WO2009121725A1 - Detergents and cleaners comprising proteases from xanthomonas - Google Patents

Detergents and cleaners comprising proteases from xanthomonas Download PDF

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WO2009121725A1
WO2009121725A1 PCT/EP2009/053283 EP2009053283W WO2009121725A1 WO 2009121725 A1 WO2009121725 A1 WO 2009121725A1 EP 2009053283 W EP2009053283 W EP 2009053283W WO 2009121725 A1 WO2009121725 A1 WO 2009121725A1
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protease
xanthomonas
according
washing
cleaning
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PCT/EP2009/053283
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German (de)
French (fr)
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Petra Siegert
Marion Merkel
Cornelia Kluin
Timothy O'connell
Karl-Heinz Maurer
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Henkel Ag & Co. Kgaa
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    • CCHEMISTRY; METALLURGY
    • C11ANIMAL AND VEGETABLE OILS, FATS, FATTY SUBSTANCES AND WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11DDETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16Organic compounds
    • C11D3/38Products with no well-defined composition, e.g. natural products
    • C11D3/386Preparations containing enzymes, e.g. protease, amylase

Abstract

The detergency of detergents and cleaners is improved by adding a protease from a bacterium of the genus Xanthomonas.

Description

Detergents and cleaners containing proteases from Xanthomonas

The invention is directed to detergent and cleaning agent containing a protease from a bacterium of the genus Xanthomonas, these proteases themselves and to the preparation and use of these proteases. Furthermore, the invention is directed to cleaning processes in which these resources are used and to uses of these agents.

preferred proteases are used so far of the subtilisin type of detergents and cleaning agents. The proteases used in the processes known from the prior art washing or cleaning agents either derive originally from microorganisms, for example of the genera Bacillus, Streptomyces, Humicola or Pseudomonas, and / or are produced according to known biotechnological processes using suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or filamentous fungi. Examples include the subtilisins BPN 'and Carlsberg, protease PB92, subtilisins 147 and 309, the protease from Bacillus lentus, in particular from Bacillus lentus DSM 5483 subtilisin DY and the subtilases, but not more subtilisins in the strict sense as enzymes thermitase, proteinase K and proteases TW3 and TW7. Other usable proteases are, for example, under the trade name Durazym®, Relase®, Everlase®, Nafizym, Natalase®, Kannase® and Ovozyme® from Novozymes, under the trade names Purafect, Purafect OxP, Purafect Prime and Properase.RTM ® from Genencor, that under the trade name Protosol® from Advanced Biochemicals Ltd., Thane, India, under the trade name Wuxi® from Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® and protease P ® from Amano Pharmaceuticals Ltd., Nagoya, Japan, and the enzymes available under the name proteinase K-16 from Kao Corp., Tokyo, Japan.

From the prior art is further known that bacteria of the genus Xanthomonas produce enzymes that have proteolytic activity. These enzymes are often associated with diseases of plants in connection causing bacteria of the genus Xanthomonas as plant pathogenic. So describe Dow al et. in two publications (Applied and Environmental Microbiology, 1990, 2994-2998 and Applied and Environmental Microbiology, 1993, 3996 to 4003), the proteases PRT1 and PRT2 pathogenesis of Xanthomonas campestris against the background of the plant. In Chang-Ho Lee et al. (Jour. Microbiol., 1995, 115-119) discloses an alkaline protease derived from Xanthomonas sp. YL-37 is formed. In addition to the generally accepted statement that proteolytic enzymes are used per se in laundry products, no washing or cleaning agents are disclosed that include a protease from Xanthomonas. so that no washing and cleaning agents are known from the prior art in which a protease from a bacterium of the genus Xanthomonas is inserted. A disadvantage of the proteases previously used in washing and cleaning agents, that they often do not have a satisfactory proteolytic activity and it is therefore based on protein-containing stains exhibit containing Mitttel no satisfactory cleaning performance. In particular this is the case at low temperatures, for example between 2O 0 C and 6O 0 C, so that the show-containing washing or cleaning agent in this temperature range, no optimal cleaning performance. Thus, there is a need, novel proteases, and in particular new microbial proteases find for use in detergents and cleaning agents and provide novel washing and cleaning agents according to compositions containing such proteases.

The present invention therefore has for its object to provide washing or cleaning agent, which in terms of several stains, exhibit improved removal of proteinaceous residues with respect to at least one stain, preferably. In particular, the washing or cleaning agents should have an improved removal of proteinaceous residues with respect to at least one stain, preferably with respect to a plurality of stains at low temperatures, in particular in a temperature range between 20 and 6O 0 C, point. Another object of the present invention is to provide just such protease enzymes suitable for use in the inventive detergents and cleaning products and by good, preferably proteolytic by an improved activity with respect to at least one stain, preferably with respect a plurality of stains, distinguished when they are used in detergents or cleaners, in particular in the above-mentioned temperature range.

The invention thus relates to a detergent or cleaning agent comprising a protease that is naturally present in a bacterium of the genus Xanthomonas and at least one other detergent ingredient. Surprisingly it has been found that proteases derived from a bacterium of the genus Xanthomonas, advantageously be used in detergents or cleaners and in the inventive detergents or cleaning formulations in particular also at low temperatures, in particular in a temperature range between 20 and 6O 0 C, improved Distance protease-sensitive residues, such as stains on textiles or dishes, allow.

In a preferred embodiment, the bacterium of the genus Xanthomonas is selected from the group consisting of Xanthomonas albilineans, Xanthomonas alfalfae, Xanthomonas alfalfae subsp. alfalfae, Xanthomonas alfalfae subsp. citrumelonis, Xanthomonas ampelina (Xylophilus ampelinus), Xanthomonas arboricola, Xanthomonas axonopodis, Xanthomonas bromi, Xanthomonas campestris, Xanthomonas cassavae, Xanthomonas citri, Xanthomonas citri subsp. citri, Xanthomonas citri subsp. malvacearum, Xanthomonas codiaei, Xanthomonas Cucurbitae, Xanthomonas Cynarae, Xanthomonas euvesicatoria, Xanthomonas fragariae, Xanthomonas fuscans, Xanthomonas fuscans subsp. aurantifolii, Xanthomonas fuscans subsp. fuscans, Xanthomonas gardneri, Xanthomonas hortorum, Xanthomonas hyacinthi, Xanthomonas melonis, Xanthomonas oryzae, Xanthomonas perforans, Xanthomonas phaseoli, Xanthomonas pisi, Xanthomonas populi, Xanthomonas sacchari, Xanthomonas theicola, Xanthomonas translucens, Xanthomonas vasicola, Xanthomonas vesicatoria. It has been found that this particular Xanthomonas species express proteases which show corresponding advantages in the inventive detergents or cleaning agents.

Naturally present in this context means that the protease is a bacterial protease own, which can be isolated from the bacterium. especially those proteases, it will not be included with, therefore, that were introduced with the aid of genetic engineering methods in a bacterial strain of the present invention and expressed by this recombinant. ie for the bacteria of the genus Xanthomonas the production organism on the basis of the incorporation of the gene encoding the protease gene in this organism by genetic engineering - - Of the prior art known proteases that are produced by means of a bacterial strain of the invention, therefore, are not subject the invention.

The classical approach to extraction of the enzymes is known to those skilled in the field of enzyme technology and is microorganisms-containing samples under the conditions considered appropriate - to cultivate - for example in an alkaline medium. In this manner, enrichment cultures of the microorganisms are obtained, which thus contain the desired enzymes, in this case, proteases which are active under the relevant conditions. From this, then for example the plating on protein-containing agar plates and measuring the lysis zones formed microorganisms selected with the most efficient enzymes and purified or they identified genes encoding and cloned. Such an approach, for example, in the textbook "Alkalophilic Microorganisms. A new microbial world "of K.Horikoshi and T.Akiba (1982), Japan Scientific Societies Press, Springer-Verlag, New York, Heidelberg, Berlin, ISBN 0-387-10924-2, Chapter 2, pages 9-26 described . this procedure described above is also applicable to obtain the proteases, or the genes encoding them from bacteria of the Xanthomonas, in particular those mentioned in this application Xanthomonas species.

However, it is by no means so that each or any protease that is naturally present in a microorganism, particularly a bacterium, is also advantageously used in a washing or cleaning agent, that comprises in said means a satisfactory proteolytic activity results when the agent is in a satisfactory removal of protein-containing stains. Therefore, it is all the more surprising that, proteases are present in bacteria of the genus Xanthomonas, in particular in the above-described Xanthomonas species that are suitable for use in detergents and cleaners and in particular in application of them containing washing and cleaning agent satisfactory cause removal of protein stains. Bacteria of this genus of bacteria - and in particular the types mentioned above - possess naturally, without genetic or molecular biological modification, proteolytic enzymes, the conditions under the demanding application have a sufficiently high proteolytic activity of detergents and cleaning agents to proteinaceous stains under the conditions of use of the reduce washing or cleaning agent. Demanding application conditions in detergents and cleaning agents result in particular due to the presence of one or more other ingredients in such compositions and in the plane formed by them wash liquor during the washing process such as bleach, bleach activators, surfactants, (Builder) scaffold -substances and / or due to the pH-value of such agents, and the wash liquor formed by them during the washing process and / or due to the ionic strength and / or temperature of the wash liquor during the washing process. It has been found that a washing and cleaning agent with a protease from a bacterium of the genus Xanthomonas having an improved performance relative to a protease-free medium and achieved a very good cleaning performance in terms of protease-sensitive stains.

