide homopolymers and ethylene oxide / propylene oxide copolymers.
  • Suitable mono- and diethers of polyalkylene glycols are the mono (C1-C18 alkyl ethers) and di (C1-C18 alkyl ethers).
  • Preferred mono- and diethers of polyalkylene glycols are the mono (C1-C6 alkyl ethers) and di (C1-C6 alkyl ethers).
  • Especially preferred are the mono (C1-C2 alkyl ethers) and di (C1-C2 alkyl ethers).
  • Particularly preferred are polyalkylene glycol monomethyl ether and polyalkylene glycol dimethyl ether.
  • At least one of the layers comprises or consists of at least one compound selected from the group consisting of (i) vinyl- imidazole containing polymers, preferably vinylpyrrolidone/vinylimidazole copolymers with a molecular weight Mw in the range of 10000 to 100000 g/mol, (ii) polyvinylpyrrolidones with a molecular weight Mw in the range of 10000 to 100000 g/mol, (iii) polyethylene imine ethox- ylates, (iv) multifunctional diamines and (v) amphoteric modified starch, and mixtures thereof.
  • vinyl- imidazole containing polymers preferably vinylpyrrolidone/vinylimidazole copolymers with a molecular weight Mw in the range of 10000 to 100000 g/mol
  • polyvinylpyrrolidones with a molecular weight Mw in the range of 10000 to 100000 g/mol
  • At least one of the layers comprises at least one additive and/or at least one additive is present between at least two layers, said additive preferably being selected from nonionic, anionic, cationic and amphoteric surfactants, builders, complexing agents such as methylglycinediacetic acid, glutaminediacetic acid, glutamic acid diacetic acid and citric acid and the sodium and potassium salts thereof, bleaches, enzymes, bases, corrosion inhibitors, defoamers, wetting agents, dyes, pigments, fragrances, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, fluores- cers, hydrotropes, antiredeposition agents, optical brighteners, graying inhibitors, antishrink agents, anticrease agents, dye transfer inhibitors, antimicrobial active ingredients, antioxidants, corrosion inhibitors, antistats, ironing aids, hydrophobizing and impregnating agents, antiswell and anti
  • At least two of the layers preferably two of the layers, comprise at least one type of enzyme EN) each.
  • two of the layers comprise one enzyme EN) each, wherein the enzymes EN) comprised in the different layers are different from each other, and preferably are incompatible with each other (as defined above).
  • At least two of the layers comprise one enzyme EN) each, and wherein the layers comprising one enzyme EN) each are spatially separated by at least one layer comprising or consisting of composition P1 ) or P2), and wherein the separating layer does not contain enzymes, and wherein the enzymes EN) comprised in the different layers are preferably different from each other, and further preferably are incompatible with each other.
  • At least one enzyme EN) is incorporated in one of the layers comprising or consisting of a composition P2), wherein this layer comprising or consisting of a composition P2) preferably comprises polyvinyl alcohol.
  • all of the enzymes EN) are incorporated in any one of the layers comprising or consisting of a composition P2).
  • At least one layer contains protease as enzyme EN1 ) (preferably as the only enzyme in this layer), and at least one other layer contains at least one enzyme EN2) different from protease, preferably at least one enzyme EN2) that is incompatible with protease and preferably different from protease, more preferably lipase as enzyme EN2), and wherein, preferably, these two layers containing EN1 ) and EN2) are spatially separated by at least one further layer neither comprising EN1) nor EN2).
  • none of the layers contains a protease inhibitor (as defined above).
  • the water-soluble multilayer film is derived from a wash active layer based on a at least one polymer chosen from P2), preferred a polymer blend, more preferred chosen from polymer composition P1 ), which is used as adhesion layer in-between two enzyme containing layers, optionally in a lamination process.
  • Multilayer films can be produced e.g. by a lamination method. Lamination methods in which two or more film layers are bonded to one another over their area are known to those skilled in the art. Lamination involves pressing two or more than two films together under elevated pressure and/or at elevated temperature. Multilayer films can also be produced by a wet-on-wet application method. In addition, multilayer films can also be produced by using combinations of the aforementioned production methods and the application method described hereinafter.
  • the multilayer film is produced by a process in which at least one free-flowing composition capable of film formation is applied to a carrier material, wherein the carrier material and/or the at least one free-flowing composition comprises or consists of the polymer composition P1 ) as defined above and hereinafter, or comprises a polymer P1’) and a polyoxyalkylene ether PE) as defined above and hereinafter.
  • the process for producing a multilayer film preferably comprises the steps of
  • a first free-flowing or pourable composition capable of film formation is applied to a carrier material to obtain a first layer
  • the first layer applied to the carrier material is optionally subjected to an increase in viscosity
  • a second free-flowing or pourable composition capable of film formation is applied to the first layer obtained in step H ) or in step i2) to obtain a second layer,
  • the second layer is optionally subjected to an increase in viscosity
  • step i3) is optionally repeated with a further composition capable of film formation to obtain a further layer and step i4) is optionally then repeated, it being possible to repeat steps i3) and i4) once or more than once,
  • the layers applied to the carrier material are optionally subjected to a further increase in viscosity
  • the multilayer film obtained is optionally detached from the carrier material, with the proviso that the free-flowing or pourable compositions each comprise a component which is capable of film formation and is independently selected from at least one polymer composition P1 , at least one polymer P2 or a mixture thereof, and with the proviso that the carrier material and/or the at least one free-flowing or pourable composition comprises or consists of a polymer composition P1 as defined above and hereinafter.
  • the application of two or more than two of the pourable compositions can also be applied partly or fully simultaneously.
  • the application of the (n+1)th composition can be commenced before the application of the nth composition has completely ended.
  • the production of the multilayer film proceeds from a carrier material which already comprises the first film layer and optionally also already comprises fur ther film layers of the multilayer film.
  • a carrier material which already comprises the first film layer and optionally further film layers of the multilayer film is used in step i1 ).
  • the carrier material forms part of the multilayer film and remains in the multilayer film after the application of all the further layers. This means that the further layers applied to the carrier material are not subsequently detached again from the carrier material. In this embodiment, there is therefore no step i7) of the above-described process.
  • the viscosity of the free-flowing composition is matched to the technical demands of the production method and is determined by factors including the concentration of the components capable of film formation, the solvent content (water), the additives added and the temperature.
  • the pourable compositions capable of film formation are applied in steps i 1 ) , i3) and i5) general- ly by means of standard methods, for example by means of pre-metered and self-metered methods selected from airblade coating, knife coating, airknife coating, squeegee coating, impregnation coating, dip coating, reverse roll coating, transfer roll coating, gravure coating, kiss coating, flow coating, cascade flow coating, slide coating, curtain coating, mono- and multilami- nar slot die coating, spray coating, spin coating, or printing methods such as relief printing, intaglio printing, rotogravure printing, flexographic printing, offset printing, inkjet printing, letter- press printing, pad printing, heatseal printing or screenprinting methods.
  • the application can also be continuous or semicontinuous, for example when the carrier material is moving, for example a permanently or intermittently moving belt.
  • Suitable carrier materials are firstly all materials which enable simple detachment of the finished multilayer film. Examples of these include glass, metals such as galvanized steel sheet or stainless steel, polymers such as silicones or polyethylene terephthalate, polymer-coated paper, such as silicone paper, etc. Suitable carrier materials are secondly monolaminar or multilaminar polymer films which remain as film layers in the multilayer film of the invention. With regard to the composition of these carrier materials, reference is made to the disclosure relating to the polymer composition P1 and the disclosure relating to polymers P2.
  • the increase in viscosity in layers i2), i4) and i6) can be effected by means of standard methods and generally depends on the form in which pourable compositions capable of film formation have been applied in steps i1 ), i3) and i5). If they have been applied as a melt, for example, there is generally already an increase in viscosity in the course of cooling.
  • the cooling can be effected by simply leaving the carrier material to stand or by active cooling, such as cooling of the carrier material, jetting with a cool gas (jet), cooling in a cold room/refrigerator and the like.
  • the free-flowing composition capable of film formation has been applied in the form of a solution or dispersion, it is generally necessary to remove at least some of the solvent, which can be effected, for example, by simply leaving the carrier material to stand, drying with an air jet or hot air jet, drying in drying cabinets, heating of the carrier material, application of a reduced pressure, optionally with simultaneous supply of heat, IR irradiation, microwave radiation, for exam ple in a corresponding oven, and the like.
  • the composition be curable, for example because the polymers present therein comprise as yet unconverted polymerizable/condensable groups, the increase in viscosity can alternatively or additionally be effected by curing the poly mer.
  • ethylenically unsaturated crosslinkable groups are especially cured by UV radiation; condensable groups, by contrast, generally cure either by being left to stand or with supply of heat.
  • the heat can again be supplied as described above, i.e., for example, by incidence of warm or hot air or other warm or hot gases, drying in drying cabinets, heating of the carrier material, IR irradiation and the like. It is also possible to gel the solution or dispersion applied by cooling, in the sense of forming a physical network extended over macroscopic di- mensions, which likewise results in an increase in viscosity.
  • the pourable compositions capable of film formation for two or more than two of the layers that form the multilayer film are applied by a wet-on-wet application method.
  • the application in i3), i5) etc. can thus be effected wet-on-wet, meaning that the next layer can also be applied to the layer applied in step i 1 ), i3) and/or i5) without an explicit step for increasing viscosity having been conducted beforehand. This is especially true when the layer to which the next polymer layer is applied is sufficiently thin, such that it solidifies sufficiently even without being explicitly left to stand, dried, heated, cured, etc. before the next layer is applied, and there is no complete mixing with the components of the next layer.
  • the polymers applied in steps i 1 ), i3), i5) etc. are film-forming polymers.
  • One or more than one of the layers comprising film-forming polymers may additionally comprise at least one additive.
  • any film-forming polymers are especially layers comprising components (functional materials) connected to the desired end use of the multi layer film.
  • these optional further layers may comprise surfactants, builders, cobuilders, bleaches, enzymes, graying inhibitors, optical brighteners, fragrances, dyes, etc.
  • surfactants may, like the polymer layers too, be applied in solution/dispersion or melt. Suitable application techniques here too are those mentioned above.
  • This can be effected by means of standard embossing, printing, stamping and punching tools.
  • the process of the invention allows the production of multilayer films without a complex lamina- tion method in which the individual films have to be bonded to one another.
  • the multilayer films of the invention can also be produced, as described above, by bond ing two or more than two film layers to one another by laminating.
  • multilaminar polymer films which serve as carrier material for application of further film layers may be provided by bonding two or more than two film layers to one another by laminating.
  • a component which is capable of film formation and is selected from polymer compositions P1 , at least one polymer P2, optionally after addition of at least one additive, is melted or dissolved in a suitable solvent or solvent mixture, the pourable composition thus obtained is poured out to form a layer and the solvent or solvent mixture is optionally removed by evaporation.
  • the solvent is preferably selected from water, ethanol, n-propanol, isopropanol, ethylene glycol, diethylene glycol, 1 ,2-propylene glycol, 1 ,2-dipropylene glycol and mixtures thereof.
  • the solvent used is selected from water and a mixture of water and at least one solvent other than water, selected from ethanol, n-propanol, isopropanol, ethylene glycol, diethylene glycol, 1 ,2-propylene glycol, 1 ,2-dipropylene glycol and mixtures thereof.
  • the multilayer film can be applied to a steel belt or a heated roller using single or multi-layer casting or coating tools such as slot nozzles, doctor blade, curtain coating, cascade casting, etc.
  • one or more layers can be applied simultaneously and the other layers optionally on a different position of the steel strip or the roller.
  • another layer can be applied in a post-drying step on the freestanding film after detaching from the carrier material (steel strip or roller). Roller-based coating processes are particularly suitable for this subsequent coating.
  • a lamination step can also be carried out with a pre viously prepared or commercially available film.
  • the laminating step of the films may be carried out before detaching a film, immediately after detaching the film and before drying of the freestanding film, during the drying of the freestanding film or after the drying, but before the wind ing.
  • a separate lamination of two films is also possible.
  • lamination is possible solely by means of a targeted adjustment of the residual moisture in the film and correspondingly selected line loads.
  • a specific embodiment is a process for producing a washing- and cleaning-active single layer or multilayer polymer film, which comprises at least one additive.
  • Additives can be added before or during the film formation in step b). Whether the addition takes place before or during step b) depends on the type and effect of the particular additive.
  • additives can be added to the aqueous composition before and/or during the film production.
  • an individual layer or a plurality of but not all the layers or all the layers may each comprise one or more than one additive.
  • at least one additive is present between at least two layers.
  • the additives may be auxiliaries for adjustment of the properties of the pourable compositions capable of film formation, typical additives of the washing and cleaning compositions or mixtures thereof.
  • a special embodiment is a single layer film that comprises at least one additive.
  • a further special embodiment is a multilayer film in which at least one of the layers includes an additive. Particular preference is given to single layer and multilayer films in which at least one of the layers includes an additive which is a constituent customary for washing and cleaning compositions.
  • the additive is preferably selected from nonionic, anionic, cationic and amphoteric surfactants, builders, complexing agents such as methylglycinediacetic acid, glutaminediacetic acid, glutamic acid diacetic acid and citric acid and the sodium and potassium salts thereof, bleaches, bleach activators, bleach catalysts, enzymes, bases, corrosion inhibitors, foam inhibitors, defoamers, wetting agents, dyes, pigments, fragrances, bitter agents such as Bitrex ® , antiyellowing agents, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, bitter substances, fluorescers, hydrotropes, antiredeposition agents, optical brighteners, graying inhibitors, antishrink agents, anticrease agents, dye transfer inhibitors, antimicrobial active ingredients, antioxidants, anti-yellowing agents, cor rosion inhibitors, antistats, ironing aids, hydrophob
  • wash-active layer comprising or consisting of P1 ) or P2), may serve not only the purpose of being wash-active, but also can be used as lamination adhesive, due to their special compo sitions and associated properties (tackiness).
  • the residual moisture of the wash-active layer comprising or consisting of P1 ) or P2, is prefer ably lower than 15 % by weight, more preferably equal to or lower than 10 % by weight.
  • the temperature during the lamination process is preferably lower than 100 °C, more preferably lower than 80 °C, even more preferably lower than 50 °C and most preferably lower than 30 °C.
  • at least one layer, preferably an enzyme-containing layer is laminated at room temperature onto any of the other layers.
  • plasticizers can be added to them before or during production.
  • plasticizers preferably 0.5% to 30% by weight, more preferably 2% to 20% by weight and especially 3% to 15% by weight of plasticizer is used, based on the total weight of the composition.
  • Suitable plasticizers are alkyleneamines, alkanolamines, polyols, such as alkylene glycols and oligoalkylene glycols, e.g. 2-methyl-1 ,3-propanediol, 3-methyl-1 ,5-pentadiol, hydroxypropylglyc- erol, neopentyl glycol, alkoxylated glycerol (such as e.g. Voranol ® from Dow Chemicals), water- soluble polyesterpolyols (such as e.g. TriRez from Geo Specialty Chemicals) and mixtures thereof.
  • alkyleneamines alkanolamines
  • polyols such as alkylene glycols and oligoalkylene glycols, e.g. 2-methyl-1 ,3-propanediol, 3-methyl-1 ,5-pentadiol, hydroxypropylglyc- erol, neopen
  • Suitable plasticizers are also polyetherpolyols, which are available under the name Lu- pranol ® from BASF SE.
  • alkyleneamines refers to condensation products of alka- nolamines with ammonia or primary amines, e.g. ethyleneamines are obtained by reaction of monoethanolamine with ammonia in the presence of a catalyst.
  • ethylenediamine, piperazine, diethylenetriamine and aminoethylethanola- mine are also polyetherpolyols, which are available under the name Lu- pranol ® from BASF SE.
  • alkyleneamines refers to condensation products of alka- nolamines with ammonia or primary amines, e.g. ethyleneamines are obtained by reaction of monoethanolamine with ammonia in the presence of a catalyst.