Within the genus Xanthomonas, some strains have been found to be particularly advantageous. This naturally contain proteases that are particularly suitable for use in inventive detergents and cleaning agents. In a preferred embodiment of the invention, the means is characterized in that the bacterium is selected from the group consisting of Xanthomonas axonopodis DSM 3585, Xanthomonas axonopodis pvar. DSM 50850 begoniae, Xanthomonas axonopodis pvar. pvar malvacearum DSM 1220 Xanthomonas campestris DSM 1050 (NCPPB 1929), Xanthomonas campestris DSM 19000, Xanthomonas campestris. campestris DSM 3586, Xanthomonas campestris pvar. pelargonii DSM 50,857th These strains have been deposited and publicly accessible in the German Collection of Microorganisms and Cell Cultures (DSMZ), Inhoffenstraße 7b, 38124 Braunschweig, Germany (www.dsmz.de).

As detergent can in this case any solid, liquid or flowable gel, packed in portions or individually portioned, powdered, granulated, pressed into tablets, paste, sprayable or assembled in other conventional dosage forms means for mechanical or manual washing of fabrics are used. Among the detergents further include washing aids, which are metered in in the manual or machine washing of textiles to the actual detergent, in order to obtain a further effect. To the cleaners all, also occurring in all specified dosage forms compositions for cleaning hard surfaces, manual and machine dishwashing detergents, carpet cleaners, scouring agents, glass cleaners, toilet Duftspüler, etc. are counted. Textilvor- and post-treatment agents are finally on the one hand, such means with which the piece of laundry is brought into contact prior to the actual wash, for example to solubilize stubborn dirt, on the other hand, such that downstream in the actual fabric laundering step, further the laundry desirable impart properties such as pleasant handle, crease resistance or low charge. At the latter means the softener are among others expected. "Flowable" in the sense of the present application are compositions which are pourable and may have viscosities up to several 10,000 mPas., The viscosity (measured using standard methods, for example, Brookfield viscometer LVT-II at 20 U / min and 2O 0 C, spindle 3) and is preferably in the range from 5 to 10,000 mPas. preferred compositions have viscosities of 10 to 8000 mPas, with values ​​between 120 3000 mPas are particularly preferred. in the present application all detergents and cleaning agents are also used as means summarized.

Preferably, an inventive composition contains the protease in an amount of from 2 ug to 20 mg, preferably from 5 ug to 17.5 mg, particularly preferably from 20 .mu.g to 15 mg and very particularly preferably from 50 .mu.g to 10 mg per g of the composition.

The washing or cleaning agent according to the invention contain at least one other detergent ingredient in addition to a protease from a bacterium of the genus Xanthomonas. Preferably, the detergent ingredient is selected from the group consisting of builder, surfactant thereof surfactant, bleaching agent based on organic and / or inorganic peroxygen compounds, bleach activators, organic solvent, acid, anti-redeposition agent, optical brightener, polymeric thickening agents and combinations thereof.

In particular, a combination of a protease which is naturally present in a bacterium of the genus Xanthomonas, with one or more further ingredient (s) of the center proves to be advantageous, since such an agent an improved cleaning performance resulting synergism, in particular between the protease and comprising, the further ingredient. This means that the agent enhanced removal of stains such as protein-containing soils, caused in comparison with an agent, which contains either only one of the two components or even in comparison to the expected cleaning performance of a product with two components because of the sheer addition of the respective individual contributions of these two components to the cleaning performance of the agent. In particular by the combination of a protease which is naturally present in a bacterium of the genus Xanthomonas, with one of the surfactants described below, and / or builders and / or bleaching agents, such synergism is achieved.

Suitable surfactants are in particular anionic surfactants, nonionic surfactants and mixtures thereof, but also cationic, zwitterionic and amphoteric surfactants in question.

Suitable nonionic surfactants are in particular alkyl glycosides and ethoxylation and / or propoxylation products of alkyl glycosides or linear or branched alcohols containing 12 to 18 carbon atoms in the alkyl moiety and 3 to 20, preferably 4 to 10 alkyl ether. In addition, corresponding ethoxylation and / or propoxylation products of N-alkylamines, vicinal diols, fatty acid amides and Fettsäureestern corresponding to the long-chain alcohol derivatives with regard to the alkyl moiety, and of alkylphenols of 5 to 12 carbon atoms in the alkyl radical. can be used as nonionic surfactants alcohol are preferably alkoxylated, advantageously ethoxylated, more especially primary alcohols preferably containing 8 to 18 carbon atoms and on average 1 to 12 moles of ethylene oxide (EO) per mole of used, in which the alcohol methyl-branched linear or preferably in the 2-position linear and methyl-branched radicals may contain the mixtures typically present in oxoalcohol radicals. However, alcohol ethoxylates containing linear radicals of alcohols of native origin with 12 to 18 carbon atoms, for example coconut, palm, tallow fat or oleyl alcohol, and preferably on average 2 to 8 EO per mole of alcohol. Preferred ethoxylated alcohols include, for example, C 12 -C 14 -alcohols containing 3 EO or 4 EO, C 9 -C 11 -alcohols with 7 EO and 2-propylheptanol with 7 EO, C 13 -C 15 alcohols with 3 EO; 5 EO, 7 EO or 8 EO, C 12 -C 18 - alcohols containing 3 EO, 5 EO or 7 EO and mixtures thereof, such as mixtures of C 12 -C 14 alcohol with 3 EO and C 12 -C 18 - alcohol containing 7 EO. Another preferred nonionic surfactant is a mixture of C16-C18 fatty alcohol with 7 EO and 2-propylheptanol with 7 EO (ratio about 1: 2). The degrees of ethoxylation mentioned are statistical averages which may be an integer or a fractional number for a specific product. Preferred alcohol ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE). In addition to these nonionic surfactants, fatty alcohols containing more than 12 EO may also be used. Examples include (TaIg-) fatty alcohols containing 14 EO, 16 EO, 20 EO, 25 EO, 30 EO or 40 EO. In particular, in compositions for use in automatic process Extremely low-foaming compounds are normally used. These preferably include C 12 -C 18 alkyl polyethylene glycol polypropylene glycol ethers containing up to 8 moles of ethylene oxide and propylene oxide units in the molecule. One can also use other known low-foaming nonionic surfactants such as C 12 -C 18 alkyl polyethylene po- lybutylenglykolether each having up to 8 moles of ethylene oxide and butylene oxide units in the molecule and end-capped Alkylpolyalkylenglykolmischether. Particularly preferably the alkoxylated alcohols containing hydroxyl, as described in European Patent Application EP O 300 305 so-called hydroxy are. The nonionic surfactants include alkyl glycosides of the formula RO (G) x employed in which R is a primary linear or methyl-branched, more particularly 2-methyl-branched aliphatic radical containing 8 to 22, preferably 12 to 18 carbon atoms and G a glycose unit having 5 or 6 C atoms, preferably for glucose. The degree of oligomerization x, which indicates the distribution of monoglycosides and oligoglycosides, is any number - which may take as an analytically determined quantity, also fractional values ​​- Between 1 and 10; x is preferably 1, 2 to 1; 4. Also suitable are polyhydroxy fatty acid amides of the formula (III) in which R 1 CO is an aliphatic acyl radical having 6 to 22 carbon atoms, R 2 represents hydrogen, an alkyl or hydroxyalkyl having 1 to 4 carbon atoms and [Z] is a linear or branched polyhydroxyalkyl having 3 to 10 carbon atoms and 3 to 10 hydroxyl groups:

R 2

R 1 -C0-N- [Z] (III) Preferably, the polyhydroxy fatty acid amides of reducing sugars having 5 or 6 carbon atoms, more particularly from glucose. The group of polyhydroxyfatty acid amides also includes compounds of formula (IV),

R 4 is -OR 5

(IV)

R 3 -CO-N- [Z]

in which R 3 is a linear or branched alkyl or alkenyl group having 7 to 12 carbon atoms, R 4 is a linear, branched or cyclic alkylene residue or an arylene radical having 2 to 8 carbon atoms and R 5 is a linear, branched or cyclic alkyl group or a aryl group or an oxyalkyl group having 1 to 8 carbon atoms, which C-ι-C 4 alkyl or phenyl groups being preferred, and [Z] is a linear polyhydroxyalkyl residue, whose alkyl chain is substituted with at least two hydroxyl groups, or alkoxylated, preferably ethoxylated or propoxylated derivatives of this residue. [Z] is preferably obtained here by reductive amination of a sugar such as glucose, fructose, maltose, lactose, galactose, mannose or xylose. The N-alkoxy- or N-aryloxy-substituted compounds can then be converted as a catalyst in the desired polyhydroxy, for example by reaction with fatty acid methyl ester in the presence of an alkoxide. Another class of preferred nonionic surfactants which are used either as sole nonionic surfactant or in combination with other nonionic surfactants, in particular together with alkoxylated fatty alcohols and / or alkyl glycosides, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl ester, preferably having 1 to 4 carbon atoms in the alkyl chain, especially fatty acid methyl ester. Nonionic surfactants of the amine oxide type, for example N- cocoalkyl-N, N-dimethylamine oxide and N-tallowalkyl-N, N-dihydroxyethylamine oxide, and the fatty acid alkanolamide may be suitable. The amount of these nonionic surfactants is preferably not more than that of the ethoxylated fat alcohols, especially not more than half of them. Other suitable surfactants are so-called Gemini surfactants can be considered. Among such compounds are generally understood that possess two hydrophilic groups per molecule. These groups are separated from each other generally by a so-called "spacer". This spacer is usually a carbon chain which should be long enough that the hydrophilic groups are a sufficient distance so that they can act independently. Such surfactants are generally characterized by an unusually low critical micelle concentration and the ability to greatly reduce the surface tension of the water from. In exceptional cases, the expression gemini surfactants not only such "dimeric" but also "trimeric" surfactants. Suitable gemini surfactants are sulfated hydroxy mixed ethers, for example, or dimer alcohol bis- and trimer alcohol tris-sulfates and ether sulfates. End-capped dimeric and trimeric mixed distinguished in particular by their bi- and multifunctionality. So the end-capped surfactants have good wetting properties and are low-foaming, so they are particularly suitable for use in machine washing or cleaning processes. but can also be used Gemini acid amides or poly-polyhydroxy. Also suitable are the Schwefelsäuremonoester the profiled with 1 to 6 moles of ethylene oxide ethoxylated linear or branched C 7 -C 2 i-alcohols such as 2-methyl-branched C 9 -C i-alcohols containing on average 3.5 mol ethylene oxide (EO) or C 12 -C 18 -FeHaIkOhOIe having 1 to 4 EO. The preferred anionic surfactants include the salts of alkylsulfosuccinic acid, which are also known as sulfosuccinates or as sulfosuccinic acid esters and the Monoester and / or diesters of sulfosuccinic acid with alcohols, preferably fatty alcohols and especially ethoxylated fatty alcohols include, represent. Preferred sulfosuccinates contain C 8 - C 18 fatty alcohol radicals or mixtures thereof. Particularly preferred sulfosuccinates contain a fatty alcohol radical derived from ethoxylated fatty alcohols which, considered in isolation, represent nonionic surfactants. Of these sulfosuccinates whose fatty alcohol radicals are derived from ethoxylated fatty alcohols with a narrow homolog distribution are particularly preferred. Likewise, it is also possible to use alk (en) ylbernstein- acid preferably containing 8 to 18 carbon atoms in the alk (en) yl chain or salts thereof. Other suitable anionic surfactants are fatty acid derivatives of amino acids, such as N- methyl taurine (taurides) and / or N-methylglycine (sarcosides) into consideration. Particularly preferred are the Sarcosides or sarcosinates, above all sarcosinates of higher and optionally mono- or polyunsaturated fatty acids, such as oleyl are. Other anionic surfactants in particular, soaps. Particularly suitable are saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid and behenic acid, and in particular from natural fatty acids, for example coconut, palm kernel or tallow soap mixtures derived. Along with these soaps or as a substitute for soaps also known alkenylsuccinic acid salts can be used.

The anionic surfactants, including the soaps, may be present in the form of their sodium, potassium or ammonium salts and as soluble salts of organic bases such as mono-, di- or triethanolamine. Preferably, the anionic surfactants are in the form of their sodium or potassium salts, in particular in the form of the sodium salts.

Surfactants are present in the compositions preferably in amounts ranging from 5 wt .-% to 50 wt .-%, particularly 8 wt .-% to 30 wt .-%, of.

An agent of the invention preferably contains at least one water-soluble and / or water-insoluble, organic and / or inorganic builders. The water-soluble organic builders include polycarboxylic acids, particularly citric acid and sugar acids, monomeric and polymeric aminopolycarboxylic acids, in particular methylglycinediacetic acid, nitrilotriacetic acid and ethylenediaminetetraacetic acid and polyaspartic acid, polyphosphonic acids, in particular aminotris (methylenephosphonic acid), ethylenediaminetetrakis (methylenephosphonic acid) and 1-hydroxyethyl than-1, 1-diphosphonic acid, acids, polymeric hydroxy compounds such as dextrin, and polymeric (poly) carboxylic, in particular obtainable by oxidation of polysaccharides or dextrins polycarboxylates, polymeric acrylic acids, methacrylic acids, maleic acids and copolymers thereof, the copolymerized also contain small amounts of polymerizable substances with no carboxylic acid functionality include can. The molecular weight of the homopolymers of unsaturated carboxylic acids is generally from 3000 to 200,000, that of the copolymers 2000-200000, preferably from 30,000 to 120,000, based on free acid. A particularly preferred acrylic acid-maleic acid copolymer has a relative molecular weight from 30,000 to 100,000. Commercial products are, for example, Sokalan CP 5, CP 10 and PA 30 from BASF. Suitable, but less preferred compounds of this class are copolymers of acrylic acid or methacrylic acid with vinyl ethers, such as vinyl, Vinylester, ethylene, propylene and styrene, in which the proportion of the acid is at least 50 wt .-%. As the water-soluble organic builders are terpolymers may be used as monomers containing two unsaturated acids and / or their salts and as third monomer, vinyl alcohol and / or an esterified vinyl alcohol or a carbohydrate. The first acidic monomer or its salt is derived from a monoethylenically unsaturated C 3 -C 8 carboxylic acid and preferably from a C 3 -C 4 monocarboxylic acid, in particular (meth) acrylic acid. The second acidic monomer or its salt may be 4 -C lylsulfonsäure a derivative of a C 8 -dicarboxylic acid, maleic acid being particularly preferred, and / or a derivative of Al, which is substituted in the 2-position with an alkyl or aryl group may be , Such polymers generally have a molecular weight from 1000 to 200,000. Other preferred copolymers are those which contain as monomers, acrolein and acrylic acid / acrylic acid salts or vinyl acetate. in the form of aqueous solutions, preferably in the form of the organic builder substances can be used 30 to 50 gewichtspro- zentiger aqueous solutions, in particular for the production of liquid detergents. All said acids are generally used in the form of their water-soluble salts, particularly their alkali metal salts.

Such organic builder substances may, if desired, in amounts up to 40 wt .-%, in particular up to 25 wt .-%, and contain preferably from 1 wt .-% to 8 wt .-%. Quantities near the upper limit mentioned are preferably used in paste-form or liquid, more particularly water-containing agents.

As the water-soluble inorganic builder materials are in particular alkali metal silicates, alkali metal carbonates and alkali metal phosphates which may be present in the form of their alkaline, neutral or acidic sodium or potassium salts, are also suitable. Examples include trisodium phosphate, tetrasodium diphosphate, disodium dihydrogen diphosphate, pentasodium triphosphate, so-called sodium hexametaphosphate, trisodium phosphate oligomer with degrees of oligomerization of 5 to 1000, particularly 5 to 50, and the corresponding potassium salts or mixtures of sodium and potassium salts. Suitable water-insoluble, water-dispersible inorganic builders are alkali metal aluminosilicates, in particular crystalline or amorphous, in amounts of up to 50 wt .-%, preferably not more than 40 wt .-%, and in liquid compositions and in particular of 1 wt .-% to 5 wt .-%, used. Among these, the crystalline sodium aluminosilicates in detergent quality, more particularly zeolite A, P and optionally X, alone or in mixtures, for example in the form of a co-crystals of zeolites A and X (Vegobond® AX, a commercial product of Condea Augusta SpA), preferably , Quantities near the upper limit mentioned are preferably used in solid particulate compositions. Suitable alumosilicates contain no particles having a particle size of about 30 microns and preferably consist of at least 80 wt .-% of particles having a size below 10 microns. Your calcium binding like that can be determined in accordance with German Patent DE 24 12 837, is usually in the range of 100 to 200 mg CaO per gram.

Suitable substitutes or partial substitutes for the alumosilicate mentioned are crystalline alkali metal silicates which may be present alone or in admixture with amorphous silicates. The use as builders in the alkali metal silicates preferably have a molar ratio of alkali metal oxide to SiO 2 of less than 0.95, in particular from 1: 1 1 to 1: 12, and may be amorphous or crystalline. Preferred alkali metal silicates are the sodium silicates, more particularly amorphous sodium silicates, with a molar ratio Na 2 O: SiO 2 of 1: 2 to 1: 2.8. The crystalline silicates which may be present alone or in admixture with amorphous silicates, are crystalline layer silicates with the general formula Na 2 Si x O y are used 2x + 1 H 2 O, in which x, known as the modulus, an integer of 1, 9 is up to 22, in particular 1, 9 to 4 and y is a number from 0 to 33, preferred values ​​for x being 2, 3 or. 4 Preferred crystalline layer silicates are those in which x assumes in said general formula the values ​​2 or the third In particular, both .beta.- and δ-sodium (Na 2 Si 2 O 5 y H 2 O) is preferred. prepared from amorphous alkali silicates, practically water-free crystalline alkali metal silicates of the abovementioned general formula in which a number of from 1: 9 to 2.1 x can be used in compositions according to the invention. In a further preferred embodiment of the agent, a crystalline sodium layered silicate with a modulus of 2 to 3, as it can be made of sand and soda. Crystalline sodium silicates with a modulus in the range of 1, 9-3.5 are used in another preferred embodiment of the agent. Crystalline layered silicates corresponding to the above formula (I) Clariant GmbH of the Fa. Sold under the trade name Na-SKS, for example Na-SKS-1 (Na 2 Si 22 O 45 XH 2 O, kenyaite), Na-SKS-2 (Na 2 Sh 4 O 29 XH 2 O, magadiite), Na-SKS-3 (Na 2 Si 8 Oi 7 XH 2 O) or Na-SKS-4 (Na 2 Si 4 O 9 XH 2 O, makatite). Of these, especially Na-SKS-5 are (OC-Na 2 Si 2 O 5), Na-SKS-7 (.beta.-Na 2 Si 2 0 5, natrosilite), Na-SKS-9 (NaHSi 2 O 5 3H 2 O), Na-SKS-10 (NaHSi 2 O 5 3H 2 O, kanemite), Na-SKS-11 (t-Na 2 Si 2 0 5) and Na-SKS-13 (NaHSi 2 O 5), but in particular Na SKS-6 (5-Na 2 Si 2 O 5). In a preferred embodiment of an agent according to the invention, a granular compound of crystalline layered silicate and citrate, of crystalline layered silicate and the above-mentioned (co) polymeric polycarboxylic acid or alkali metal silicate and alkali metal carbonate, for example, under the name Nabion® as 15 is commercially available. Builders are in the compositions preferably in amounts up to 75 wt .-%, containing in particular 5% by weight to 50th

When for use in the inventive compositions suitable peroxygen compounds especially organic peracids or peracid salts of organic acids such as phthalimidopercaproic, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and under the washing conditions release hydrogen peroxide inorganic salts, including perborate, percarbonate, persilicate and / or persulfate such as Caroat® belong, into consideration. If solid peroxygen compounds are to be used, they can be used in the form of powders or granules, the manner known in principle can also be encapsulated. If a composition comprises peroxygen compounds, they are present in amounts of preferably up to 50 wt .-%, particularly 5 wt .-% to 30 wt .-%, yet. The addition of small amounts of known bleach stabilizers, for example phosphonates, borates or metaborate and Metasili- skating as well as magnesium salts such as magnesium sulfate, may be appropriate.