  • main components ethylenediamine, piperazine, diethylenetriamine and aminoethylethanola- mine.
  • the plasticizers are selected from glycerol, diglycerol, propylene glycols with a weight-average molecular weight of up to 400, e.g. dipropylene glycol, ethylene glycol, diethylene glycol, triethylene glycol, tetraethylene glycol, sorbitol, isopentyldiol, polyethylene glycol, trimethylolpropane, diethylenetriamine, triethylenepentamine, triethanolamine and mixtures thereof.
  • glycerol diglycerol
  • propylene glycols with a weight-average molecular weight of up to 400, e.g. dipropylene glycol, ethylene glycol, diethylene glycol, triethylene glycol, tetraethylene glycol, sorbitol, isopentyldiol, polyethylene glycol, trimethylolpropane, diethylenetriamine, triethylenepentamine, triethanolamine and mixtures thereof.
  • scavengers capture molecules
  • Suitable scavengers are polyamines, polymeric polyamines, such as polyethyleneimines,
  • poly(amidoamines) and polyamides are also possible to use ammonium sulfate, primary and secondary amines with a low vapor pressure, such as ethanolamines, amino acid and salts thereof, and also polyamino acid and salts thereof, fatty amines, glucosamines and other aminated sugars.
  • reducing agents such as sulfites, bisulfites, thiosulfites, thiosulfates, iodides, nitrites and antioxidants such as carbamates, ascorbates and mixtures thereof can be used.
  • At least one surface or both surfaces of the single and multilayer films of the invention may be subject to at least partial coating with at least one additive.
  • a treatment may serve, for example, to provide the surface with particular properties, such as nonstick action, antistatic action, hydrophilic or hydrophobic properties, etc.
  • the single and multilayer films for example, with better detachment properties from the carrier material used in the production, better roll-off properties, better glide properties, reduced tack, better compatibility with particular components ensheathed or coated therewith, etc.
  • the application can be effected by standard methods, for example by spraying, dipping, powder application, etc.
  • Suitable additives for coating of the sur face of the multilayer films of the invention are, for example, talc, surfactants such as silicone- containing surfactants, waxes, etc.
  • a further subject of the present invention is a process for producing a water-soluble container comprising the steps of:
  • At least one of the first or second water-soluble films is a multi-layered film as above, and wherein before the sealing step the second water-soluble film covering the filled pouch is contacted with water.
  • an inventive multilayer film or obtainable by an inventive process, as a washing composition or as a cleaning composition is a subject of the present invention.
  • a further inventive subject is the use of a multilayer film as defined above or obtainable by a process as defined above, for at least partial ensheathing of a liquid and/or solid washing and cleaning composition.
  • Another inventive subject is a sheath or coating for a washing composition portion or cleaning composition portion, comprising or consisting of a multilayer film as defined above or obtainable by a process as defined above.
  • a subject of the invention is also a washing or cleaning composition
  • a washing or cleaning composition comprising:
  • At least one sheath and/or coating comprising or consisting of a washing- and cleaning- active multilayer film as defined above or obtainable by a process as defined above,
  • further additive preferably selected from enzymes, bases, corro- sion inhibitors, defoamers, dyes, fragrances, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, fluores- cers, hydrotropes
  • the enzyme EN is preferably selected from an oxidoreductase (EC 1), a transferase (EC 2), a hydrolase (EC 3), a lyase (EC 4), a Isomerase (EC 5), or a Ligase (EC 6) (EC-numbering according to Enzyme Nomenclature, Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology in cluding its supplements published 1993-1999).
  • EC 1 oxidoreductase
  • EC 2 transferase
  • hydrolase EC 3
  • a lyase EC 4
  • Isomerase EC 5
  • Ligase EC 6
  • the enzyme is a hydrolase (EC 3), preferably, a glycosidase (EC 3.2) or a pep tidase (EC 3.4).
  • Especially preferred enzymes are enzymes selected from the group consisting of an amylase (in particular an alpha-amylase (EC 3.2.1.1 )), a cellulase (EC 3.2.1.4), a lactase (EC 3.2.1 .108), a mannanase (EC 3.2.1.25), a lipase (EC 3.1.1.3), a phytase (EC 3.1.3.8), a nuclease (EC 3.1 .1 1 to EC 3.1.31 ), and a protease (EC 3.4).
  • an amylase in particular an alpha-amylase (EC 3.2.1.1 )
  • a cellulase EC 3.2.1.4
  • a lactase EC 3.2.1 .108
  • a mannanase
  • the enzyme EN is preferably selected from the group consisting of proteases, amylases, lipases, cellulases, perhydrolases, mannanases, nucleases, peroxidases, oxidases, lyases, pectinases, arabinases, galactanases, xylanases, and mixtures thereof.
  • Enzymes are generally produced commercially by using recombinant cells which express the desired enzyme by cultivation of the same under conditions suitable for expression of the desired enzyme.
  • the term“recombinant cell” (also called“genetically modified cell” herein) refers to a cell which has been genetically altered, modified or engineered such that it exhibits an altered, modified or different genotype as compared to the wild-type cell which it was derived from.
  • The“recombinant cell” may comprise an exogenous polynucleotide.
  • the recombinant cell may comprise exogenous polynucleotide encoding for a certain protein or enzyme and therefore may express said protein or enzyme.
  • heterologous or exogenous or foreign or recombinant polypeptide is defined herein as a polypeptide that is not native to the host cell, a polypeptide native to the host cell in which structural modifications, e.g., deletions, substitutions, and/or insertions, have been made to alter the native polypeptide, or a polypeptide native to the host cell whose expression is quantitatively altered or whose expression is directed from a genomic location different from the native host cell as a result of manipulation of the DNA of the host cell by recombinant DNA techniques, e.g., a stronger promoter.
  • heterologous refers to a polynucleotide that is not native to the host cell, a polynucleotide native to the host cell in which structural modifications, e.g., deletions, substitutions, and/or insertions, have been made to alter the native polynucleotide, or a polynucleotide native to the host cell whose expression is quantitatively altered as a result of manipulation of the regulatory elements of the polynucleotide by recombinant DNA techniques, e.g., a stronger promoter, or a polynucleotide native to the host cell, but integrated not within its natural genetic environment as a result of genetic manipulation by recombinant DNA techniques.
  • heterologous is used to characterized that the two or more polynucleotide sequences or two or more amino acid sequences are naturally not occurring in the specific combination with each other.
  • nucleotide or polypeptide refers to the cell or organism as found in nature and to the polynucleotide or polypeptide in question as found in a cell in its natural form and genetic environment, respectively (i.e., without there being any human intervention).
  • Cultivation normally takes place in a suitable nutrient medium allowing the recombinant host cells to grow (this process may be called fermentation) and express the desired protein.
  • fermentation broth is collected and may be further processed, wherein the fermentation broth comprises a liquid fraction and a solid fraction.
  • the desired protein or enzyme may be secreted (into the liquid fraction of the fermentation broth) or may not be secreted from the host cells (and therefore is comprised in the solid frac tion of the fermentation broth). Depending on this, the desired protein or enzyme may be recovered from the liquid fraction of the fermentation broth or from cell lysates. Recovery of the de- sired enzyme uses methods known to those skilled in the art. Suitable methods for recovery of proteins or enzymes from fermentation broth include but are not limited to collection, centrifugation, filtration, extraction, and precipitation.
  • the isolated polypeptide may then be further purified by a variety of procedures known in the art including, but not limited to, chromatography (e.g., ion exchange, affinity, hydrophobic, chroma- tofocusing, and size exclusion), electrophoretic procedures (e.g., preparative isoelectric focus- ing (IEF), differential solubility (e.g., ammonium sulfate precipitation), or extraction (see, e.g., Protein Purification, J.-C. Janson and Lars Ryden, editors, VCH Publishers, New York, 1989).
  • the purified polypeptide may then be concentrated by procedures known in the art including, but not limited to, ultrafiltration and evaporation, in particular, thin film evaporation.
  • the final enzyme-comprising product may be liquid or aqueous and may be called enzyme concentrate.
  • Liquid enzyme-comprising products may be dried to stabilize enzyme(s).
  • dried enzymes need to be re-solved in solvent such as water or water-containing buffer prior to use.
  • solvent such as water or water-containing buffer prior to use.
  • enzyme-comprising products are often aqueous before they are used in applications.
  • Liquid enzyme concentrate herein means any liquid enzyme-comprising product comprising at least one type of enzyme.“Liquid” in the context of enzyme concentrate is related to the physi cal appearance at 20°C and 101.3 kPa.
  • Liquid enzyme concentrates may comprise amounts of enzyme in the range of 0.1 % to 40% by weight, or 0.5% to 30% by weight, or 1 % to 25% by weight, all relative to the total weight of the enzyme concentrate.
  • the liquid enzyme concentrate may comprise more than one type of enzyme.
  • liquid enzyme concentrate is an aqueous enzyme concentrate.
  • Aqueous enzyme concentrate herein means any aqueous enzyme-comprising product comprising at least one type of enzyme, which may result e.g. from fermentation.
  • Aqueous enzyme concentrate may also mean that at least one type of enzyme in its solid state has been dissolved in aqueous solvent.
  • Aqueous enzyme concentrates of the invention may comprise water in amounts of more than about 50% by weight, more than about 60% by weight, more than about 70% by weight, or more than about 80% by weight, all relative to the total weight of the enzyme concentrate.
  • Liquid enzyme concentrate of the invention may comprise residual components such as salts originating from the fermentation medium, cell debris originating from the production host cells, metabolites produced by the production host cells during fermentation.
  • residual components may be comprised in liquid enzyme concentrates in amounts less than 30% by weight, less than 20% by weight less, than 10% by weight, or less than 5% by weight, all relative to the total weight of the aqueous enzyme concentrate.
  • the water-soluble multilayer film of the invention comprises at least one lipase.“Lipases”,“lipolytic enzyme”,“lipid esterase”, all refer to an enzyme of EC class 3.1.1 (“carboxylic ester hydrolase”).
  • Such an enzyme may have lipase activity (or lipolytic activity; triacylglycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74; enzymes having cutinase ac- tivity may be called cutinase herein), sterol esterase activity (EC 3.1.1.13) and/or wax-ester hydrolase activity (EC 3.1.1.50).
  • Lipases include those of bacterial or fungal origin.
  • lipase enzymes include but are not limited to those sold under the trade names LipolaseTM, LipexTM, LipolexTM and LipocleanTM (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (Gist-Brocades/ now DSM).
  • a suitable lipase is selected from the following: lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa ( T. lanuginosus) as described in EP 258068, EP 305216, WO 92/05249 and WO 2009/109500 or from H. inso/ens as described in WO 96/13580,
  • Bacillus lipases e.g. as disclosed in WO 00/60063, lipases from B. subtilis es disclosed in Dartois et al. (1992), Biochemica et Biophysica Acta, 1 131 , 253-360 or WO 201 1/084599, B. stearothermophilus (JP S64-074992) or B. pumi/us (WO 91/16422).
  • Suitable lipases include also those referred to as acyltransferases or perhydrolases, e.g. acyl- transferases with homology to Candida antarctica lipase A (WO 2010/1 1 1 143), acyltransferase from Mycobacterium smegmatis (WO 2005/056782), perhydrolases from the CE7 family (WO 2009/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant (WO 2010/100028).
  • acyltransferases or perhydrolases e.g. acyl- transferases with homology to Candida antarctica lipase A (WO 2010/1 1 1 143), acyltransferase from Mycobacterium smegmatis (WO 2005/056782), perhydrolases from the CE7 family (WO 2009/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant
  • Suitable lipases include also those which are variants of the above described lipases and/or cutinases which have lipolytic activity.
  • Such suitable lipase variants are e.g. those which are developed by methods as disclosed in WO 95/22615, WO 97/04079, WO 97/07202, WO 00/60063, WO 2007/087508, EP 407225 and EP 260105.
  • Suitable lipases/cutinases include also those, which are variants of the above described lipas- es/cutinases which have lipolytic activity.
  • Suitable lipase/cutinase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
  • lipase/cutinase variants having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of the parent en- zyme as disclosed above.
  • the invention relates to lipase/cutinase variants comprising conservative mutations not pertaining the functional domain of the respective lipase/cutinase.
  • Li pase/cutinase variants of this embodiment having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least
  • Enzyme variants may be defined by their sequence identity when compared to a parent en- zyme. Sequence identity usually is provided as“% sequence identity” or“% identity”. To determine the percent-identity between two amino acid sequences in a first step a pairwise sequence alignment is generated between those two sequences, wherein the two sequences are aligned over their complete length (i.e., a pairwise global alignment). The alignment is generated with a program implementing the Needleman and Wunsch algorithm (J. Mol. Biol. (1979) 48, p.
  • the preferred alignment for the purpose of this invention is that alignment, from which the highest sequence identity can be determined.
  • %-identity (identical residues / length of the alignment region which is showing the respective sequence of this invention over its complete length) * 100.
  • sequence identity in relation to comparison of two amino acid sequences according to this embodiment is calculated by dividing the number of identical residues by the length of the alignment region which is showing the re spective sequence of this invention over its complete length. This value is multiplied with 100 to give“%-identity”.
  • the pairwise alignment shall be made over the complete length of the coding region from start to stop codon excluding introns.
  • the pairwise alignment shall be made over the complete length of the sequence of this invention, so the complete sequence of this invention is compared to another sequence, or regions out of another sequence.
  • Seq B GATCTGA length: 7 bases
  • sequence B is sequence B.
  • the ⁇ ” symbol in the alignment indicates identical residues (which means bases for DNA or amino acids for proteins). The number of identical residues is 6.
  • the symbol in the alignment indicates gaps.
  • the number of gaps introduced by alignment within the Seq B is 1.
  • the number of gaps introduced by alignment at borders of Seq B is 2, and at borders of Seq A is 1.
  • the alignment length showing the aligned sequences over their complete length is 10.
  • the alignment length showing the shorter sequence over its complete length is 8 (one gap is present which is factored in the alignment length of the shorter sequence).
  • the alignment length showing Seq A over its complete length would be 9 (meaning Seq A is the sequence of the invention).
  • the alignment length showing Seq B over its complete length would be 8 (meaning Seq B is the sequence of the invention).
  • Enzyme variants may be defined by their sequence similarity when compared to a parent en zyme. Sequence similarity usually is provided as“% sequence similarity” or“%-similarity”. For calculating sequence similarity in a first step a sequence alignment has to be generated as described above. In a second step, the percent-similarity has to be calculated, whereas percent sequence similarity takes into account that defined sets of amino acids share similar properties, e.g., by their size, by their hydrophobicity, by their charge, or by other characteristics.
  • the exchange of one amino acid with a similar amino acid is referred to as‘‘conservative muta tion”. Enzyme variants comprising conservative mutations appear to have a minimal effect on protein folding resulting in certain enzyme properties being substantially maintained when compared to the enzyme properties of the parent enzyme.
  • %-similarity For determination of %-similarity according to this invention the following applies, which is also in accordance with the BLOSUM62 matrix, which is one of the most used amino acids similarity matrix for database searching and sequence alignments
  • Amino acid A is similar to amino acids S
  • Amino acid D is similar to amino acids E; N
  • Amino acid E is similar to amino acids D; K; Q
  • Amino acid F is similar to amino acids W; Y
  • Amino acid H is similar to amino acids N; Y
  • Amino acid I is similar to amino acids L; M; V;
  • Amino acid K is similar to amino acids E; Q; R
  • Amino acid L is similar to amino acids I; M; V
  • Amino acid M is similar to amino acids I; L; V
  • Amino acid N is similar to amino acids D; H; S;
  • Amino acid Q is similar to amino acids E; K; R
  • Amino acid R is similar to amino acids K; Q
  • Amino acid S is similar to amino acids A; N; T
  • Amino acid T is similar to amino acids S
  • Amino acid V is similar to amino acids I; L; M
  • Amino acid W is similar to amino acids F; Y
  • Amino acid Y is similar to amino acids F; H; W.
  • Conservative amino acid substitutions may occur over the full length of the sequence of a poly peptide sequence of a functional protein such as an enzyme. In one embodiment, such mutations are not pertaining the functional domains of an enzyme. In another embodiment conservative mutations are not pertaining the catalytic centers of an enzyme.
  • %-similarity [ (identical residues + similar residues) / length of the alignment region which is showing the respective sequence of this invention over its complete length ] * 100.
  • se quence similarity in relation to comparison of two amino acid sequences herein is calculated by dividing the number of identical residues plus the number of similar residues by the length of the alignment region which is showing the respective sequence of this invention over its complete length. This value is multiplied with 100 to give“%-similarity”.