Suitable bleach activators are compounds which, under perhydrolysis conditions produce aliphatic peroxocarboxylic acids preferably containing 1 to 10 carbon atoms, especially 2 to 4 carbon atoms, and / or optionally substituted perbenzoic acid, can be used. Suitable substances which carry O- and / or N-acyl groups of said number of carbon atoms and / or optionally substituted benzoyl groups. Preference is given to polyacylated alkylenediamines, especially tetraacetylethylenediamine (TAED), acylated triazine derivatives, especially 1, 5-diacetyl-2,4-dioxohexahydro-1, 3,5-triazine (DADHT), acylated glycolurils, in particular tetraacetylglycoluril (TAGU), N- acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenol sulfonates, more particularly n- nonanoyl or isononanoyloxybenzenesulfonate (n- or iso-NOBS), carboxylic anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, especially triacetin, ethylene glycol diacetate, 2,5-diacetoxy 2,5-dihydrofuran and the enol esters and acetylated sorbitol and mannitol and the described mixtures (SORMAN), acylated sugar derivatives, especially pentaacetylglucose (PAG), pentaacetyl fructose, tetraacetyl xylose and octaacetyl lactose and acetylated, optionally N-alkylated glucamine and gluconolactone, and / or N acylated lactams, for example N-benzoyl caprolactam. The hydrophilically substituted acyl acetals and the acyl lactams are also preferably used. Combinations of conventional bleach activators may be used. Such bleach activators, especially in the presence of the above-mentioned hydrogen peroxide releasing bleaching agent, in the usual quantities, preferably all the in amounts of 0.5 wt .-% to 10 wt .-%, particularly 1 wt .-% to 8 wt .-%, based means, be present, but absent when percarboxylic acid as the sole bleaching agent preferably entirely. In addition to the conventional bleach activators or instead of them, sulfone and / or bleach-boosting transition metal salts or transition metal complexes may be present as so-called bleach catalysts. To the invention in the compositions, especially when they are present in liquid or paste form, be used in addition to water organic solvents include alcohols having 1 to 4 carbon atoms, especially methanol, ethanol, isopropanol and tert-butanol, diols having from 2 to 4 C -atoms, especially ethylene glycol and propylene glycol, and mixtures thereof and the derivable from the aforesaid compound classes ether. Such water-miscible solvents are present in the compositions preferably in amounts not exceeding 30 wt .-%, particularly 6 wt .-% to 20 wt .-%, yet.

To establish a desired, is not self-resultant pH may be prepared by mixing the other components of the central system and environmentally safe acids, particularly citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid and / or adipic acid, mineral acids, especially sulfuric acid, or bases, particularly ammonium or alkali metal hydroxides. Such pH regulators are present in the compositions in amounts of preferably not more than 20 wt .-%, in particular 1, 2 wt .-% to 17 wt .-%, of.

Graying inhibitors have the task of keeping suspended detached from the textile fiber dirt in the fleet. Water-soluble colloids usually of an organic nature are suitable, for example starch, glue, gelatin, salts of ether carboxylic acids or ether sulfonic acids of starch or cellulose or salts of acidic Schwefelsäureestern of cellulose or starch. Water-soluble polyamides containing acid groups are suitable for this purpose. Furthermore, other than the abovementioned starch derivatives can be used, for example aldehyde. Preferred are cellulose ethers such as carboxymethyl cellulose (Na salt), methyl cellulose, hydroxyalkyl cellulose, and mixed ethers, such as methylhydroxyethylcellulose, methylhydroxypropylcellulose, methyl carboxymethyl cellulose and mixtures thereof, for example, in amounts of from 0.1 to 5 wt .-%, based on the agent.

Laundry detergents may contain, for example, derivatives of diaminostilbene disulfonic acid or alkali metal salts, although they are preferably free of optical brighteners for use as color detergents as an optical brightener. Suitable are, for example, salts of 4,4'-bis (2-anilino- 4-morpholino-1, 3,5-triazinyl-6-amino) stilbene-2,2'-disulfonic acid or compounds of similar structure, instead of the morpholino group a diethanolamino, a methylamino group, an anilino group or a 2-methoxyethylamino carry. Brighteners of the substituted diphenyl styryl type, for example alkali metal salts of 4,4'-bis (2-sulfostyryl) - diphenyl, 4,4'-bis (4-chloro-3-sulfostyryl) or 4 - (4-chlorostyryl) -4 '- (2-sulfostyryl). Mixtures of the above-mentioned optical brighteners may be used.

For thickening, the agent may be one or more polymeric thickening agents. Polymeric thickeners are the polyelectrolytes as thickening polycarboxylates, preferably homo- and copolymers of acrylic acid, especially acrylic acid copolymers such as acrylic methacrylic acid copolymers, and the polysaccharides, in particular heteropolysaccharides, and other conventional thickening polymers. Suitable polysaccharides and heteropolysaccharides are the polysaccharide gums, for example gum arabic, agar, alginates, carrageenans and their salts, guar, guaran, tragacanth, gellan, Ramsan, dextran or xanthan and their derivatives, for example, propoxylated guar, and mixtures thereof. Other polysaccharide thickeners such as starches or cellulose derivatives, may alternatively, but are preferably used in addition to a polysaccharide gum, for example, starches of various origins and starch derivatives, for example hydroxyethyl, Stärkephosphatester or starch acetates, or carboxymethyl cellulose or its sodium salt, methyl, ethyl, hydroxyethyl, hydroxypropyl, hydroxypropyl-methyl or hydroxyethyl methyl cellulose or cellulose acetate. A preferred polymeric thickener is the microbial anionic heteropolysaccharide xanthan gum, which is produced by Xanthomonas campestris and some other species under aerobic conditions with a molecular weight of 2-15x106 and for example, by Fa. Kelco under the tradename Keltrol®, for example, as a cream Keltrol® powder T (transparent) or the white granules Keltrol® RD (Readily Dispersable). When polymeric thickeners suitable acrylic acid polymers are, for example, also high molecular weight with a polyalkenyl polyether, in particular an allyl ether of sucrose, pentaerythritol, or propylene, crosslinked homopolymers of acrylic acid (INCI Carbomer), which are also known as carboxyvinyl polymers. Such polyacrylic acids are obtainable inter alia from Fa. BFGoodrich under the tradename Carbopol, such as Carbopol 940 (molecular weight about 4,000,000), Carbopol 941 (molecular weight approximately 1,250,000) or Carbopol 934 (molecular weight approximately 3,000. 000). The content of the polymeric thickener is usually not more than 8 wt .-%, preferably between 0.1 and 7 wt .-%, particularly preferably between 0.5 and 6 wt .-%, especially between 1 and 5% by weight and most preferably between 1, 5 and 4 wt .-%, for example between 2 and 2.5 wt .-%.

The ingredients of the inventive composition to be chosen as well as the conditions under which it is used according to the invention, such as temperature, pH, ionic strength, redox conditions or mechanical influences, are usually optimized for the particular application.

Among the solid dosage forms of an agent of the invention include, in particular extrudates, granules, tablets or pouches, which may also be packed in portions both in bulk as well. Alternatively, the agent is present as a free-flowing powder, in particular having a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l. Further, agents of the invention may also be liquid, gel or paste form, in particular it könenn be in the form of a non-aqueous liquid detergent or a non-aqueous paste or in the form of an aqueous liquid detergent or a water-containing paste. An inventive washing or cleaning agent may further in a container, preferably be packed in an air-permeable container from which it is released shortly before use or during the washing process. In particular, the protease contained in the agent and / or other ingredients of the composition may be coated with a room temperature or in the absence of water for the enzyme impermeable substance which is permeable to the enzyme under application conditions of the agent. Such an embodiment of the invention is thus characterized in that the protease is coated with an impermeable at room temperature or in the absence of water for the protease substance.

Agents of the invention can contain only one protease as described. Alternatively, however, they can also contain other proteases or other enzymes in an expedient for the effectiveness of the agent concentration. A further subject of the invention thus provides a detergent or cleaning agent is, which is characterized in that it comprises at least one further enzyme, especially a protease, amylase, cellulase, carbohydrase, hemicellulase, mannanase, xylanase, pectinase, beta-glucosidase, Carrageenase , thereof lipase, oxidase, oxidoreductase, or combinations, in principle any known in the art for this purpose enzymes can be used. The enzymes may be adsorbed onto supports and / or encapsulated in membrane materials to protect them against premature inactivation. They are in the inventive detergents or cleaning agents, preferably in amounts of 1 x 10 -8 to 5 percent by weight based on active protein (dry matter) contained. the enzymes from 0.001 to 5 wt .-%, more preferably from 0.01 to 5 wt .-%, even more preferably from 0.05 to 4 wt .-% and particularly preferably 0.075 to 3.5 by weight are preferred. -% included, each enzyme may be contained in the above amount. In liquid compositions the weight of the liquid agent is determined so that the data are based on weight and enzyme weight average. If several enzymes are used in the inventive composition, these can be present separately or packaged together in the composition, for example as granules, or as individual granules which contain at least two different enzymes.

The protein concentration can be determined using known methods, for example the BCA method (bicinchonic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method (Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp 751-766) are determined. The protease activity in such compositions S. method described can 125-132 after in surfactants, Volume 7 (1970), are determined. It is given in PU (protease units).