  • variant enzymes comprising conservative mutations which are at least m percent similar to the respective parent sequences with m being an integer between 50 and 100, prefer ably 50, 55, 60, 65, 70, 75, 80, 85, 90, 91 , 92, 93, 94, 95, 96, 97, 98 or 99 compared to the full length polypeptide sequence, are expected to have essentially unchanged enzyme properties.
  • Variant enzymes described herein with m percent-similarity when compared to a parent en- zyme have enzymatic activity.
  • Lipases according to the invention have“lipolytic activity”.
  • the methods for determining lipolytic activity are well-known in the literature (see e.g. Gupta et al. (2003), Biotechnol. Appl. Biochem. 37, p. 63-71).
  • the lipase activity may be measured by ester bond hydrolysis in the substrate para-nitrophenyl palmitate (pNP-Palmitate, C:16) and releases pNP which is yellow and can be detected at 405 nm.
  • Lipase variants may have lipolytic activity according to the present invention when said lipase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the lipolytic activity of the re spective parent lipase.
  • the water-soluble multilayer film of the invention comprises at least one protease.
  • Enzymes having proteolytic activity are called“proteases” or peptidases in the context of the invention and are members of class EC 3.4.
  • Preferred proteases are further classified as aminopeptidases (EC 3.4.11 ), dipeptidases (EC 3.4.13), dipeptidyl-peptidases and tripeptidyl-peptidases (EC 3.4.14), peptidyl-dipeptidases (EC 3.4.15), serine-type carboxypeptidases (EC 3.4.16), metallocarboxypeptidases (EC 3.4.17), cysteine-type carboxypeptidases (EC 3.4.18), omega peptidases (EC 3.4.19), serine endopep- tidases (EC 3.4.21 ), cysteine endopeptidases (EC 3.4.22), aspartic endopeptidases (EC 3.4.23), metallo-endopeptidases (EC 3.4.24), threonine endopeptidases (EC 3.4.25), endopep tidases of unknown catalytic mechanism (EC 3.4.99).
  • aminopeptidases EC 3.4.11
  • protease in the context of the present invention may be an endopeptidase of any kind or a mixture of endopeptidases of any kind.
  • protease according to the invention is selected from serine protease (EC 3.4.21).
  • Serine proteases or serine peptidases are characterized by having a serine in the catalytically active site, which forms a covalent adduct with the substrate during the catalytic reaction.
  • a ser ine protease according to the invention is selected from the group consisting of chymotrypsin (e.g., EC 3.4.21.1), elastase (e.g., EC 3.4.21.36), elastase (e.g., EC 3.4.21.37 or EC 3.4.21.71 ), granzyme (e.g., EC 3.4.21.78 or EC 3.4.21 .79), kallikrein (e.g., EC 3.4.21.34, EC 3.4.21.35, EC 3.4.21.118, or EC 3.4.21.119,) plasmin (e.g., EC 3.4.21.7), trypsin (e.g., EC 3.4.21.4), thrombin (e.g., EC 3.4.21.5,) and subtilisin (also known as subtilopeptidase, e.g., EC 3.4.21.62), the latter hereinafter also being referred to as“subtilisin”.
  • protease activity In general, the three main types of protease activity (proteolytic activity) are: trypsin-like, where there is cleavage of amide substrates following Arg (N) or Lys (K) at P1 , chymotrypsin-like where cleavage occurs following one of the hydrophobic amino acids at P1 , and elastase-like with cleavage following an Ala (A) at P1.
  • subtilases A sub-group of the serine proteases tentatively designated subtilases has been proposed by Siezen et al. (1991), Protein Eng. 4:719-737 and Siezen et al. (1997), Protein Science 6:501 - 523. They are defined by homology analysis of more than 170 amino acid sequences of serine proteases previously referred to as subtilisin-like proteases. A subtilisin was previously often defined as a serine protease produced by Gram-positive bacteria or fungi, and according to Siezen et al. now is a subgroup of the subtilases. A wide variety of subtilases have been identified, and the amino acid sequence of a number of subtilases has been determined. For a more detailed description of such subtilases and their amino acid sequences reference is made to Siezen et al. (1997), Protein Science 6:501 -523.
  • the subtilases may be divided into 6 sub-divisions, i.e. the subtilisin family, thermitase family, the proteinase K family, the lantibiotic peptidase family, the kexin family and the pyrolysin family.
  • subtilisins which are serine proteases from the family S8 as defined by the MEROPS database (http://merops.sanger.ac.uk).
  • Peptidase family S8 con tains the serine endopeptidase subtilisin and its homologues.
  • subfamily S8A the active site residues frequently occurs in the motifs Asp-Thr/Ser-Gly (which is similar to the sequence motif in families of aspartic endopeptidases in clan AA), His-Gly-Thr-His and Gly-Thr-Ser-Met-Ala- Xaa-Pro.
  • Most members of the family are active at neutral-mildly alkali pH.
  • Many peptidases in the family are thermostable.
  • Casein is often used as a protein substrate and a typical synthetic substrate is Suc-Ala-Ala-Pro-Phe-NHPhN02.
  • Prominent members of family S8, subfamily A are:
  • subtilisin related class of serine proteases shares a common amino acid sequence defining a catalytic triad which distinguishes them from the chymotrypsin related class of serine proteases.
  • subtilisin In the subtilisin related proteases the relative order of these amino acids, reading from the amino to carboxy-terminus is aspartate-histidine-serine. In the chymotrypsin related proteases the relative order, however is histidine-aspartate-serine.
  • subtilisin herein refers to a serine protease having the catalytic triad of subtilisin related proteases. Examples include the subtilisins as described in WO 89/06276 and EP 0283075, WO 89/06279, WO 89/09830, WO 89/09819, WO 91/06637 and WO 91/02792.
  • Parent proteases of the subtilisin type (EC 3.4.21.62) and variants may be bacterial proteases.
  • Said bacterial protease may be a Gram-positive bacterial polypeptide such as a Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacitius, Staphylococcus, Streptococcus, or Streptomyces protease, or a Gram-negative bacterial polypeptide such as a Campylobacter, E. co/i, Flavobacterium, Fusobacterium, Helicobacter, Hyobacter, Neisseria, Pseudomonas, Salmonella, or Ureaptasma protease.
  • protease enzymes include those sold under the trade names Alcalase®, Blaze®, DuralaseTM, DurazymTM, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Pri- mase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Co- ronase® Ultra, Neutrase®, Everlase® and Esperase® (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect® Prime, Purafect MA®, Purafect Ox®, Purafect OxP®, Puramax®, Properase®, FN2®, FN3®, FN4®, Excellase®, Eraser®, Ultimase®, Opticlean®, Effectenz®, Preferenz® and Optimase®
  • the parent enzymes and variants may be a Bacillus alcalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circuians, Bacillus c/ausii, Bacillus coagu- lans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus Hcheniformis, Bacillus megaterium, Bacillus pumiius, Bacillus sphaericus , Bacillus stearothermophilus, Bacil lus subti!is, or Bacillus thuringiensis protease.
  • subtilase is selected from the following:
  • subtilisin from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J. Bacteriol. Volume 159, p. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume 1 1 , p. 791 1-7925),
  • subtilisin from Bacillus Hcheniformis subtilisin Carlsberg; disclosed in EL Smith et al. (1968) in J. Biol Chem, Volume 243, pp. 2184-2191 , and Jacobs et al. (1985) in Nucl. Ac- ids Res, Vol 13, p. 8913-8926),
  • subtilisin PB92 original sequence of the alkaline protease PB92 is described in EP 283075 A2)
  • subtilisin 147 and/or 309 (Esperase®, Savinase®) as disclosed in GB 1243784, subtilisin from Bacillus lentus as disclosed in WO 91/02792, such as from Bacillus lentus
  • subtilisin from Bacillus gibsonii ⁇ DSM 14391 as disclosed in WO 2003/054184, subtilisin from Bacillus sp. (DSM 14390) disclosed in WO 2003/056017,
  • subtilisin from Bacillus sp. (DSM 14392) disclosed in WO 2003/055974,
  • subtilisin having SEQ ID NO: 4 as described in WO 2005/063974 or a subtilisin which is at least 40% identical thereto and having proteolytic activity,
  • subtilisin having SEQ ID NO: 4 as described in WO 2005/103244 or subtilisin which is at least 80% identical thereto and having proteolytic activity
  • subtilisin having SEQ ID NO: 7 as described in WO 2005/103244 or subtilisin which is at least 80% identical thereto and having proteolytic activity
  • subtilisin having SEQ ID NO: 2 as described in application DE 102005028295.4 or subtil isin which is this at least 66% identical thereto and having proteolytic activity.
  • Examples of useful proteases in accordance with the present invention comprise the variants described in: WO 92/19729, WO 95/23221 , WO 96/34946, WO 98/20115, WO 98/20116, WO 99/1 1768, WO 01/44452, WO 02/088340, WO 03/006602, WO 2004/03186, WO 2004/041979, WO 2007/006305, WO 201 1/036263, WO 2011/036264, and WO 201 1/072099.
  • Suitable exam ples comprise especially protease variants of subtilisin protease derived from SEQ ID NO:22 as described in EP 1921 147 (which is the sequence of mature alkaline protease from Bacillus len tus DSM 5483) with amino acid substitutions in one or more of the following positions: 3, 4, 9,
  • subtilisin protease is not mutated at positions Asp32, His64 and Ser221 (according to BPN’ numbering).
  • the subtilisin has SEQ ID NO:22 as described in EP 1921 147, or a subtilisin which is at least 80% identical thereto and has proteolytic activity.
  • a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is charac terized by having amino acid glutamic acid (E), or aspartic acid (D), or asparagine (N), or glutamine (Q), or alanine (A), or glycine (G), or serine (S) at position 101 (according to BPN’ numbering) and has proteolytic activity.
  • subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by having amino acid glutamic acid (E), or aspartic acid (D), at position 101 (according to BPN’ numbering) and has proteolytic activity.
  • Such a subtilisin variant may comprise an amino acid substitution at position 101 , such as R101 E or R101 D, alone or in combination with one or more substitutions at positions 3, 4, 9, 15, 24, 27, 33, 36, 57, 68, 76, 77, 87, 95, 96, 97, 98, 99, 100, 101 , 102, 103, 104, 106, 118, 120, 123, 128, 129, 130, 131 , 154, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and/or 274 (according to BPN’ numbering) and has proteolytic activity.
  • a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by comprising at least the following amino acids (according to BPN’ numbering) and has proteolytic activity:
  • a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by comprising one amino acid (according to (a)-(h)) or combinations according to (i) together with the amino acid 101 E, 101 D, 101 N, 101 Q, 101 A, 101 G, or 101 S (according to BPN’ numbering) and has proteolytic activity.
  • a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921147 and is characterized by comprising the mutation (according to BPN’ numbering) R101 E, or S3T + V4I + V205I, or S3T + V4I + V199M + V205I + L217D, and has proteolytic activity.
  • the subtilisin comprises an amino acid sequence having at least 80% identity to SEQ ID NO:22 as described in EP 1921147 and being further characterized by com prising R101 E and S3T, V4I, and V205I (according to the BPN’ numbering) and has proteolytic activity.
  • a subtilisin comprises an amino acid sequence having at least 80% identical to SEQ ID NO:22 as described in EP 1921147 and being further characterized by comprising R101 E, and one or more substitutions selected from the group consisting of S156D, L262E, Q137H, S3T, R45E,D,Q, P55N, T58W,Y,L, Q59D,M,N,T, G61 D,R, S87E, G97S, A98D,E,R, S106A,W, N1 17E, H120V,D,K,N, S125M, P129D, E136Q, S144W, S161 T,
  • subtilisin variant enzymes as disclosed above which are at least n% identical to the respective parent sequences include variants with n being at least 40 to 100.
  • subtilisin variants in one embodiment have proteolytic activity and are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical when compared to the full length polypeptide sequence of the parent enzyme.
  • subtilisin variants comprising conservative mu tations not pertaining the functional domain of the respective subtilisin protease.
  • subtilisin variants of this embodiment have proteolytic activity and are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full length polypeptide sequence of the parent enzyme.
  • proteolytic activity or “protease activity” or“proteolytic activity”.
  • This property is related to hydrolytic activity of a pro- tease (proteolysis, which means hydrolysis of peptide bonds linking amino acids together in a polypeptide chain) on protein containing substrates, e.g. casein, haemoglobin and BSA.
  • proteolytic activity is related to the rate of degradation of protein by a protease or proteolytic enzyme in a defined course of time.
  • the methods for analyzing proteolytic activity are well-known in the literature (see e.g. Gupta et al. (2002), Appl. Microbiol. Biotechnol. 60: 381 - 395).
  • proteolytic activity as such can be determined by using Succinyl-Ala- Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, short AAPF; see e.g. DelMar et al. (1979), Analytical Biochem 99, 316-320) as substrate.
  • pNA is cleaved from the substrate molecule by proteo- lytic cleavage, resulting in release of yellow color of free pNA which can be quantified by meas- uring OD405.
  • Other methods are known to those skilled in the art.
  • Protease variants may have proteolytic activity according to the present invention when said protease variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the proteolytic activity of the respective parent protease.
  • the pi value (isoelectric point) of the subtilisin protease is between pH 7.0 and pH 10.0, preferably between pH 8.0 and pH 9.5.
  • the water-soluble multilayer film of the invention comprises at least one amylase.“Amylases” according to the invention (alpha and/or beta) include those of bacterial or fungal origin (EC 3.2.1.1 and 3.2.1.2, respectively). Chemically modified or protein engineered mutants are included.
  • amylase enzymes include but are not limited to those sold under the trade names DuramylTM, TermamylTM, FungamylTM, StainzymeTM, Stainzyme PlusTM, Natala- seTM, Liquozyme X and BANTM (from Novozymes A/S), and RapidaseTM, PurastarTM,
  • amylase is a parent or variant enzyme which is selected from the following:
  • Suitable variants are those which are at least 90% identical to SEQ ID NO: 2 as described in WO 95/10603 and/or comprising one or more substitutions in the following positions:
  • Suitable variants of SEQ ID NO:6 include those which is at least 90% identical thereto and/or further comprise a deletion in positions 181 and/or 182 and/or a substitution in position 193.
  • Suitable amylases are comprising amino acids 1 to 485 of SEQ ID NO:2 as described in WO 00/60060 or amylases comprising an amino acid sequence which is at least 96% identical with amino acids 1 to 485 of SEQ ID NO:2 which have amylolytic activity.
  • Suitable amylases are those having SEQ ID NO: 12 as described in WO 2006/002643 or amylases having at least 80% identity thereto and have amylolytic activity.
  • Suitable amylases include those having at least 80% identity compared to SEQ ID NO:12 and/or comprising the substitutions at positions Y295F and M202LITV and have amylolytic activity.
  • Suitable amylases include those having SEQ ID NO:6 as described in WO 2011/098531 or am ylases having at least 80% identity thereto having amylolytic activity. Suitable amylases include those having at least 80% identity compared to SEQ ID NO:6 and/or comprising a substitution at one or more positions selected from the group consisting of 193 [G,A,S,T or M], 195
  • Suitable amylases are those having SEQ ID NO:1 as described in WO 2013/001078 or amylas es having at least 85% identity thereto having amylolytic activity.
  • Suitable amylases include those having at least 85% identity compared to SEQ ID NO:1 and/or comprising an alteration at two or more (several) positions corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476, and G477 and having amylolytic activity.
  • amylases are those having SEQ ID NO:2 as described in WO 2013/001087 or amylases having at least 85% identity thereto and having amylolytic activity.
  • Suitable amylases include those having at least 85% identity compared to SEQ ID NO:2 and/or comprising a dele- tion of positions 181 +182, or 182+183, or 183+184, which have amylolytic activity.
  • Suitable am ylases include those having at least 85% identity compared to SEQ ID NO:2 and/or comprising a deletion of positions 181 +182, or 182+183, or 183+184, which comprise one or two or more modifications in any of positions corresponding to W140, W159, W167, Q169, W189, E194, N260, F262, W284, F289, G304, G305, R320, W347, W439, W469, G476 and G477 and have amylolytic activity.
  • Amylases also include hybrid a-amylase from above mentioned amylases as for example as described in WO 2006/066594.
  • Suitable amylases include also those which are variants of the above described amylases which have amylolytic activity.
  • amylase variants in one embodiment may be those which are least 40 to 100% identical when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
  • amylase variants having amylolytic activity may be at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
  • amylase variants comprising conservative mutations not pertaining the functional domain of the respective amylase.
  • amylase variants in this embodiment may be amylases have amylolytic activity which may be least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar when compared to the full length polypeptide sequence of the parent enzyme.
  • Amylases according to the invention have“amylolytic activity” or“amylase activity” according to the invention involves (endo)hydrolysis of glucosidic linkages in polysaccharides
  • a-amylase activity may be determined by assays for measurement of a-amylase activity which are known to those skilled in the art. Examples for assays measuring a-amylase activity are: a-amylase activity can be determined by a method employing Phadebas tablets as substrate (Phadebas Amylase Test, supplied by Magle Life Science). Starch is hydrolyzed by the a- amylase giving soluble blue fragments.
  • the absorbance of the resulting blue solution, measured spectrophotometrically at 620 nm, is a function of the a-amylase activity.
  • the measured absorbance is directly proportional to the specific activity (activity/mg of pure a-amylase protein) of the a-amylase in question under the given set of conditions.
  • a-amylase activity can also be determined by a method employing the Ethyliden-4-nitrophenyl- a-D-maltoheptaosid (EPS).
  • EPS Ethyliden-4-nitrophenyl- a-D-maltoheptaosid
  • D-maltoheptaoside is a blocked oligosaccharide which can be cleaved by an endo-amylase.
  • kits containing EPS substrate and a- glucosidase is manufactured by Roche Costum Biotech (cat. No. 10880078103).
  • the slope of the time dependent absorption-curve is directly proportional to the specific activity (activity per mg enzyme) of the a-amylase in question under the given set of conditions.
  • Amylase variants have amylolytic activity according to the present invention when said amylase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the amylolytic activity of the respective parent amylase.
  • the water-soluble multilayer film of the invention comprises at least one perhydrolase.
  • Suitable“perhydrolases” are capable of catalyzing a perhydrolysis reaction that results in the production of a peracid from a carboxylic acid ester (acyl) substrate in the pres ence of a source of peroxygen (e.g., hydrogen peroxide). While many enzymes perform this reaction at low levels, perhydrolases exhibit a high perhydrolysis:hydrolysis ratio, often greater than 1.
  • Suitable perhydrolases may be of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
  • useful perhydrolases include naturally occurring Mycobacterium perhydrolase enzymes, or variants thereof.
  • An exemplary enzyme is derived from Mycobacterium smegmatis. Such enzyme, its enzymatic properties, its structure, and variants thereof, are described in WO 2005/056782, WO 2008/063400, US 2008145353, and US 2007167344.
  • the water-soluble multilayer film of the invention comprises at least one mannanase.
  • “Mannanase” may be an alkaline mannanase of Family 5 or 26. It may be a wild- type from Bacillus or Humicoia, particularly B. agaradhaerens, B. Hcheniformis, B. haiodurans,
  • Mannaway® Novozymes AIS
  • the water-soluble multilayer film of the invention comprises at least one peroxidase and/or oxidase.
  • Suitable peroxidases and oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
  • An oxidase according to the invention include, in particular, any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1 .10.3.1 ), an o-aminophenol oxidase (EC 1 .10.3.4), or a bilirubin oxidase (EC 1.3.3.5).
  • a catechol oxidase EC 1 .10.3.1
  • an o-aminophenol oxidase EC 1 .10.3.4
  • 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. crassa, Podospora, Botrytis, Collybia, Fames , Lentinus, P/eurotus, Tra metes, e.g. T. villosa and T. versicolor, Rhi- zoctonia, e.g. R. so!ani, Coprinopsis, e.g. C. cinerea, C. comatus, C. friesii, and C.
  • a laccase may be derived from Coprinopsis or Myceliophthora.
  • a laccase is derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora ther- mophiia, as disclosed in WO 95/33836.
  • the laccase may be a bacterial laccase, e.g. the laccase may be a Gram positive bacterial pol ypeptide such as a Bacillus, Streptococcus, Streptomyces, Staphylococcus, Enterococcus, Lactobacillus, Lactococcus, Clostridium, Geobacillus, or OceanobaciHus laccase, or a Gram negative bacterial polypeptide such as an E. coH, Pseudomonas, Salmonella, Campylobacter, Heli cobacter, Fiavobacterium, Fusobacterium, Hyobacter, Neisseria, or Ureap!asma laccase.
  • a Gram positive bacterial pol ypeptide such as a Bacillus, Streptococcus, Streptomyces, Staphylococcus, Enterococcus, Lactobacillus, Lactococcus, Clostridium, Geobacillus, or OceanobaciHus laccase
  • laccase is selected from those as described in SEQ ID NO: 2, 4, 6, and 8 of WO 2009/127702 and variants thereof.
  • laccase activity is defined herein as covered by enzyme classification EC 1 .10.3.2, or a similar activity, such as a catechol oxidase activity (EC 1.10.3.1), o-aminophenol oxidase activity (EC 1.10.3.4), or bilirubin oxidase activity (EC 1.3.3.5), that catalyzes the oxidation of a substrate using molecular oxygen.
  • enzyme classification EC 1 .10.3.2 or a similar activity, such as a catechol oxidase activity (EC 1.10.3.1), o-aminophenol oxidase activity (EC 1.10.3.4), or bilirubin oxidase activity (EC 1.3.3.5), that catalyzes the oxidation of a substrate using molecular oxygen.
  • “Laccase activity” is determined by oxidation of syringaldazin under aerobic conditions. The violet colour produced is measured at 530 nm. The analytical conditions are 19 mM syringaldazin, 23 mM Tris/maleate buffer, pH 7.5, 30°C, and 1 min reaction time.
  • Oxidases and their corresponding substrates may be used as hydrogen peroxide generating enzyme systems, and thus a source of hydrogen peroxide.
  • enzymes such as pe- roxidases, haloperoxidases and perhydrolases, require a source of hydrogen peroxide.
  • Peroxidases utilize hydrogen peroxide as substrate.
  • useful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, WO 98/10060 and WO 98/15257.
  • peroxidases include GuardzymeTM (Novozymes A/S), PrimaGreenTM
  • Peroxidase activity may be measured by the ABTS method as described in Childs et al. 1975 (Biochemical J, 145, p. 93-103) and commercial kits are available from different suppliers. Other measuring methods are known to those known in the art.
  • a peroxidase for use in the invention also include a haloperoxidase enzyme, such as chlo- roperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxi- dase activity.
  • haloperoxidases are classified according to their specificity for halide ions. Chlo- roperoxidases (E.C. 1.1 1.1.10) catalyze formation of hypochlorite from chloride ions.
  • the haloperoxidase is a chloroperoxidase. In one embodiment, the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase. In one embodiment of the present invention the vanadate-containing haloperoxidase is combined with a source of chloride ion.
  • Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caidariomyces, e.g., C. fumago, Aiternaria, Cur- vularia, e.g., C. verrucuiosa and C. inaequa/is, Drechslera, Ulocladium and Botrytis.
  • Haloperox idases have also been isolated from bacteria such as Pseudomonas , e.g. P. pyrrocinia, and Streptomyces, e.g. S. aureofaciens.
  • the haloperoxidase is from Curvularia sp., in particular Curvularia verrucu- losa or Curvularia inaequaiis, such as C. inaequa/is CBS 102.42 as described in WO 95/27046; or C. verrucuiosa CBS 147.63 or C.
  • the water-soluble multilayer film of the invention comprises at least one lyase.“Lyase” may be a pectate lyase derived from Bacillus, particularly B. iicheniformis or B. agaradhaerens, or a variant derived of any of these, e.g. as described in US 6,124,127, WO 99/027083, WO 99/027084, WO 2002/006442, WO 2002/092741 , WO 2003/095638.
  • lyase may be a pectate lyase derived from Bacillus, particularly B. iicheniformis or B. agaradhaerens, or a variant derived of any of these, e.g. as described in US 6,124,127, WO 99/027083, WO 99/027084, WO 2002/006442, WO 2002/092741 , WO 2003/095638.
  • pectate lyases are XpectTM, PectawashTM and PectawayTM (Novozymes A/S); PrimaGreenTM, EcoScour (DuPont).
  • the water-soluble multilayer film of the invention comprises at least one enzyme selected from the group of pectinases, and/or arabinases, and/or galactanases, and/or xylanases.
  • Suitable pectinases, and/or arabinases, and/or galactanases, and/or xylanases are known to those skilled in the art.
  • Nuclease (EC 3.1.21.1 ) also known as Deoxyribonuclease I, or DNase preforms endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.
  • Nuclease enzymes have been described in patents and published patent applications including, but not limited to: US3451935, GB1300596, DE10304331 , WO2015155350, WO2015155351 , WO2015166075, WO2015181287, and WO2015181286.
  • Oxo alcohol and water were initially charged and the initial charge was heated to 75 ° C with stirring at 100 rpm.
  • the feeds 1 , 2 and 3 were then added in 4 hours and the reaction mixture was polymerized for an additional hour. Then the mixture was allowed to cool to room temperature.
  • the polymer composition was obtained in the form of a transparent and viscous solution. 100 g of the polymer composition was heated to 80°C. After adding 4.2 g of glycerol, the concentration of the polymer composition was diluted to 65% wt% with deionized water. The appli- cation solution was well mixed and tempered at 80°C until the stirred-in air had completely escaped.
  • Time 0 of the shelf life aging tests is the instant when the enzyme containing polymer solution is prepared.
  • Film sample preparation coating and dry ing at room temperature and humidity typically takes 1 -2 days with subsequent enzyme activity determination by protease or lipase assay.
  • protease acitivty was determined using Succinyl - Ala - Ala - Pro - Phe - p-Nitroanilide (Suc-AAPF-pNA, short : AAPF) as substrate.
  • pNA is cleaved from the substrate molecule at 30°C, pH 8.6 TRIS buffer.
  • the rate of cleavage can be determined by the increase of the yellow color of free pNA in the solution by measuring OD405, the optical density at 405 nm.
  • Lipase activity is determined by a method employing para Nitrophenol-valerate (pNP-C5). Fol- lowing cleavage, a free pNP molecule is liberated with an absorption increase that can be moni tored at a wavelength of 405 nm.
  • the sample to be analyzed is diluted in residual activity buffer (100 mM Tris pH 8.0, 2% w/w Arabic gum, 0.01 % Triton X100). The dilution is as such that the final dilution is in the linear range of the assay.
  • the slope (absorbance increase at 405 nm per minute) of the time dependent absorption-curve is directly proportional to the activity of the lipase.
  • the enzyme activity in films has been determined by adding a solid piece of film into a microtiter plate. Activity evolution in aging tests at 37°C is measured during film dissolution over a period of time (typically 15min) until the activity value has reached a constant value. Activies might spread (100% plus, minus 10%) due to residual moisture in the films which impact the activity values of sample amounts determined gravimetrically .
  • Example 1 Preparation of protease and amylase containing films based on the color transfer inhibitor polymer Sokalan HP56 (BASF SE) (application solution B):
  • an automatic film applicator and a universal applicator from Zehntner were used.
  • the application solution B was applied to a PET substrate (Hostaphan ® , Mitsubishi Polyester Film).
  • the gap width of the doctor blade was chosen so that the layer after drying at room temperature has a thickness of 30 pm.
  • Table 2 Change of normalized protease and amylase activity over time in single layer film based on color transfer inhibitor polymer stored at 37°C conditions:
  • Example 2 Preparation of protease and lipase containing single layer films based on PVOH and glycerol (application solution A4):
  • an automatic film applicator and a universal applicator from Zehntner were used.
  • the application solution A4 was applied to a PET substrate (Hostaphan ® , Mitsubishi Polyester Film).
  • the gap width of the doctor blade was chosen so that the layer after drying at room temperature has a thickness of 30 pm.
  • Example 3 Preparation of 2-layer films containing a lipase top-layer on a layer comprising both protease and amylase based on PVOH, propane-1 ,2-diol and glycerol (application solution A1 & A2):
  • an automatic film applicator and a universal applicator from Zehntner were used.
  • the application solution A2 was applied to a PET substrate (Hostaphan ® , Mitsubishi Polyester Film).
  • the gap width of the doctor blade was chosen so that the layer after drying at room temperature has a thickness of 30 pm.
  • the application solution A1 was applied.
  • the gap width of the doctor blade was adjusted so that after drying at room temperature, the total layer thickness of the film is 40 pm.
  • Example 4 Preparation of 3-layer films containing wash active polymer composition as adhesion layer in-between lipase top-layer and the combination of protease and amylase as bottom- layer based on PVOH, propane-1 ,2-diol and glycerol (application solution A1 & A3):
  • an automatic film applicator and a universal applicator from Zehntner were used.
  • the application solution A2 was applied to a first PET substrate (Hostaph an ® , Mitsubishi Polyester Film).
  • the gap width of the doctor blade was chosen so that the layer 1 after drying at room temperature has a thickness of 30 pm.
  • the application solution C of the wash active polymer composition heated to 80°C was applied.
  • the gap width of the doctor blade was adjusted so that after drying at room temperature, the total layer thick ness of the first film comprising layer 1 and 2 is 110 pm.
  • the application solution A1 was applied on a second PET substrate (Hostaphan ® , Mitsubishi Polyester Film).
  • Table 4 Change of normalized protease and amylase activity over time in layer 1 stored at 37°C conditions:
  • Table 5 Change of normalized lipase activity over time in layer 3 stored at 37°C conditions:
  • wash performance tests have been conducted.
  • the films were stored for 8 weeks at 37 °C in a heating cabinet.
  • the wash performance of the films was determined directly and after 2, 6 and 8 weeks.
  • the different enzymes had to be tested on varying stains.
  • test fabric was washed at 25°C in the presence of cotton ballast fabric with addition of the film. After the wash cycle, the test fabric was rinsed, spun and dried. In order to determine the washing effect, the L * , a * and b * values of the test fabric were determined by photometry before and after the wash cycle. The values for the protease and amylase relevant stains were determined with a Datacolor (Elrepho 2000) photometer. The values for the lipase relevant stains were determind by MACH 5. The Delta E values were calculated from the L * , a * and b * values before and after wash.
  • Protease and amylase embedded in the film are stable over 8 weeks stored at 37 °C
  • Table C Wash result for wash active polymer composition layer 2 and layer 3 containing li pase, stored at 37°C and washed in formulation 2 at 25 °C on a multi stain set (sum of delta E values)
  • the examples show that in case of the combination of protease and lipase, it is not possible to embed both incompatible enzymes (example 2) in different layers of a 2-layer film, since during film manufacturing of subsequent coating and drying the bottom enzyme migrates into the top layer (example 3).
  • both enzyme containing layers are laminated with each other.
  • the properties of the wash active polymer composition layer matches exactly with requirements for an adhesive layer and makes a lamination process feasible. By this process, including the wash active polymer composition layer as an adhesive interlayer in-between both enzyme layers mi- gration processes are prevented and enzyme activity of the individual layers is preserved (ex ample 4).
  • wash performance tests show that the demonstrated wash active multilayer films not only exhibit enzyme activity but also provide additional wash performance if such films are used in addition to typical liquid detergent pouch formulation (example 4).
  • the wash tests show the enzymes embedded in the film exhibit a very high storage stability.
  • a water-soluble multilayer film comprising at least one layer comprising or consisting of a polymer composition P1 ) obtainable by physical blending of a at least one polymer PT) and at least one polyether component PE), or free-radical polymerization of a monomer composition M1 ) comprising at least one monomer A) selected from a,b-ethylenically un saturated mono- and dicarboxylic acids, salts of a,b-ethylenically unsaturated mono- and dicarboxylic acids, anhydrides of a,b-ethylenically unsaturated mono- and dicarboxylic ac ids and mixtures thereof, in the presence of at least one polyether component PE), select ed from polyether alcohols with a number average molecular weight Mn of at least 200 g/mol, mono and di-(Ci to C 6 -alkyl)ethers of such polyether alcohols, polyether groups- containing surfactants or mixtures thereof, and/or
  • a water-soluble multilayer film according to item 1 wherein the film comprises at least one layer comprising or consisting of at least one washing- and/or cleaning active polymer or polymer blend, wherein (i) the washing- and/or cleaning active polymer or polymer blend is selected from P1 ), and/or (ii) the washing- and/or cleaning active polymer or polymer blend is selected from P2).
  • the enzyme EN is selected from the group consisting of proteases, amylases, lipases, cellulases, perhydrolases, mannanases, nucleases, peroxidases, oxidases, lyases, pectinases, arabinases, galactanases, xylanases, and mixtures thereof.
  • a water-soluble multilayer film according to any one of items 1 to 8, wherein at least one layer contains protease as enzyme EN1 ), and at least one other layer contains at least one enzyme EN2) different from protease, preferably at least one enzyme EN2) that is incompatible with protease, more preferably lipase as enzyme EN2), and wherein, preferably, these two layers containing EN1) and EN2) are spatially separated by at least one further layer neither comprising EN1) nor EN2).
  • Water soluble multilayer film according to any one of items 1 to 10, derived from a wash active layer based on a at least one polymer chosen from P2, preferred a polymer blend, more preferred chosen from polymer composition P 1 , which is used as adhesion layer in- between two enzyme containing layers, optionally in a lamination process.
  • homo- and copolymers comprising repeat units which derive from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof,
  • homo- and copolymers comprising at least one copolymerized monomer selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole,
  • homo- and copolymers of acrylic acid and/or methacrylic acid especially copolymers comprising at least one copolymerized acrylic monomer selected from acrylic acid, acrylic salts and mixtures thereof, and at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof,
  • copolymers comprising at least one copolymerized (meth)acrylic monomer selected from acrylic acid, methacrylic acid, salts thereof and mixtures thereof and at least one copolymerized hydrophobic monomer selected from Ci-Cs-alkyl esters of (meth)acrylic acid, C2-C10 olefins, styrene and a-methylstyrene,
  • copolymers comprising at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof and at least one copolymerized C 2 -C 8 olefin,
  • polyalkylene glycols mono- or diethers of polyalkylene glycols
  • multifunctional alkoxylated diamines preferably alkoxylated diamines with 2 to 10 methylene groups
  • cellulose derivatives preferably cellulose ethers, cellulose esters, carboxyalkyl cellu- loses and salts thereof, sulfoalkyl celluloses and salts thereof, acidic sulfuric ester salts of cellulose, alkyl celluloses, hydroxyalkyl celluloses, hydroxyalkyl alkyl celluloses and mixtures of two or more of these cellulose derivatives
  • amphoteric modified starch and
  • a first free-flowing composition capable of film formation is applied to a carrier material to obtain a first layer
  • the first layer applied to the carrier material is optionally subjected to an increase in viscosity
  • a second free-flowing composition capable of film formation is applied to the first layer obtained in step i1 ) or in step i2) to obtain a second layer
  • the second layer is optionally subjected to an increase in viscosity
  • step i3) is optionally repeated with a further composition capable of film formation to obtain a further layer and step i4) is optionally then repeated, it being possible to re peat steps i3) and i4) once or more than once,
  • the layers applied to the carrier material are optionally subjected to a further in crease in viscosity
  • the multilayer film obtained is optionally detached from the carrier material, with the proviso that the free-flowing compositions each comprise a component which is ca pable of film formation and is independently selected from at least one polymer composition P1 ), at least one polymer P2) or a mixture thereof, and with the proviso that at least one of the free-flowing compositions and/or the carrier material comprises or consists of a polymer composition P 1 ) as defined in any of the preceding claims,
  • Washing composition comprising a multilayer film according to any of items 1 to 13 or obtainable by a process as defined in item 14.