Particularly preferably, the enzymes exhibit synergistic effects in terms of their effect against certain stains or spots, ie the enzymes contained in the composition assist in their cleaning performance each other. Very particularly preferably, such synergism is present between the protease according to the invention contained, and a further enzyme of an inventive agent, including, in particular between the protease according to the invention contained and a further protease and / or amylase and / or a mannanase and / or a lipase. Examples of proteases are the subtilisins BPN 'from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, protease PB92, subtilisins 147 and 309, the protease from Bacillus lentus subtilisin DY and the subtilases, but not more subtilisins in the strict sense as enzymes thermitase, proteinase K and proteases TW3 and TW7. Subtilisin Carlsberg in further developed form under the trade name Alcalase by the company Novozymes A / S, Bagsvaerd, Denmark. The subtilisins 147 and 309 are under the trade names Esperase, or sold Savinase.RTM by the company Novozymes. Of the protease from Bacillus lentus DSM 5483 protease BLAP® listed under the name variants derive. Further useable proteases are, for example, under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase® and Ovozyme® by the company Novozymes, the Prime under the trade names Purafect, Purafect OxP, Purafect Excellase® and Properase® by the company Danisco / Genencor, that under the trade name Protosol® by the company Advanced Biochemicals Ltd., Thane, India, that the under the trade name Wuxi® by the company Wuxi Snyder Bioproducts Ltd., China, under trade names Proleather® and protease P® by the company Amano Pharmaceuticals Ltd., Nagoya, Japan, and the enzymes available under the name proteinase K-16 by the company Kao Corp., Tokyo, Japan. the proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in the international patent applications WO 08/086916 and WO 07/131656 are particularly preferably used. Other proteases can be used advantageously are disclosed in the patent applications WO 91/02792, WO 08/007319, WO 93/18140, WO 01/44452, GB 1243784, WO 96/34946, WO 02/029024 and WO 03/057246. Other useful proteases are those sphaericus are naturally present in the microorganisms Stenotrophomonas maltophilia, in particular Stenotrophomonas maltophilia K279a, Bacillus intermedius and Bacillus.

Examples of amylases are the α-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens or Bacillus stearothermophilus, and in particular their improved for use in washing or cleaning compositions. The enzyme from Bacillus licheniformis is available from the company Novozymes under the name Termamyl and by the company Danisco / Genencor under the name Purastar®ST. Development products of this α-amylase are available from the company Novozymes under the trade names Duramyl.RTM and Termamyl®ultra, by the company Danisco / Genencor under the name Purastar®OxAm and by the company Daiwa Seiko Inc., Tokyo, Japan, as Keistase®. The α-amylase from Bacillus amyloliquefaciens is marketed by the company Novozymes under the name BAN®, and derived variants from the α- amylase from Bacillus stearothermophilus under the names BSG® and Novamyl®, also from the company Novozymes. Furthermore, the α-amylase from Bacillus sp for this purpose. A 7-7 (DSM 12368), and the cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) emphasized. Furthermore, the amylolytic enzymes can be used which are disclosed in the international patent applications WO 03/002711, WO 03/054177 and WO07 / 079,938th Similarly, fusion products of all said molecules can be used. Moreover, further developments of α-amylase sold under the trade names Fungamyl® by the company Novozymes from Aspergillus niger and A. oryzae, which are. Further commercial products are for example the Amylase-LT® and Stainzyme® or Stainzyme® ultra® or plus® Stainzyme®, the latter also from the company Novozymes. Also available by point mutations variants of these enzymes can be used according to the invention.

An example of a cellulase (endoglucanases, EG) is the fungal endoglucanase (EG) -rich cellulase preparation and developments thereof, which is offered by the company Novozymes under the trade name Celluzyme®. The products Endolase® and Carezyme® also available from the company Novozymes based on the 50 kD EG and 43 kD EG from Humicola insolens DSM 1800. Further commercial products of this company are Cellusoft®, Renozyme® and Celluclean®. are still used, for example the 20 kD EG Melanocarpus that are available from the company AB Enzymes, Finland, under the trade names Ecostone® and Biotouch®. Other commercial products the company AB Enzymes are Econase® and Ecopulp®. Other suitable cellulases are from Bacillus sp. CBS 670.93 and CBS 669.93, the Bacillus sp. CBS is available under the trade name Puradax® 670.93 by the company Danisco / Genencor. Other commercial products the company Danisco / Genencor are "Genencor detergent cellulase L" and lndiAge®Neutra.

Further preferred hydrolytic enzymes are those which under the term glycosidases (EC 3.2.1.X) are summarized. These include in particular arabinases, fucosidases, galactosidases, galactanases, Arabico galactan galactosidases, mannanases (also referred to as mannosidases or mannanases), Glucuronosidasen, agarase Carrageenasen, pullulanases, beta-glucosidases, xyloglucanases (xylanases) and pectin-degrading enzymes (pectinases ). Preferred Gylcosidasen be summarized under the term hemicellulases. To hemicellulases include, in particular, mannanases, xyloglucanases (xylanases), beta-glucosidases and Carrageenasen and further pectinases, pullulanases and beta-glucanases.

Pectinases are pectin-degrading enzymes, wherein the hydrolytic pectin-degrading enzymes are, in particular belonging to the enzyme classes EC 3.1.1.11, EC 3.2.1.15, EC 3.2.1.67 and EC 3.2.1.82. Other names for this are pectin esterase, Pectindemethoxylase, Pectinmethoxylase, pectin methylesterase, pectase, pectin methylesterase, Pectinoesterase, Pectinpectylhydrolase, Pectindepolymerase, endopolygalacturonase, Pectolase, Pectinhydrolase, pectin polygalacturonase, endo-polygalacturonase, poly-α-1, 4-galacturonide Glycanohydrolase, Endogalacturonase, Endo D- galacturonase, Galacturan 1, 4-α-Galacturonidase, Exopolygalacturonase, poly (galacturonate) hydrolase, exo-D-Galacturonase, exo-D-Galacturonanase, exopoly-D-Galacturonase, exopoly-α- Galacturonosidase, or Exopolygalacturonosidase Exopolygalacturanosidase. In this regard, suitable enzymes are, for example, under the name Gamanase® and Pektinex AR® by the company Novozymes under the name Rohapec® B1 L from the company AB Enzymes and under the name Pyrolase® by the company Diversa Corp., San Diego, CA, USA available. The recovered from Bacillus subtilis beta-glucanase is available under the name Cereflo® by the company Novozymes. According to the invention particularly preferred glycosidases or hemicellulases are mannanases, which are marketed under the trade names Mannaway® by the company Novozymes or Purabrite® by the company Danisco / Genencor.

Examples of lipases or cutinases are originally from Humicola lanuginosa (Thermomyces lanuginosus) or further developed from lipases, in particular those with the D96L amino acid substitution. They are sold, for example, by the company Novozymes under the trade names Lipolase, Lipolase®Ultra, LipoPrime®, Lipozyme® and Lipex®. Furthermore, the cutinases are for example used, which were originally isolated from Fusarium solani pisi insolens and Humicola. Likewise useable lipases are available from the company Amano under the designations Lipase CE ®, Lipase P®, Lipase B®, or lipase CES®, lipase AKG®, Bacillis sp. Lipase, lipase AP®, lipase M-AP® and lipase AML® available. By the company Danisco / Genencor, for example, the lipases and cutinases are used are those whose starting enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii. Other important commercial products are originally from the company Gist-Brocades (now Danisco / Genencor) marketed preparations M1 Lipase and Lipomax® and OF® by the company Meito Sangyo KK, Japan under the names Lipase MY-30®, Lipase to mention and lipase PL®, and also the product Lumafast® by the company Danisco / Genencor.

To enhance the bleaching effect agent of the invention can also be oxidoreductases, such as oxidases, oxygenases, catalases (that react at low H 2 O 2 concentrations as peroxidase), peroxidases such as halo-, chloro-, bromo-, lignin, glucose or peroxidases, laccases or dioxygenases (phenol oxidases, polyphenol oxidases) included. Suitable commercial products Denilite® be mentioned 1 and 2 from Novozymes. As used advantageously as systems for enzymatic perhydrolysis referenced applications WO 98/45398 A1, WO 2005/056782 A2 and WO 2004/058961 A1. A combined enzymatic bleach system comprising an oxidase and a perhydrolase describes the application WO 2005/124012.

Among all these enzymes, particularly preferred are those which are relatively stable in themselves to oxidation or for example by mutations, in particular by substitution, deletion or insertion of one or more amino acids have been stabilized. For this purpose, the aforementioned commercial products Everlase and Purafect® OxP are particular to cite as examples of such proteases and Duramyl as an example of such an α-amylase. The enzymes used in the invention preferably originate from microorganisms such as the genera Bacillus, Streptomyces, Humicola or Pseudomonas, and / or are produced according to known biotechnological processes using suitable microorganisms such as by transgenic expression hosts of the genera Bacillus or filamentous fungi. It is stressed in particular that it may be technical enzyme preparations of each enzyme hydrolytic also, that impurities may be present. Therefore, the enzymes may be formulated and used together with accompanying substances, such as from the fermentation or stabilizers.

In Table 1 formulations for inventive detergents and cleaning agents are given. Each formulation in this case comprises a protease from said bacterium, and at least the detergent ingredient stated in each case in said amount range.

Table 1 :

Figure imgf000019_0001

Figure imgf000020_0001

All formulations shown in Table 1 may include one or more additional detergent ingredients. For example, in the following Table 2, the formulations of Table 1 as a basic formulas marked with a each additionally present in the respective base formulation detergent ingredient in the stated amount. In this case, each base formulation with each ingredient, a further, independent formulation. For example, the formula 1 with an organic solvent (particularly alcohol), with an acid, with an optical brightener and an anti-redeposition agent as four independent Eizelrezepturen are to be understood.

Table 2:

Figure imgf000020_0002
Figure imgf000021_0001
Figure imgf000022_0001
Figure imgf000023_0001

Figure imgf000024_0001

A separate subject invention provides the use of an inventive detergent or cleaning agent to remove soils, particularly protease-sensitive stains on textiles or hard surfaces, ie for cleaning textiles or hard surfaces. Because, agents according to the invention, in particular due the above-described properties of the protease contained, be advantageously used to remove from fabrics or hard surfaces corresponding impurities. Embodiments of this inventive object provide for example the hand laundering, manual removal of stains from textiles or hard surfaces or the use in connection with a machine method. All facts, subjects and embodiments described for inventive washing or cleaning agents, are also on apply this inventive subject matter. Therefore, reference is expressly made at this point to the disclosure at the appropriate point by pointing out that this disclosure also applies to the above inventive use. In preferred embodiments of this use, the washing or cleaning agent in question according to the invention are provided by one of the above-described embodiments.