Abstract

La présente invention concerne des films multicouches hydrosolubles contenant des produits chimiques et des enzymes actifs de lavage, leur production et leur utilisation.
PCT/EP2019/065359 2018-06-15 2019-06-12 Films multicouches hydrosolubles contenant des produits chimiques et des enzymes actifs de lavage WO2019238761A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP18178107 2018-06-15
EP18178107.1 2018-06-15

Publications (1)

Publication Number Publication Date
WO2019238761A1 true WO2019238761A1 (fr) 2019-12-19

Family

ID=62705430

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/EP2019/065359 WO2019238761A1 (fr) 2018-06-15 2019-06-12 Films multicouches hydrosolubles contenant des produits chimiques et des enzymes actifs de lavage

Country Status (1)

Country Link
WO (1) WO2019238761A1 (fr)

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN114931934A (zh) * 2022-05-25 2022-08-23 安徽皖仪科技股份有限公司 一种接枝型阳离子交换色谱柱填料及其制备方法
WO2023225459A2 (fr) 2022-05-14 2023-11-23 Novozymes A/S Compositions et procédés de prévention, de traitement, de suppression et/ou d'élimination d'infestations et d'infections phytopathogènes
CN114931934B (zh) * 2022-05-25 2024-04-23 安徽皖仪科技股份有限公司 一种接枝型阳离子交换色谱柱填料及其制备方法