A further subject of the invention is a method for cleaning textiles or hard surfaces, which is characterized in that in at least one process step, a washing or cleaning agent according to the invention is applied. These include both manual and automatic methods, wherein automatic methods due to their precise controllability with regard, for example, the amounts and reaction times used, preferred. A process for cleaning textiles or hard surfaces are generally distinguished by the fact that in several process steps, various cleaning-active substances are applied to the cleaned and washed after the contact time, or that the items to be cleaned in any other way with a detergent or a solution or dilution of this by means treated. All conceivable washing or cleaning methods can be enriched by the application of an inventive washing or cleaning agent in at least one of the process steps and then represent embodiments of the present invention. All facts, objects and embodiments are described for the inventive detergents or cleaning agents, are applicable to this subject invention. Therefore, reference is expressly made at this point to the disclosure at the appropriate point by pointing out that this disclosure also applies to the above process according to the invention.

Another object of the invention is a protease, which is characterized in that it is naturally present in a bacterium of the genus Xanthomonas and it has a Proteolyseindex of at least 1 1 in an aqueous solution in the presence of at least one surfactant. The surfactant may be a surfactant. With increasing preference of at least Proteolyseindex has a value of 1, 2, 1, 3, 1, 4, 1, 5, 1, 6, 1, 7, 1, 8, 1, 9, 2.0, 2.1, 2 , 2, 2.3, 2.4, 2.5, 2.6, 2.7, 2.8, 2.9, 3.0, 3.25, 3.5, 3.75, 4.0 , 4.25, 4.5, 4.75 and 5.0 in. This Proteolyseindex is determined by standardized soiled fabrics which can be obtained from the Swiss Federal Material Audit and -Versuchsanstalt, St. Gallen, Switzerland (EMPA) or the Center For Test Materials BV, Vlaardingen, Netherlands. For the index determination one of the following stains is to use: A (grass on cotton, EMPA 164), B (whole egg / soot on cotton, 10N), C (blood / milk / ink on cotton, C-05). This test material with the surfactant-containing solution, preferably a dissolved detergent, that is, a wash liquor, washed for 60 minutes at a temperature of 4O 0 C, in the presence and absence of the respective protease. To determine the Proteolyseindex various detergent formulations can be used in principle, primary importance is the presence of a surfactant. The detergent or surfactant solution may, but need not necessarily contain bleach. The water to be used is tap water having a water hardness of about 16 ° German hardness. A particularly suitable detergent formulation is composed as follows (all figures in percentage weight): 10% linear alkyl benzene sulphonate (sodium salt), 1, 5% C12-C18-fatty alcohol sulfate (sodium salt), 2.0% C12-C18 fatty alcohol with 7 EO, 20% sodium carbonate, 6.5% sodium bicarbonate, 4.0% amorphous sodium disilicate, 17% sodium carbonate peroxohydrate, 4.0% TAED, 3.0% polyacrylate, 1, 0% carboxymethylcellulose, 1, 0% phosphonate, 25% sodium sulfate, rest: foam inhibitors, optical brighteners, perfumes, optionally water.. Their dosage is 5.9 g of the detergent per liter wash liquor.

Preferably, the surfactant or surfactant mixture selected from the above-described surfactants. The surfactant is contained in an amount of at least 0.5 g / l and preferably of at least 0.75 g / l in the solution. The measurement of the whiteness is performed on a previously calibrated with a white standard spectrometer in a conventional way familiar to the expert. The Proteolyseindex is then defined as the quotient of the measured value of the whiteness of the surfactant-containing solution with a protease from Xanthomonas and the measured value of the whiteness of the surfactant solution without an inventive protease from Xanthomonas over a pH value range of at least 0.5, and increasingly preferably from 0.75, 1, 1, 25, 1, 5, 1, 75 and 2 pH units. Preferably, this pH range is located in a neutral or alkaline pH range, ie, the smallest pH in this pH range is therefore greater than or equal to pH 7. The Proteolyseindex expresses that a protease of the invention over a larger pH range a corresponding cleaning performance, ie catalytic performance, yields, making them particularly advantageous for use in detergents and cleaners.

In a preferred embodiment of this subject invention, the protease is naturally in a bacterium present, which is selected from the group consisting of Xanthomonas albilineans, Xanthomonas alfalfae, Xanthomonas alfalfae subsp. alfalfae, Xanthomonas alfalfae subsp. citrumelonis, Xanthomonas ampelina (Xylophilus ampelinus), Xanthomonas arboricola, Xanthomonas axonopodis Xanthomonas bromi, Xanthomonas campestris, Xanthomonas cassavae, Xanthomonas citri, Xanthomonas citri subsp. citri, Xanthomonas citri subsp. malvacearum, Xanthomonas codiaei, Xanthomonas Cucurbitae, Xanthomonas Cynarae, Xanthomonas euvesicatoria, Xanthomonas fragariae, Xanthomonas fuscans, Xanthomonas fuscans subsp. aurantifolii, Xanthomonas fuscans subsp. fuscans, Xanthomonas gardneri, Xanthomonas hortorum, Xanthomonas hyacinthi, Xanthomonas melonis, Xanthomonas oryzae, Xanthomonas perforans, Xanthomonas phaseoli, Xanthomonas pisi, Xanthomonas populi, Xanthomonas sacchari, Xanthomonas theicola, Xanthomonas translucens, Xanthomonas vasicola, Xanthomonas vesicatoria. Particularly preferably, the protease is naturally present in a bacterium, which is selected from the group consisting of Xanthomonas axonopodis DSM 3585, Xanthomonas axonopodis pvar. DSM 50850 begoniae, Xanthomonas axonopodis pvar. pvar malvacearum DSM 1220 Xanthomonas campestris DSM 1050 (NCPPB 1929), Xanthomonas campestris DSM 19000, Xanthomonas campestris. campestris DSM 3586, Xanthomonas campestris pvar. pelargonii DSM 50,857th In a further embodiment, it is not the protease to the proteases PRT1 and PRT2 (from Xanthomonas campestris according to Dow et al., Applied and Environmental Microbiology, 1990, 2994 to 2998 and Dow et al., Applied and Environmental Microbiology , 1993, 3996- 4003) and not the protease from Xanthomonas sp. YL-37 (according to Chang-Ho Lee et al., Jour. Microbiol. 1995, 115-119).

Another object of the invention is a nucleic acid encoding a protease according to the invention as well as a vector containing such a nucleic acid. Nucleic acids are understood to be naturally composed of nucleotides as an information carrier serving molecules in the context of the present application, which code for the linear amino acid sequence in proteins or enzymes. It may be DNA or RNA, each as a single strand can be used as a present to single strand complementary single strand or a double strand. In particular, the DNA sequences of both complementary strands are to be considered in all three possible reading frames. Further, it should be noted that different codon triplets can code for the same amino acids, so that a particular amino acid sequence of several different and may only have low identity Nucleotide sequences may be derived which is called degeneracy of the genetic code. For these reasons, both amino acid sequences and nucleotide sequences must be included in the scope of protection. Therefore, all nucleotide sequences are included in the invention, which can encode an above-described enzyme. The expert is able to determine these nucleotide sequences with certainty as defined in spite of the degeneracy of the genetic code, individual codons amino acids are attributable. One skilled in the art is it about nowadays generally known methods such as chemical synthesis or the polymerase chain reaction (PCR) in conjunction with molecular-biological and / or protein-chemical standard methods, to produce the corresponding nucleic acids on the basis of known DNA and / or amino acid sequences. Such methods are for example, Sambrook, J., Fritsch, EF and Maniatis, T. (2001, Molecular cloning: a laboratory manual, 3rd Edition Cold Spring Laboratory Press.) Known.

Vectors of the present invention will be understood from existing elements within the meaning nucleic acids which contain, as characteristic nucleic acid region of a nucleic acid according to the invention. They are able to establish this as a stable genetic element in a species or a cell line over several generations or cell divisions. Vectors are special plasmids, in particular for use in bacteria, ie circular genetic elements. In the present invention, the nucleic acid is suitably cloned in a vector. Vectors can be derived from bacterial plasmids, from viruses or from bacteriophages or predominantly synthetic vectors or plasmids with elements verschiedenster origin. With the further each existing genetic elements vectors to establish themselves in host cells over several generations as stable units. It is irrelevant for the purposes of the invention, whether they establish themselves extrachromosomally as independent units or integrated into a chromosome. The choice of a vector is carried out, for example, on the basis of achievable copy number of the available selection systems, including particularly antibiotic resistance, or based on the culturability of host cells into which the vector is to be introduced.

Preferably, the vector is an expression vector. Expression vectors are capable of replicating in the host cells or host organisms and the nucleic acid contained therein, for example, as a transgene, in order to express. Preferred embodiments are expression vectors which themselves carry the genetic elements necessary for expression. Expression is influenced, for example, by promoters which regulate the transcription of the nucleic acid. Thus, expression can take place by the natural, original localized before to be expressed, the nucleic acid promoter but also by genetic fusion both through a provided on the expression vector promoter of the host cell and by a modified, or an entirely different promoter of another organism, or other host cell , In particular, expression vectors can be regulated. For example, by controlled addition of chemical compounds serving as activators, by changing the culturing conditions of the host cells, they contained in or on reaching a certain cell density, the host cells they contained this can be induced for expression. This allows efficient production of proteins of the invention. An example of such a chemical compound is the galactose derivative isopropyl-ß-D-thiogalactopyranoside (IPTG), which is used as an activator of the bacterial lactose operon (lac operon). Expression vectors enable the associated protein can be produced in or by a host cell. These in vivo synthesis of an enzyme according to the invention, ie by living cells requires the transfer of an appropriate vector into a host cell, the so-called transformation. The host cells may well be associated with different organisms or from different organisms. Also, a homologous protein extraction from a nucleic acid naturally expressing host cell via an appropriate vector is within the scope of the present invention. This may have the advantage that natural, standing in connection with a translational modification reactions are carried out on the resulting protein as much as they would take place naturally.