Citations (133)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3451935A (en) 1966-04-25 1969-06-24 Procter & Gamble Granular enzyme-containing laundry composition
GB1243784A (en) 1967-10-03 1971-08-25 Novo Terapeutisk Labor As Proteolytic enzymes, their production and use
GB1300596A (en) 1969-11-19 1972-12-20 Knapsack Ag Process for the manufacture of enzyme-containing granules
US4115292A (en) * 1977-04-20 1978-09-19 The Procter & Gamble Company Enzyme-containing detergent articles
EP0218272A1 (fr) 1985-08-09 1987-04-15 Gist-Brocades N.V. Enzymes lipolytiques et leur usage dans des compositions détergentes
EP0258068A2 (fr) 1986-08-29 1988-03-02 Novo Nordisk A/S Additif enzymatique pour détergent
EP0260105A2 (fr) 1986-09-09 1988-03-16 Genencor, Inc. Préparation d'enzymes à activité modifiée
DE3700128A1 (de) 1987-01-03 1988-07-14 Hoechst Ag Biologisch abbaubare poly- (hydroxyalkyl)- aminodicarbonsaeure-derivate, verfahren zu ihrer herstellung und verwendung derselben fuer depotzubereitungen mit kontrollierter wirkstoffabgabe
EP0283075A2 (fr) 1987-02-27 1988-09-21 Gist-Brocades N.V. Clonage moléculaire et expression de gènes codant pour des enzymes protéolytiques
WO1988009367A1 (fr) 1987-05-29 1988-12-01 Genencor, Inc. Compositions de nettoyage a base de cutinase
EP0305216A1 (fr) 1987-08-28 1989-03-01 Novo Nordisk A/S Lipase recombinante de humicola et procédé de production de lipases recombinantes de humicola
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
WO1989006279A1 (fr) 1988-01-07 1989-07-13 Novo-Nordisk A/S Genes de subtilisine mutes
WO1989006276A2 (fr) 1988-01-08 1989-07-13 Dpz Deutsches Primatenzentrum Gesellschaft Mbh Retrovirus de primates du type hiv-2, vaccins, compositions diagnostiques et pharmaceutiques
EP0331376A2 (fr) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. ADN recombinant, bactérie du genre pseudomonas le contenant et son utilisation dans un procédé de production de lipase
WO1989009830A1 (fr) 1988-04-12 1989-10-19 Genex Corporation Mutations de subtilisine
WO1989009819A1 (fr) 1988-04-12 1989-10-19 Genex Corporation Mutations combinantes de stabilisation de subtilisine
WO1990009446A1 (fr) 1989-02-17 1990-08-23 Plant Genetic Systems N.V. Cutinase
JPH02238885A (ja) 1989-03-13 1990-09-21 Oji Paper Co Ltd フェノールオキシダーゼ遺伝子組換えｄｎａ、該組換えｄｎａにより形質転換された微生物、その培養物及びフェノールオキシダーゼの製造方法
EP0407225A1 (fr) 1989-07-07 1991-01-09 Unilever Plc Enzymes et compositions détergentes enzymatiques
WO1991002792A1 (fr) 1989-08-25 1991-03-07 Henkel Research Corporation Enzyme proteolytique alcaline et procede de production
WO1991006637A1 (fr) 1989-10-31 1991-05-16 Genencor International, Inc. Mutants de subtilisine
WO1991016422A1 (fr) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Lipases bacillaires alcalines, sequences d'adn de codage pour celles-ci et bacilles produisant ces lipases
EP0458079A2 (fr) 1990-04-26 1991-11-27 Hoechst Aktiengesellschaft Agent de contraste ultrasonique, sa préparation et application comme diagnostic ou thérapeutique
WO1992001046A1 (fr) 1990-07-06 1992-01-23 Valtion Teknillinen Tutkimuskeskus Production de laccase au moyen d'organismes recombines
WO1992005249A1 (fr) 1990-09-13 1992-04-02 Novo Nordisk A/S Variantes lipasiques
WO1992019729A1 (fr) 1991-05-01 1992-11-12 Novo Nordisk A/S Enzymes stabilisees et compositions detergentes
WO1993024618A1 (fr) 1992-06-01 1993-12-09 Novo Nordisk A/S Variante de peroxydase avec stabilite amelioree vis-a-vis du peroxyde d'hydrogene
WO1994001541A1 (fr) 1992-07-06 1994-01-20 Novo Nordisk A/S Lipase de c. antarctica et variantes lipasiques
WO1994002597A1 (fr) 1992-07-23 1994-02-03 Novo Nordisk A/S Alpha-amylase mutante, detergent, agent de lavage de vaisselle et de liquefaction
WO1994018314A1 (fr) 1993-02-11 1994-08-18 Genencor International, Inc. Alpha-amylase stable a l'oxydation
WO1994025578A1 (fr) 1993-04-27 1994-11-10 Gist-Brocades N.V. Nouveaux variants de lipase utilises dans des detergents
US5389536A (en) 1986-11-19 1995-02-14 Genencor, Inc. Lipase from Pseudomonas mendocina having cutinase activity
WO1995006720A1 (fr) 1993-08-30 1995-03-09 Showa Denko K.K. Nouvelle lipase, micro-organisme la produisant, procede de production de cette lipase, et utilisation de ladite lipase
WO1995010602A1 (fr) 1993-10-13 1995-04-20 Novo Nordisk A/S Variants de peroxydase stables par rapport a h2o¿2?
WO1995010603A1 (fr) 1993-10-08 1995-04-20 Novo Nordisk A/S Variants d'amylase
WO1995014783A1 (fr) 1993-11-24 1995-06-01 Showa Denko K.K. Gene de lipase et lipase variante
WO1995022615A1 (fr) 1994-02-22 1995-08-24 Novo Nordisk A/S Procede pour preparer un variant d'une enzyme lipolytique
WO1995023221A1 (fr) 1994-02-24 1995-08-31 Cognis, Inc. Enzymes ameliorees et detergents les contenant
WO1995027046A2 (fr) 1994-03-31 1995-10-12 Unilever Nv Compositions antimicrobiennes enzymatiques comprenant des haloperoxydases
WO1995030744A2 (fr) 1994-05-04 1995-11-16 Genencor International Inc. Lipases a resistance aux tensioactifs amelioree
WO1995033836A1 (fr) 1994-06-03 1995-12-14 Novo Nordisk Biotech, Inc. Phosphonyldipeptides efficaces dans le traitement de maladies cardiovasculaires
WO1995035381A1 (fr) 1994-06-20 1995-12-28 Unilever N.V. Lipases modifiees provenant de pseudomonas et leur utilisation
WO1996000292A1 (fr) 1994-06-23 1996-01-04 Unilever N.V. Pseudomonas lipases modifiees et leur utilisation
WO1996012012A1 (fr) 1994-10-14 1996-04-25 Solvay S.A. Lipase, micro-organisme la produisant, procede de preparation de cette lipase et utilisation de celle-ci
WO1996013580A1 (fr) 1994-10-26 1996-05-09 Novo Nordisk A/S Enzyme a activite lipolytique
WO1996023872A1 (fr) 1995-02-02 1996-08-08 Stichting Centraal Laboratorium Van De Bloedtransfusiedienst Van Het Nederlandse Rode Kruis Enrichissement de cellules souches hematopoietiques provenant du sang ou de la moelle osseuse
WO1996027002A1 (fr) 1995-02-27 1996-09-06 Novo Nordisk A/S Nouveau gene de lipase et procede de production de lipase a l'aide de celui-ci
WO1996034946A1 (fr) 1995-05-05 1996-11-07 Novo Nordisk A/S Variantes du type protease et compositions
WO1997004079A1 (fr) 1995-07-14 1997-02-06 Novo Nordisk A/S Enzyme modifiee a activite lipolytique
WO1997004102A1 (fr) 1995-07-14 1997-02-06 Novo Nordisk A/S Haloperoxydases provenant de curvularia verruculosa et acides nucleiques les codant
WO1997007202A1 (fr) 1995-08-11 1997-02-27 Novo Nordisk A/S Nouvelles enzymes lipolytiques
WO1997008325A2 (fr) 1995-08-25 1997-03-06 Novo Nordisk Biotech, Inc. Laccases de coprin purifiees et acides nucleiques les codant
DE19545678A1 (de) 1995-12-07 1997-06-12 Goldschmidt Ag Th Copolymere Polyaminosäureester
WO1997043424A1 (fr) 1996-05-14 1997-11-20 Genencor International, Inc. α-AMYLASES MODIFIEES POSSEDANT DES PROPRIETES MODIFIEES DE FIXATION DU CALCIUM
WO1998010060A1 (fr) 1996-09-03 1998-03-12 Novo Nordisk A/S Variantes de peroxydase
WO1998015257A1 (fr) 1996-10-08 1998-04-16 Novo Nordisk A/S Derives de l'acide diaminobenzoique en tant que precurseurs de matieres tinctoriales
WO1998020116A1 (fr) 1996-11-04 1998-05-14 Novo Nordisk A/S Variants de subtilase et compositions
WO1998020115A1 (fr) 1996-11-04 1998-05-14 Novo Nordisk A/S Variants et compositions de subtilase
WO1999011768A1 (fr) 1997-08-29 1999-03-11 Novo Nordisk A/S Variants de la protease et compositions
WO1999019467A1 (fr) 1997-10-13 1999-04-22 Novo Nordisk A/S MUTANTS D'α-AMYLASE
WO1999027083A1 (fr) 1997-11-24 1999-06-03 Novo Nordisk A/S ENZYMES DE DEGRADATION DE LA PECTINE PROVENANT DU $i(BACILLUS LICHENIFORMIS)
WO1999027084A1 (fr) 1997-11-24 1999-06-03 Novo Nordisk A/S Nouvelles lyases de pectate
WO1999064619A2 (fr) 1998-06-10 1999-12-16 Novozymes A/S Nouvelles mannanases
WO2000022103A1 (fr) 1998-10-13 2000-04-20 Novozymes A/S Polypeptide modifie a reponse immunitaire reduite
WO2000034450A1 (fr) 1998-12-04 2000-06-15 Novozymes A/S Variantes de cutinase
US6124127A (en) 1997-11-24 2000-09-26 Novo Nordisk A/S Pectate lyase
WO2000060060A2 (fr) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides presentant une activite alcaline alpha-amylase et acides nucleiques les codant
WO2000060063A1 (fr) 1999-03-31 2000-10-12 Novozymes A/S Variante genetique de lipase
WO2001044452A1 (fr) 1999-12-15 2001-06-21 Novozymes A/S Variants de subtilase a performance de nettoyage amelioree sur des taches d'oeuf
WO2001079458A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides ayant une activite d'haloperoxidase
WO2001079461A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides a activite haloperoxydase
WO2001079460A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides a activite haloperoxydase
WO2001079459A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides ayant une activite d'haloperoxydase et acides nucleiques qui les codent
WO2001092502A1 (fr) 2000-06-02 2001-12-06 Novozymes A/S Variants de cutinase
WO2002006442A2 (fr) 2000-07-19 2002-01-24 Novozymes A/S Variants d'enzymes degradant la paroi cellulaire
WO2002010355A2 (fr) 2000-08-01 2002-02-07 Novozymes A/S Mutants d'alpha-amylase a proprietes modifiees
DE10064983A1 (de) 2000-12-23 2002-07-18 Henkel Kgaa Neue Alkalische Protease aus Bacillus alcalophilus (DSM 11233)
WO2002088340A2 (fr) 2001-05-02 2002-11-07 Henkel Kommanditgesellschaft Auf Aktien Nouvelles variantes de proteases alcalines et detergents contenant ces nouvelles variantes
WO2002092741A2 (fr) 2001-05-14 2002-11-21 Novozymes A/S Compositions detergentes comprenant des lyases de pectates de bacillus subtilis
WO2003006602A2 (fr) 2001-07-12 2003-01-23 Novozymes A/S Variants de subtilase
WO2003054184A1 (fr) 2001-12-20 2003-07-03 Henkel Kommanditgesellschaft Auf Aktien Nouvelle protease alcaline extraite de bacillus gibsonii (dsm 14393) et agents de lavage et de nettoyage contenant cette nouvelle protease alcaline
WO2003055974A2 (fr) 2001-12-22 2003-07-10 Henkel Kommanditgesellschaft Auf Aktien Nouvelle protease alcaline obtenue a partir de bacillus sp. (dsm 14392) et agents de lavage et de nettoyage contenant cette protease alcaline
WO2003056017A2 (fr) 2001-12-22 2003-07-10 Henkel Kommanditgesellschaft Auf Aktien Nouvelle protease alcaline obtenue a partir de bacillus sp (dsm 14390) et agents de lavage et de nettoyage contenant cette protease alcaline
WO2003095638A1 (fr) 2002-05-14 2003-11-20 Novozymes A/S Variants de pectate lyase
WO2004003186A2 (fr) 2002-06-26 2004-01-08 Novozymes A/S Subtilases et variants de la subtilase presentant une immunogenicite modifiee
WO2004041979A2 (fr) 2002-11-06 2004-05-21 Novozymes A/S Variantes de subtilase
DE10304331A1 (de) 2003-02-04 2004-08-12 Henkel Kgaa Enzymatische Entfernung von Biofilmen auf Haushaltsoberflächen
WO2005056782A2 (fr) 2003-12-03 2005-06-23 Genencor International, Inc. Perhydrolase
WO2005063974A1 (fr) 2003-12-23 2005-07-14 Henkel Kommanditgesellschaft Auf Aktien Nouvelle protease alcaline et produits detergents et nettoyants contenant cette nouvelle protease alcaline
WO2005103244A1 (fr) 2004-04-23 2005-11-03 Henkel Kommanditgesellschaft Auf Aktien Nouvelles proteases alcalines et agents de lavage et detergents renfermant celles-ci
WO2006002643A2 (fr) 2004-07-05 2006-01-12 Novozymes A/S Variants d'alpha-amylases presentant des proprietes modifiees
WO2006066594A2 (fr) 2004-12-23 2006-06-29 Novozymes A/S Variantes de l'alpha-amylase
DE102005028295A1 (de) 2005-06-18 2006-11-16 Henkel Kgaa Proteasen aus psychrophilen Organismen
WO2007006305A1 (fr) 2005-07-08 2007-01-18 Novozymes A/S Variants de subtilase
US20070167344A1 (en) 2003-12-03 2007-07-19 Amin Neelam S Enzyme for the production of long chain peracid
WO2007087508A2 (fr) 2006-01-23 2007-08-02 Novozymes A/S Variantes de lipase
WO2008051491A2 (fr) 2006-10-20 2008-05-02 Danisco Us, Inc. Genencor Division Polyol oxydases
WO2009061380A2 (fr) 2007-11-05 2009-05-14 Danisco Us Inc., Genencor Division Variants de bacillus sp. ts-23 alpha-amylase à propriétés modifiées
WO2009067279A1 (fr) 2007-11-21 2009-05-28 E.I. Du Pont De Nemours And Company Production de peracides employant une enzyme ayant une activité de perhydrolyse
WO2009109500A1 (fr) 2008-02-29 2009-09-11 Novozymes A/S Polypeptides à activité lipase et polynucléotides codant ces polypeptides
WO2009127702A2 (fr) 2008-04-17 2009-10-22 Novozymes A/S Variants de laccase
WO2010065455A2 (fr) 2008-12-01 2010-06-10 Danisco Us Inc. Enzymes ayant une activité lipase
WO2010100028A2 (fr) 2009-03-06 2010-09-10 Huntsman Advanced Materials (Switzerland) Gmbh Procédés enzymatiques de blanchissement-azurage des textiles
WO2010104675A1 (fr) 2009-03-10 2010-09-16 Danisco Us Inc. Alpha-amylases associées à la souche bacillus megaterium dsm90, et leurs procédés d'utilisation
WO2010107560A2 (fr) 2009-03-18 2010-09-23 Danisco Us Inc. Cutinase fongique de magnaporthe grisea
WO2010111143A2 (fr) 2009-03-23 2010-09-30 Danisco Us Inc. Acyltransférases associées à cal a et leurs procédés d'utilisation
WO2011036263A1 (fr) 2009-09-25 2011-03-31 Novozymes A/S Variants de subtilase
WO2011036264A1 (fr) 2009-09-25 2011-03-31 Novozymes A/S Utilisation de variants de protéase
WO2011072099A2 (fr) 2009-12-09 2011-06-16 Danisco Us Inc. Compositions et procédés comprenant des variants de protéase
WO2011084599A1 (fr) 2009-12-21 2011-07-14 Danisco Us Inc. Compositions détergentes contenant une lipase de bacillus subtilis et procédés d'utilisation associés
WO2011084417A1 (fr) 2009-12-21 2011-07-14 Danisco Us Inc. Compositions détergentes contenant une lipase issue de geobacillus stearothermophilus et leurs procédés d'utilisation
WO2011084412A1 (fr) 2009-12-21 2011-07-14 Danisco Us Inc. Compositions détergentes contenant une lipase issue de thermobifida fusca et leurs procédés d'utilisation
WO2011098531A1 (fr) 2010-02-10 2011-08-18 Novozymes A/S Variants et compositions contenant des variants à stabilité élevée en présence d'un agent chélateur
WO2011150157A2 (fr) 2010-05-28 2011-12-01 Danisco Us Inc. Compositions de détergent contenant une lipase de streptomyces griseus et leurs procédés d'utilisation
WO2012137147A1 (fr) 2011-04-08 2012-10-11 Danisco Us, Inc. Compositions
WO2013001087A2 (fr) 2011-06-30 2013-01-03 Novozymes A/S Procédé de criblage d'alpha-amylases
WO2013001078A1 (fr) 2011-06-30 2013-01-03 Novozymes A/S Variants d'alpha-amylase
US20130244920A1 (en) * 2012-03-16 2013-09-19 David M. Lee Water soluble compositions incorporating enzymes, and method of making same
WO2013148492A1 (fr) 2012-03-29 2013-10-03 Novozymes A/S Utilisation d'enzymes pour préparer des films hydrosolubles
WO2013184577A1 (fr) 2012-06-08 2013-12-12 Danisco Us Inc. Variants d'alpha-amylase dérivés de l'alpha-amylase de cytophaga sp. amylase/ (cspamy2)
WO2014152674A1 (fr) 2013-03-14 2014-09-25 Novozymes A/S Films solubles dans l'eau contenant des enzymes et des inhibiteurs
WO2014152547A2 (fr) 2013-03-14 2014-09-25 Novozymes A/S Poche de détergent comportant un film enzymatique soluble dans l'eau
EP2799533A1 (fr) 2013-04-30 2014-11-05 Novozymes A/S Inhibiteur et protease contenant des films solubles dans l'eau
WO2014186464A1 (fr) 2013-05-14 2014-11-20 Novozymes A/S Varaints de lipase humicola lanuginosa stabilisée dans des films hydrosolubles
WO2015155351A1 (fr) 2014-04-11 2015-10-15 Novozymes A/S Composition de détergent
WO2015155350A1 (fr) 2014-04-11 2015-10-15 Novozymes A/S Composition de détergent
WO2015166075A1 (fr) 2014-05-02 2015-11-05 Novozymes A/S Composition de détergent
WO2015181286A1 (fr) 2014-05-28 2015-12-03 Novozymes A/S Utilisation d'un polypeptide
WO2015181287A1 (fr) 2014-05-28 2015-12-03 Novozymes A/S Polypeptide ayant une activité de dnase permettant une réduction de l'électricité statique
WO2016087401A1 (fr) * 2014-12-05 2016-06-09 Novozymes A/S Variantes de lipase et polynucléotides codant pour ces dernières
WO2016096711A2 (fr) 2014-12-15 2016-06-23 Novozymes A/S Variants de subtilase
US20160369210A1 (en) 2013-07-03 2016-12-22 Basf Se Gel-like polymer composition obtained by polymerising a monomer containing acid groups in the presence of a polyether compound