Another object of the invention is thus a non-human host cell, which includes a protease of the invention or a fragment thereof, or comprises a nucleic acid of the invention or which contains a vector according to the invention, especially one having a nucleus or one that is a bacterium. Suitable host cells are in principle all cells are suitable, that is prokaryotic or eukaryotic cells. Such host cells can be genetically handled advantageous as regards for example, transformation with the expression vector and its stable establishment, such as unicellular fungi or bacteria. In particular, those host cells are preferred, which are characterized in that they are obtained after transformation with one of the vectors described above. Preferred embodiments are those host cells which are adjustable due to genetic regulatory elements which are made for example in the expression vector are available, but also may be present from the outset in these cells in their activity. The host cells may be altered to the culture conditions with respect to their requirements, have other or additional selection marker or express other or additional proteins. It can be, in particular those host cells which express in addition to the inventively produced protein further, particularly economically interesting proteins.

Preferred host cells are prokaryotic or bacterial cells. Bacteria are distinguished from eukaryotes usually by shorter generation times and less demanding cultivation conditions from. This cost-effective method for obtaining proteins of the invention can be established. In gram-negative bacteria such as Escherichia coli (E. coli), a large number of proteins are secreted into the periplasmic space, ie into the compartment between the two membranes, the cells inclusive. This can be advantageous for particular applications. Gram-positive bacteria such as bacilli or actinomycetes or other representatives of Actinomycetales, in contrast, have no outer membrane so that secreted proteins into the culture medium surrounding the cells are delivered, from which the expressed proteins according to the invention can be purified directly. Preferably, said host cell secreted protein of the invention in the surrounding medium.

In a preferred embodiment, the host cell of the invention is characterized in that it is a bacterium, in particular one which is selected from a) the group of genera of Escherichia, Bacillus, and Arthrobacter, Streptomyces, Stenotrophomonas, Xanthomonas and Pseudomonas, or b) the group of Escherichia coli, Bacillus licheniformis, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus alcalophilus and Arthrobacter oxidans, Streptomyces lividans, Streptomyces coelicolor and Stenotrophomonas maltophilia.

Particularly suitable host cells are bacteria of the genus Xanthomonas, and most preferably including a referred to in Table 1 Xanthomonas-type or a named in Table 1 Xanthomonas strain.

However, the host cell may be a eukaryotic cell, which is characterized in that it possesses a nucleus. In contrast to prokaryotic cells, eukaryotic cells are able to modify posttranslationally the protein produced. Examples include fungi such as actinomycetes or yeasts such as Saccharomyces or Kluyveromyces. This can for example be particularly advantageous if the proteins in connection with their synthesis to learn specific modifications which enable such systems. These include the binding of small molecules such as membrane anchors or oligosaccharides.

The host cells according to the invention are cultured in a conventional manner and fermented, for example in batch or continuous systems. In the first case a suitable nutrient medium with the host cell is inoculated and harvested the product after a period of time to be determined experimentally from the medium. Continuous fermentations are characterized by attainment of a steady state in which, over a comparatively long period of time cells partially die but also grow and at the same product from the medium can be removed. Here, typically, the media components to be consumed by the continuous cultivation are fed, whereby increases are achieved in both of the cell density, and also in the dry biomass and / or especially the activity of the protein of interest. Further, the fermentation can also be designed so that unwanted metabolic products filtered out or be neutralized by the addition of buffer or matching counter ions.

Another object of the invention is thus a process for the preparation of a protease according to the invention. In principle, this includes any method that is suitable for the production of a protease invention described above or which allows to obtain a protease of the invention. These include, in principle, chemical synthesis methods. However, fermentative production method involving as process step culturing a host cell of the invention are preferred. Therefore, the process steps a) according to the invention preferred method for producing a protease comprising culturing a host cell b) isolating the protease from the cultured host cells and / or from the surrounding host cells medium c) optionally purifying the isolated protease of the invention.

Another object of the invention is a method for cleaning textiles or hard surfaces, which is characterized in that a protease of the invention is catalytically active in at least one method step, in particular in such a way that the protease in an amount of 40 micrograms to 4 g, preferably is inserted from 50 micrograms to 3 g, particularly preferably from 100 micrograms to 2 g and very particularly preferably from 200 .mu.g to 1 g per application. A further object of this invention is the use of a protease according to the invention for cleaning textiles or hard surfaces. the protease in this application in an amount of 40 micrograms to 4 g preferably is used preferably from 50 micrograms to 3 g, particularly preferably from 100 micrograms to 2 g and more preferably from 200 .mu.g to 1 g.

Examples:

Example 1: Cultivation of the strains and screening for proteases

Culturing of the bacteria of the genus Xanthomonas was carried out in nutrient broth medium (peptone 5.0 g / 1 meat extract and 3.0 g / 1) overnight at 3O 0 C with shaking at 180 revolutions per minute. The bacteria thus obtained were powdered milk containing agar plates (peptone 5.0 g / 1 meat extract and 3.0 g / 1 agar and 15.0 g / l and 2% skimmed milk powder) were plated and 48 hours at 3O 0 C. Based on a clearance Court (Lysehof) about the respective bacterial colony to a proteolytic activity of the bacteria showed. They were cultured again so that the culture medium containing the bacteria formed by the protease and thus a proteolytic activity. In this manner, the proteolytic activity of bacteria of the Xanthomonas strains Xanthomonas axonopodis DSM 3585, Xanthomonas axonopodis was pvar. DSM 50850 begoniae, Xanthomonas axonopodis pvar. pvar malvacearum DSM 1220 Xanthomonas campestris DSM 1050 (NCPPB 1929), Xanthomonas campestris DSM 19000, Xanthomonas campestris. campestris DSM 3586 and Xanthomonas campestris pvar. pelargonii DSM obtained 50,857th

Example 2: Determination of the cleaning performance at 3O 0 C

Were used standardized soiled fabrics with a blood / milk / ink soiling (C-05, Center For Test Materials BV, Vlaardingen, The Netherlands). This test material, various detergent formulations that differed by each contained protease were tested for their cleaning performance down. For this, the approaches for 60 minutes at a temperature of 3O 0 C were washed. The dosage was 5.9 g of detergent per liter wash liquor. It was with tap water having a water hardness of 16 ° German hardness (DH) is washed in a pH range between pH 8 and pH 9. The detergent formulation was composed as follows (all figures in percentage weight): 10% linear alkyl benzene sulfonate (sodium salt), 1, 5% C12-C18-fatty alcohol sulfate (sodium salt), 2.0% C12-C18 fatty alcohol with 7 EO, 20% sodium carbonate, 6.5% sodium bicarbonate, 4.0% amorphous sodium disilicate, 17% sodium carbonate peroxohydrate, 4.0% TAED, 3.0% polyacrylate, 1, 0% carboxymethylcellulose, 1, 0% phosphonate, 25% sodium sulfate, rest: foam inhibitors, optical brighteners, perfumes, water.

The detergent formulation were each mixed in equal amounts for the various series of tests to those given in Table 3 proteolytic activities from the Xanthomonas strains of Example. 1 The comparative formulation containing an established for detergents and according to WO 92/21760 performance-enhanced variant of the alkaline protease from Bacillus lentus DSM 5483 ( "Comparison"), which is not derived from a bacterium of the genus Xanthomonas. After washing, the absorbance of the wash liquor was (as a marker intended for dissolved from the textiles soil) at a wavelength of 650 nm. Further, the proteolytic activity of the protease preparation used in each case was determined. the result clearly shows that the detergent achieved with proteases from Xanthomonas despite lower employed proteolytic activity comparable or even better cleaning performance than the control. the compositions with the Xanthomonas proteases are therefore more powerful agents.

Table 3:

Figure imgf000031_0001

Example 3: Determination of the cleaning performance on 4O 0 C

Were used standardized soiled textiles, the Netherlands, had been obtained from the Swiss Federal Institute of materials testing and -Versuchsanstalt, St. Gallen, Switzerland (EMPA) or the Center For Test Materials BV, Vlaardingen. The following soilings and textiles were used: A (grass on cotton, EMPA 164), B (whole egg / soot on cotton, 10N), C (blood / milk / ink on cotton, C-05). This test material, various detergent formulations were prepared as described in Example 2, tested for their cleaning performance out with the exception that was washed at 4O 0 C. The detergent formulation was admixed for the various experimental series with identical activities with the various proteases from Xanthomonas strains. The protease activity employed was either 5 or 10 PU (protease units) per ml wash liquor. By comparison formulations procedure was the same, provided that these proteases contained. Comparison formulations containing either no protease or protease that is not derived from a bacterium of the genus Xanthomonas. After washing, the whiteness of the washed fabrics was, that is, the brightening of the stains measured. The measurement was performed on a spectrometer Minolta CM508d (illuminant D65, 10 °). The instrument has been calibrated with a white standard.

Again, the detergent with Xanthomonas proteases showed a high to very high cleaning performance to said stains, in particular on a pH value range of one pH unit. Accordingly, the proteases from Xanthomonas have a Proteolyseindex of at least 1. 1 This was determined as the quotient of the measuring results obtained in washing with a detergent containing a protease and a carried out in parallel control wash with detergent without protease.