Patent Citations (137)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3451935A (en) 1966-04-25 1969-06-24 Procter & Gamble Granular enzyme-containing laundry composition
GB1243784A (en) 1967-10-03 1971-08-25 Novo Terapeutisk Labor As Proteolytic enzymes, their production and use
GB1300596A (en) 1969-11-19 1972-12-20 Knapsack Ag Process for the manufacture of enzyme-containing granules
US4115292A (en) * 1977-04-20 1978-09-19 The Procter & Gamble Company Enzyme-containing detergent articles
EP0218272A1 (fr) 1985-08-09 1987-04-15 Gist-Brocades N.V. Enzymes lipolytiques et leur usage dans des compositions détergentes
EP0258068A2 (fr) 1986-08-29 1988-03-02 Novo Nordisk A/S Additif enzymatique pour détergent
EP0260105A2 (fr) 1986-09-09 1988-03-16 Genencor, Inc. Préparation d'enzymes à activité modifiée
US5389536A (en) 1986-11-19 1995-02-14 Genencor, Inc. Lipase from Pseudomonas mendocina having cutinase activity
DE3700128A1 (de) 1987-01-03 1988-07-14 Hoechst Ag Biologisch abbaubare poly- (hydroxyalkyl)- aminodicarbonsaeure-derivate, verfahren zu ihrer herstellung und verwendung derselben fuer depotzubereitungen mit kontrollierter wirkstoffabgabe
EP0283075A2 (fr) 1987-02-27 1988-09-21 Gist-Brocades N.V. Clonage moléculaire et expression de gènes codant pour des enzymes protéolytiques
WO1988009367A1 (fr) 1987-05-29 1988-12-01 Genencor, Inc. Compositions de nettoyage a base de cutinase
EP0305216A1 (fr) 1987-08-28 1989-03-01 Novo Nordisk A/S Lipase recombinante de humicola et procédé de production de lipases recombinantes de humicola
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
WO1989006279A1 (fr) 1988-01-07 1989-07-13 Novo-Nordisk A/S Genes de subtilisine mutes
WO1989006276A2 (fr) 1988-01-08 1989-07-13 Dpz Deutsches Primatenzentrum Gesellschaft Mbh Retrovirus de primates du type hiv-2, vaccins, compositions diagnostiques et pharmaceutiques
EP0331376A2 (fr) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. ADN recombinant, bactérie du genre pseudomonas le contenant et son utilisation dans un procédé de production de lipase
WO1989009830A1 (fr) 1988-04-12 1989-10-19 Genex Corporation Mutations de subtilisine
WO1989009819A1 (fr) 1988-04-12 1989-10-19 Genex Corporation Mutations combinantes de stabilisation de subtilisine
WO1990009446A1 (fr) 1989-02-17 1990-08-23 Plant Genetic Systems N.V. Cutinase
JPH02238885A (ja) 1989-03-13 1990-09-21 Oji Paper Co Ltd フェノールオキシダーゼ遺伝子組換えｄｎａ、該組換えｄｎａにより形質転換された微生物、その培養物及びフェノールオキシダーゼの製造方法
EP0407225A1 (fr) 1989-07-07 1991-01-09 Unilever Plc Enzymes et compositions détergentes enzymatiques
WO1991002792A1 (fr) 1989-08-25 1991-03-07 Henkel Research Corporation Enzyme proteolytique alcaline et procede de production
US5352604A (en) 1989-08-25 1994-10-04 Henkel Research Corporation Alkaline proteolytic enzyme and method of production
WO1991006637A1 (fr) 1989-10-31 1991-05-16 Genencor International, Inc. Mutants de subtilisine
WO1991016422A1 (fr) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Lipases bacillaires alcalines, sequences d'adn de codage pour celles-ci et bacilles produisant ces lipases
EP0458079A2 (fr) 1990-04-26 1991-11-27 Hoechst Aktiengesellschaft Agent de contraste ultrasonique, sa préparation et application comme diagnostic ou thérapeutique
WO1992001046A1 (fr) 1990-07-06 1992-01-23 Valtion Teknillinen Tutkimuskeskus Production de laccase au moyen d'organismes recombines
WO1992005249A1 (fr) 1990-09-13 1992-04-02 Novo Nordisk A/S Variantes lipasiques
WO1992019729A1 (fr) 1991-05-01 1992-11-12 Novo Nordisk A/S Enzymes stabilisees et compositions detergentes
WO1993024618A1 (fr) 1992-06-01 1993-12-09 Novo Nordisk A/S Variante de peroxydase avec stabilite amelioree vis-a-vis du peroxyde d'hydrogene
WO1994001541A1 (fr) 1992-07-06 1994-01-20 Novo Nordisk A/S Lipase de c. antarctica et variantes lipasiques
WO1994002597A1 (fr) 1992-07-23 1994-02-03 Novo Nordisk A/S Alpha-amylase mutante, detergent, agent de lavage de vaisselle et de liquefaction
WO1994018314A1 (fr) 1993-02-11 1994-08-18 Genencor International, Inc. Alpha-amylase stable a l'oxydation
WO1994025578A1 (fr) 1993-04-27 1994-11-10 Gist-Brocades N.V. Nouveaux variants de lipase utilises dans des detergents
WO1995006720A1 (fr) 1993-08-30 1995-03-09 Showa Denko K.K. Nouvelle lipase, micro-organisme la produisant, procede de production de cette lipase, et utilisation de ladite lipase
WO1995010603A1 (fr) 1993-10-08 1995-04-20 Novo Nordisk A/S Variants d'amylase
WO1995010602A1 (fr) 1993-10-13 1995-04-20 Novo Nordisk A/S Variants de peroxydase stables par rapport a h2o¿2?
WO1995014783A1 (fr) 1993-11-24 1995-06-01 Showa Denko K.K. Gene de lipase et lipase variante
WO1995022615A1 (fr) 1994-02-22 1995-08-24 Novo Nordisk A/S Procede pour preparer un variant d'une enzyme lipolytique
EP1921147A2 (fr) 1994-02-24 2008-05-14 Henkel Kommanditgesellschaft auf Aktien Enzymes améliorées et détergents les contenant
WO1995023221A1 (fr) 1994-02-24 1995-08-31 Cognis, Inc. Enzymes ameliorees et detergents les contenant
WO1995027046A2 (fr) 1994-03-31 1995-10-12 Unilever Nv Compositions antimicrobiennes enzymatiques comprenant des haloperoxydases
WO1995030744A2 (fr) 1994-05-04 1995-11-16 Genencor International Inc. Lipases a resistance aux tensioactifs amelioree
WO1995033836A1 (fr) 1994-06-03 1995-12-14 Novo Nordisk Biotech, Inc. Phosphonyldipeptides efficaces dans le traitement de maladies cardiovasculaires
WO1995035381A1 (fr) 1994-06-20 1995-12-28 Unilever N.V. Lipases modifiees provenant de pseudomonas et leur utilisation
WO1996000292A1 (fr) 1994-06-23 1996-01-04 Unilever N.V. Pseudomonas lipases modifiees et leur utilisation
WO1996012012A1 (fr) 1994-10-14 1996-04-25 Solvay S.A. Lipase, micro-organisme la produisant, procede de preparation de cette lipase et utilisation de celle-ci
WO1996013580A1 (fr) 1994-10-26 1996-05-09 Novo Nordisk A/S Enzyme a activite lipolytique
WO1996023872A1 (fr) 1995-02-02 1996-08-08 Stichting Centraal Laboratorium Van De Bloedtransfusiedienst Van Het Nederlandse Rode Kruis Enrichissement de cellules souches hematopoietiques provenant du sang ou de la moelle osseuse
WO1996027002A1 (fr) 1995-02-27 1996-09-06 Novo Nordisk A/S Nouveau gene de lipase et procede de production de lipase a l'aide de celui-ci
WO1996034946A1 (fr) 1995-05-05 1996-11-07 Novo Nordisk A/S Variantes du type protease et compositions
WO1997004102A1 (fr) 1995-07-14 1997-02-06 Novo Nordisk A/S Haloperoxydases provenant de curvularia verruculosa et acides nucleiques les codant
WO1997004079A1 (fr) 1995-07-14 1997-02-06 Novo Nordisk A/S Enzyme modifiee a activite lipolytique
WO1997007202A1 (fr) 1995-08-11 1997-02-27 Novo Nordisk A/S Nouvelles enzymes lipolytiques
WO1997008325A2 (fr) 1995-08-25 1997-03-06 Novo Nordisk Biotech, Inc. Laccases de coprin purifiees et acides nucleiques les codant
DE19545678A1 (de) 1995-12-07 1997-06-12 Goldschmidt Ag Th Copolymere Polyaminosäureester
WO1997043424A1 (fr) 1996-05-14 1997-11-20 Genencor International, Inc. α-AMYLASES MODIFIEES POSSEDANT DES PROPRIETES MODIFIEES DE FIXATION DU CALCIUM
WO1998010060A1 (fr) 1996-09-03 1998-03-12 Novo Nordisk A/S Variantes de peroxydase
WO1998015257A1 (fr) 1996-10-08 1998-04-16 Novo Nordisk A/S Derives de l'acide diaminobenzoique en tant que precurseurs de matieres tinctoriales
WO1998020116A1 (fr) 1996-11-04 1998-05-14 Novo Nordisk A/S Variants de subtilase et compositions
WO1998020115A1 (fr) 1996-11-04 1998-05-14 Novo Nordisk A/S Variants et compositions de subtilase
WO1999011768A1 (fr) 1997-08-29 1999-03-11 Novo Nordisk A/S Variants de la protease et compositions
WO1999019467A1 (fr) 1997-10-13 1999-04-22 Novo Nordisk A/S MUTANTS D'α-AMYLASE
WO1999027083A1 (fr) 1997-11-24 1999-06-03 Novo Nordisk A/S ENZYMES DE DEGRADATION DE LA PECTINE PROVENANT DU $i(BACILLUS LICHENIFORMIS)
WO1999027084A1 (fr) 1997-11-24 1999-06-03 Novo Nordisk A/S Nouvelles lyases de pectate
US6124127A (en) 1997-11-24 2000-09-26 Novo Nordisk A/S Pectate lyase
WO1999064619A2 (fr) 1998-06-10 1999-12-16 Novozymes A/S Nouvelles mannanases
WO2000022103A1 (fr) 1998-10-13 2000-04-20 Novozymes A/S Polypeptide modifie a reponse immunitaire reduite
WO2000034450A1 (fr) 1998-12-04 2000-06-15 Novozymes A/S Variantes de cutinase
WO2000060060A2 (fr) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides presentant une activite alcaline alpha-amylase et acides nucleiques les codant
WO2000060063A1 (fr) 1999-03-31 2000-10-12 Novozymes A/S Variante genetique de lipase
WO2001044452A1 (fr) 1999-12-15 2001-06-21 Novozymes A/S Variants de subtilase a performance de nettoyage amelioree sur des taches d'oeuf
WO2001079458A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides ayant une activite d'haloperoxidase
WO2001079461A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides a activite haloperoxydase
WO2001079460A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides a activite haloperoxydase
WO2001079459A2 (fr) 2000-04-14 2001-10-25 Novozymes A/S Polypeptides ayant une activite d'haloperoxydase et acides nucleiques qui les codent
WO2001092502A1 (fr) 2000-06-02 2001-12-06 Novozymes A/S Variants de cutinase
WO2002006442A2 (fr) 2000-07-19 2002-01-24 Novozymes A/S Variants d'enzymes degradant la paroi cellulaire
WO2002010355A2 (fr) 2000-08-01 2002-02-07 Novozymes A/S Mutants d'alpha-amylase a proprietes modifiees
DE10064983A1 (de) 2000-12-23 2002-07-18 Henkel Kgaa Neue Alkalische Protease aus Bacillus alcalophilus (DSM 11233)
WO2002088340A2 (fr) 2001-05-02 2002-11-07 Henkel Kommanditgesellschaft Auf Aktien Nouvelles variantes de proteases alcalines et detergents contenant ces nouvelles variantes
WO2002092741A2 (fr) 2001-05-14 2002-11-21 Novozymes A/S Compositions detergentes comprenant des lyases de pectates de bacillus subtilis
WO2003006602A2 (fr) 2001-07-12 2003-01-23 Novozymes A/S Variants de subtilase
WO2003054184A1 (fr) 2001-12-20 2003-07-03 Henkel Kommanditgesellschaft Auf Aktien Nouvelle protease alcaline extraite de bacillus gibsonii (dsm 14393) et agents de lavage et de nettoyage contenant cette nouvelle protease alcaline
WO2003055974A2 (fr) 2001-12-22 2003-07-10 Henkel Kommanditgesellschaft Auf Aktien Nouvelle protease alcaline obtenue a partir de bacillus sp. (dsm 14392) et agents de lavage et de nettoyage contenant cette protease alcaline
WO2003056017A2 (fr) 2001-12-22 2003-07-10 Henkel Kommanditgesellschaft Auf Aktien Nouvelle protease alcaline obtenue a partir de bacillus sp (dsm 14390) et agents de lavage et de nettoyage contenant cette protease alcaline
WO2003095638A1 (fr) 2002-05-14 2003-11-20 Novozymes A/S Variants de pectate lyase
WO2004003186A2 (fr) 2002-06-26 2004-01-08 Novozymes A/S Subtilases et variants de la subtilase presentant une immunogenicite modifiee
WO2004041979A2 (fr) 2002-11-06 2004-05-21 Novozymes A/S Variantes de subtilase
DE10304331A1 (de) 2003-02-04 2004-08-12 Henkel Kgaa Enzymatische Entfernung von Biofilmen auf Haushaltsoberflächen
WO2005056782A2 (fr) 2003-12-03 2005-06-23 Genencor International, Inc. Perhydrolase
US20070167344A1 (en) 2003-12-03 2007-07-19 Amin Neelam S Enzyme for the production of long chain peracid
US20080145353A1 (en) 2003-12-03 2008-06-19 Amin Neelam S Perhydrolase
WO2005063974A1 (fr) 2003-12-23 2005-07-14 Henkel Kommanditgesellschaft Auf Aktien Nouvelle protease alcaline et produits detergents et nettoyants contenant cette nouvelle protease alcaline
WO2005103244A1 (fr) 2004-04-23 2005-11-03 Henkel Kommanditgesellschaft Auf Aktien Nouvelles proteases alcalines et agents de lavage et detergents renfermant celles-ci
WO2006002643A2 (fr) 2004-07-05 2006-01-12 Novozymes A/S Variants d'alpha-amylases presentant des proprietes modifiees
WO2006066594A2 (fr) 2004-12-23 2006-06-29 Novozymes A/S Variantes de l'alpha-amylase
DE102005028295A1 (de) 2005-06-18 2006-11-16 Henkel Kgaa Proteasen aus psychrophilen Organismen
WO2007006305A1 (fr) 2005-07-08 2007-01-18 Novozymes A/S Variants de subtilase
WO2007087508A2 (fr) 2006-01-23 2007-08-02 Novozymes A/S Variantes de lipase
WO2008051491A2 (fr) 2006-10-20 2008-05-02 Danisco Us, Inc. Genencor Division Polyol oxydases
WO2008063400A1 (fr) 2006-11-09 2008-05-29 Danisco Us, Inc., Genencor Division Enzyme de fabrication de peracides à chaîne longue
WO2009061380A2 (fr) 2007-11-05 2009-05-14 Danisco Us Inc., Genencor Division Variants de bacillus sp. ts-23 alpha-amylase à propriétés modifiées
WO2009067279A1 (fr) 2007-11-21 2009-05-28 E.I. Du Pont De Nemours And Company Production de peracides employant une enzyme ayant une activité de perhydrolyse
WO2009109500A1 (fr) 2008-02-29 2009-09-11 Novozymes A/S Polypeptides à activité lipase et polynucléotides codant ces polypeptides
WO2009127702A2 (fr) 2008-04-17 2009-10-22 Novozymes A/S Variants de laccase
WO2010065455A2 (fr) 2008-12-01 2010-06-10 Danisco Us Inc. Enzymes ayant une activité lipase
WO2010100028A2 (fr) 2009-03-06 2010-09-10 Huntsman Advanced Materials (Switzerland) Gmbh Procédés enzymatiques de blanchissement-azurage des textiles
WO2010104675A1 (fr) 2009-03-10 2010-09-16 Danisco Us Inc. Alpha-amylases associées à la souche bacillus megaterium dsm90, et leurs procédés d'utilisation
WO2010107560A2 (fr) 2009-03-18 2010-09-23 Danisco Us Inc. Cutinase fongique de magnaporthe grisea
WO2010111143A2 (fr) 2009-03-23 2010-09-30 Danisco Us Inc. Acyltransférases associées à cal a et leurs procédés d'utilisation
WO2011036263A1 (fr) 2009-09-25 2011-03-31 Novozymes A/S Variants de subtilase
WO2011036264A1 (fr) 2009-09-25 2011-03-31 Novozymes A/S Utilisation de variants de protéase
WO2011072099A2 (fr) 2009-12-09 2011-06-16 Danisco Us Inc. Compositions et procédés comprenant des variants de protéase
WO2011084599A1 (fr) 2009-12-21 2011-07-14 Danisco Us Inc. Compositions détergentes contenant une lipase de bacillus subtilis et procédés d'utilisation associés
WO2011084417A1 (fr) 2009-12-21 2011-07-14 Danisco Us Inc. Compositions détergentes contenant une lipase issue de geobacillus stearothermophilus et leurs procédés d'utilisation
WO2011084412A1 (fr) 2009-12-21 2011-07-14 Danisco Us Inc. Compositions détergentes contenant une lipase issue de thermobifida fusca et leurs procédés d'utilisation
WO2011098531A1 (fr) 2010-02-10 2011-08-18 Novozymes A/S Variants et compositions contenant des variants à stabilité élevée en présence d'un agent chélateur
WO2011150157A2 (fr) 2010-05-28 2011-12-01 Danisco Us Inc. Compositions de détergent contenant une lipase de streptomyces griseus et leurs procédés d'utilisation
WO2012137147A1 (fr) 2011-04-08 2012-10-11 Danisco Us, Inc. Compositions
WO2013001087A2 (fr) 2011-06-30 2013-01-03 Novozymes A/S Procédé de criblage d'alpha-amylases
WO2013001078A1 (fr) 2011-06-30 2013-01-03 Novozymes A/S Variants d'alpha-amylase
US20130244920A1 (en) * 2012-03-16 2013-09-19 David M. Lee Water soluble compositions incorporating enzymes, and method of making same
WO2013148492A1 (fr) 2012-03-29 2013-10-03 Novozymes A/S Utilisation d'enzymes pour préparer des films hydrosolubles
WO2013184577A1 (fr) 2012-06-08 2013-12-12 Danisco Us Inc. Variants d'alpha-amylase dérivés de l'alpha-amylase de cytophaga sp. amylase/ (cspamy2)
WO2014152674A1 (fr) 2013-03-14 2014-09-25 Novozymes A/S Films solubles dans l'eau contenant des enzymes et des inhibiteurs
WO2014152547A2 (fr) 2013-03-14 2014-09-25 Novozymes A/S Poche de détergent comportant un film enzymatique soluble dans l'eau
EP2799533A1 (fr) 2013-04-30 2014-11-05 Novozymes A/S Inhibiteur et protease contenant des films solubles dans l'eau
WO2014186464A1 (fr) 2013-05-14 2014-11-20 Novozymes A/S Varaints de lipase humicola lanuginosa stabilisée dans des films hydrosolubles
US20160369210A1 (en) 2013-07-03 2016-12-22 Basf Se Gel-like polymer composition obtained by polymerising a monomer containing acid groups in the presence of a polyether compound
WO2015155351A1 (fr) 2014-04-11 2015-10-15 Novozymes A/S Composition de détergent
WO2015155350A1 (fr) 2014-04-11 2015-10-15 Novozymes A/S Composition de détergent
WO2015166075A1 (fr) 2014-05-02 2015-11-05 Novozymes A/S Composition de détergent
WO2015181286A1 (fr) 2014-05-28 2015-12-03 Novozymes A/S Utilisation d'un polypeptide
WO2015181287A1 (fr) 2014-05-28 2015-12-03 Novozymes A/S Polypeptide ayant une activité de dnase permettant une réduction de l'électricité statique
WO2016087401A1 (fr) * 2014-12-05 2016-06-09 Novozymes A/S Variantes de lipase et polynucléotides codant pour ces dernières
WO2016096711A2 (fr) 2014-12-15 2016-06-23 Novozymes A/S Variants de subtilase

Non-Patent Citations (15)

* Cited by examiner, † Cited by third party
Title
"Current Protocols", 1998, GREENE PUBLISHING ASSOCIATES, INC. AND JOHN WILEY & SONS, INC., article "Current Protocols in Molecular Biology"
"Protein Purification", 1989, VCH PUBLISHERS, NEW YORK
CHILDS ET AL., BIOCHEMICAL J, vol. 145, 1975, pages 93 - 103
DARTOIS ET AL., BIOCHEMICA ET BIOPHYSICA ACTA, vol. 1131, 1992, pages 253 - 360
DELMAR ET AL., ANALYTICAL BIOCHEM, vol. 99, 1979, pages 316 - 320
EL SMITH ET AL., J. BIOL CHEM, vol. 243, 1968, pages 2184 - 2191
GUPTA ET AL., APPL. MICROBIOL. BIOTECHNOL., vol. 60, 2002, pages 381 - 395
GUPTA ET AL., BIOTECHNOL. APPL. BIOCHEM., vol. 37, 2003, pages 63 - 71
JA WELLS ET AL., NUCLEIC ACIDS RESEARCH, vol. 11, 1983, pages 7911 - 7925
JACOBS ET AL., NUCL. ACIDS RES, vol. 13, 1985, pages 8913 - 8926
NEEDLEMANWUNSCH ALGORITHM, J. MOL. BIOL., vol. 48, 1979, pages 443 - 453
R. SIEZEN: "Subtilisin enzymes", 1996, article "Subtilases: Subtilisin-like Proteases", pages: 75 - 95
SIEZEN ET AL., PROTEIN ENG., vol. 4, 1991, pages 719 - 737
SIEZEN ET AL., PROTEIN SCIENCE, vol. 6, 1997, pages 501 - 523
VASANTHA ET AL., J. BACTERIOL., vol. 159, 1984, pages 811 - 819

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2023225459A2 (fr) 2022-05-14 2023-11-23 Novozymes A/S Compositions et procédés de prévention, de traitement, de suppression et/ou d'élimination d'infestations et d'infections phytopathogènes
CN114931934A (zh) * 2022-05-25 2022-08-23 安徽皖仪科技股份有限公司 一种接枝型阳离子交换色谱柱填料及其制备方法
CN114931934B (zh) * 2022-05-25 2024-04-23 安徽皖仪科技股份有限公司 一种接枝型阳离子交换色谱柱填料及其制备方法

Similar Documents

Publication Publication Date Title
ES2763561T3 (es) Composiciones de limpieza y sus usos
ES2699838T3 (es) Composición de detergente
EP2992076B1 (fr) Microencapsulation d'enzymes détergentes
CN108026487B (zh) 包含具有黄原胶降解活性的多肽的洗涤剂组合物
CA3058520A1 (fr) Compositions de detergent et leurs utilisations
WO2018185285A1 (fr) Compositions de nettoyage et utilisations correspondantes
CA3058519A1 (fr) Compositions de nettoyage comprenant une desoxyribonuclease et une protease
US20210189296A1 (en) Cleaning compositions and uses thereof
EP3607043A1 (fr) Compositions de nettoyage et leurs utilisations
US11634665B2 (en) Detergent composition
US20170218315A1 (en) Detergents and Compositions with Enzymatic Polymer Particles
JP6615758B2 (ja) 水可溶性フィルム中の酵素粒子の使用
KR20220073769A (ko) 세제 조성물에서의 데옥시리보스뉴클레아제 용도
US20170145353A1 (en) Co-Granulate of Enzyme and Bleach Catalyst
WO2019238761A1 (fr) Films multicouches hydrosolubles contenant des produits chimiques et des enzymes actifs de lavage
EP3137589B1 (fr) Microencapsulation de composants détergents
WO2018121398A1 (fr) Produit enzymatique solide encapsulé
US11021681B2 (en) Manganese bleach catalyst granules for use in dishwash detergents
WO2022089571A1 (fr) Composition détergente et procédé de nettoyage
WO2019076800A1 (fr) Compositions de nettoyage et leurs utilisations
WO2022083538A1 (fr) Utilisation de polypeptide, composition détergente et procédé de nettoyage
KR20220119609A (ko) 디스페르신 vi을 포함하는 세정 조성물

Legal Events

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

Ref document number: 19730340

Country of ref document: EP

Kind code of ref document: A1

NENP Non-entry into the national phase

Ref country code: DE

122 Ep: pct application non-entry in european phase

Ref document number: 19730340

Country of ref document: EP

Kind code of ref document: A1