Claims

claims
1. Washing or cleaning composition comprising a protease that is naturally present in a bacterium of the genus Xanthomonas and at least one other detergent ingredient.
2. Washing or cleaning composition according to claim 1, characterized in that the additional detergent ingredient is selected from the group consisting of builder, surfactant, surfactant, bleaching agent based on organic and / or inorganic peroxygen compounds, bleach activators, organic solvent, acid, graying inhibitor, optical brighteners, polymeric thickening agents and combinations thereof.
3. washing or cleaning agent according to any one of claims 1 or 2, characterized in that it is in solid form, especially as free-flowing powder having a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l, is present, or that it is in liquid, gel or paste form.
4. Washing or cleaning composition according to any one of claims 1 to 3, characterized in that the protease is coated with an at room temperature and / or in the absence of water for the protease impermeable substance.
5. Washing or cleaning composition according to any one of claims 1 to 4, characterized in that it comprises at least one further enzyme, especially a protease, amylase, cellulase, carbohydrase, hemicellulase, mannanase, xylanase, pectinase, beta-glucosidase, Carrageenase, lipase , thereof oxidase, oxidoreductase, or combinations thereof.
6. Use of a washing or cleaning agent according to one of claims 1 to 5 for the removal of protease sensitive stains on textiles or hard surfaces.
7. A process for cleaning textiles or hard surfaces, characterized in that in at least one process step, a washing or cleaning agent is applied according to one of claims 1 to. 5
8. protease, characterized in that it is present in a bacterium of the genus Xanthomonas and naturally it has a Proteolyseindex of at least 1 1 in an aqueous solution in the presence of at least one surfactant.
9. nucleic acid encoding a protease of claim 8.
10. A vector containing a nucleic acid according to claim. 9
11. Non-human host cell, which includes a protease according to claim 8 or a fragment thereof or which contains a nucleic acid according to claim 9 or incorporating a vector according to claim 10, in particular one having a nucleus or one that is a bacterium.
12. The host cell of claim 11, characterized in that it is a bacterium selected from a) the group of genera of Escherichia, Bacillus, and Arthrobacter, Streptomyces, Stenotrophomonas, Xanthomonas and Pseudomonas, or b) the group of Escherichia coli, Bacillus licheniformis, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus alcalophilus and Arthrobacter oxidans, Streptomyces lividans, Streptomyces coelicolor and Stenotrophomonas maltophilia.
13. A process for the preparation of a protease according to claim 8 comprising the steps of a) culturing a host cell according to any one of claims 11 or 12 b) isolating the protease from the cultured host cells and / or from the surrounding host cells medium c) optionally purifying the isolated protease
14. A process for cleaning textiles or hard surfaces, characterized in that a protease according to claim 8 is proteolytically active in at least one process step.
15. Use of a protease according to claim 8 for cleaning textiles or hard surfaces.
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Cited By (81)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2010146036A1 (en) 2009-06-19 2010-12-23 Henkel Ag & Co. Kgaa Novel proteases and means containing said proteases
WO2011110625A1 (en) 2010-03-11 2011-09-15 Henkel Ag & Co. Kgaa Performance-enhanced protease variant
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DE102016214383A1 (en) 2016-08-03 2018-02-08 Henkel Ag & Co. Kgaa Detergents containing keratinase
DE102016216014A1 (en) 2016-08-25 2018-03-01 Henkel Ag & Co. Kgaa Method for Evaluation of cellulases for fabric care
EP3299457A1 (en) 2016-09-26 2018-03-28 Henkel AG & Co. KGaA New lipase
EP3309249A1 (en) 2013-07-29 2018-04-18 Novozymes A/S Protease variants and polynucleotides encoding same
EP3321360A2 (en) 2013-01-03 2018-05-16 Novozymes A/S Alpha-amylase variants and polynucleotides encoding same

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH09299082A (en) * 1996-05-10 1997-11-25 Kao Corp Low-temperature alkali protease x, microorganism capable of producing the same, production of the same, and detergent composition containing the enzyme and enzyme preparation for food processing
WO2000029534A1 (en) * 1998-11-13 2000-05-25 Genencor International, Inc. Fluidized bed low density granule
US20020019325A1 (en) * 1998-03-27 2002-02-14 Hans Sejr Olsen Acidic cleaning composition comprising an acidic protease obtained from aspergillus aculeatus
US20070212706A1 (en) * 2004-04-23 2007-09-13 Susanne Wieland Novel alkaline proteases and detergents and cleaners comprising these novel alkaline proteases
DE102006042797A1 (en) * 2006-09-08 2008-03-27 Henkel Kgaa Enzyme granules with a high concentration of enzyme, especially e.g. alkaline protease or subtilisin types, useful in detergents and cleaning materials, especially tablets for washing machines and dishwashers

Family Cites Families (16)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE3723873A1 (en) 1987-07-18 1989-01-26 Henkel Kgaa Using hydroxyalkylpolyethylenglykolethern in klarspuelmitteln for machine dishwashing,
DK0493398T3 (en) 1989-08-25 2000-05-22 Henkel Research Corp Alkaline proteolytic enzyme and process for production thereof
US5340735A (en) 1991-05-29 1994-08-23 Cognis, Inc. Bacillus lentus alkaline protease variants with increased stability
DE19713852A1 (en) 1997-04-04 1998-10-08 Henkel Kgaa Activators for peroxygen compounds in detergents and cleaning agents
CA2343878A1 (en) 1998-10-28 2000-05-04 Novozymes A/S Method for generating a gene library
DE10121463A1 (en) 2001-05-02 2003-02-27 Henkel Kgaa New alkaline protease variants and detergents and cleaning agents containing these novel alkaline protease variants
DE10131441A1 (en) 2001-06-29 2003-01-30 Henkel Kgaa A new group of alpha-amylases and a method for identifying and obtaining new alpha-amylases
DE10153792A1 (en) 2001-10-31 2003-05-22 Henkel Kgaa New alkaline protease variants and detergents and cleaning agents containing these novel alkaline protease variants
DE10162727A1 (en) 2001-12-20 2003-07-10 Henkel Kgaa New alkaline protease from Bacillus gibsonii (DSM 14391) and detergents and cleaning compositions comprising these novel alkaline protease
DE10162728A1 (en) 2001-12-20 2003-07-10 Henkel Kgaa New alkaline protease from Bacillus gibsonii (DSM 14393) and detergents and cleaning compositions comprising these novel alkaline protease
DE10163748A1 (en) 2001-12-21 2003-07-17 Henkel Kgaa new glycosyl
DE10163883A1 (en) 2001-12-22 2003-07-10 Henkel Kgaa New alkaline protease from Bacillus sp. (DSM 14390) and detergents and cleaning agents containing these novel alkaline protease
DE10163884A1 (en) 2001-12-22 2003-07-10 Henkel Kgaa New alkaline protease from Bacillus sp. (DSM 14392) and detergents and cleaning agents containing these novel alkaline protease
DE10260903A1 (en) 2002-12-20 2004-07-08 Henkel Kgaa new perhydrolases
ES2361838T3 (en) 2003-12-03 2011-06-22 Danisco Us Inc. Perhidrolasa.
DE102004029475A1 (en) 2004-06-18 2006-01-26 Henkel Kgaa New enzymatic bleaching system

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH09299082A (en) * 1996-05-10 1997-11-25 Kao Corp Low-temperature alkali protease x, microorganism capable of producing the same, production of the same, and detergent composition containing the enzyme and enzyme preparation for food processing
US20020019325A1 (en) * 1998-03-27 2002-02-14 Hans Sejr Olsen Acidic cleaning composition comprising an acidic protease obtained from aspergillus aculeatus
WO2000029534A1 (en) * 1998-11-13 2000-05-25 Genencor International, Inc. Fluidized bed low density granule
US20070212706A1 (en) * 2004-04-23 2007-09-13 Susanne Wieland Novel alkaline proteases and detergents and cleaners comprising these novel alkaline proteases
DE102006042797A1 (en) * 2006-09-08 2008-03-27 Henkel Kgaa Enzyme granules with a high concentration of enzyme, especially e.g. alkaline protease or subtilisin types, useful in detergents and cleaning materials, especially tablets for washing machines and dishwashers

Cited By (107)

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WO2010146036A1 (en) 2009-06-19 2010-12-23 Henkel Ag & Co. Kgaa Novel proteases and means containing said proteases
WO2011110625A1 (en) 2010-03-11 2011-09-15 Henkel Ag & Co. Kgaa Performance-enhanced protease variant
WO2011134809A1 (en) 2010-04-26 2011-11-03 Novozymes A/S Enzyme granules
EP2840134A1 (en) 2010-04-26 2015-02-25 Novozymes A/S Enzyme granules
DE102010030609A1 (en) 2010-06-28 2011-12-29 Henkel Ag & Co. Kgaa New proteases and agents containing them
WO2012000829A1 (en) 2010-06-28 2012-01-05 Henkel Ag & Co. Kgaa Novel proteases and compositions comprising them
DE102011005354A1 (en) 2011-03-10 2012-09-13 Henkel Ag & Co. Kgaa Performance enhanced protease variants
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US9260706B2 (en) 2011-03-10 2016-02-16 Henkel Ag & Co. Kgaa Performance-enhanced protease variants
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WO2012175708A2 (en) 2011-06-24 2012-12-27 Novozymes A/S Polypeptides having protease activity and polynucleotides encoding same
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WO2013007594A1 (en) 2011-07-12 2013-01-17 Novozymes A/S Storage-stable enzyme granules
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WO2013041689A1 (en) 2011-09-22 2013-03-28 Novozymes A/S Polypeptides having protease activity and polynucleotides encoding same
DE102011118021A1 (en) 2011-10-28 2013-05-02 Henkel Ag & Co. Kgaa Performance enhanced and temperature-stable protease variants
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WO2013092635A1 (en) 2011-12-20 2013-06-27 Novozymes A/S Subtilase variants and polynucleotides encoding same
WO2013110766A1 (en) 2012-01-26 2013-08-01 Novozymes A/S Use of polypeptides having protease activity in animal feed and detergents
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