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WO2009121725A1 - Agents de lavage et de nettoyage contenant des protéases sécrétées par xanthomonas - Google Patents

Agents de lavage et de nettoyage contenant des protéases sécrétées par xanthomonas Download PDF

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Publication number
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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Prior art keywords
protease
xanthomonas
washing
acid
cleaning
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PCT/EP2009/053283
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German (de)
English (en)
Inventor
Petra Siegert
Marion Merkel
Cornelia Kluin
Timothy O'connell
Karl-Heinz Maurer
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Henkel AG and Co KGaA
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Henkel AG and Co KGaA
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Publication of WO2009121725A1 publication Critical patent/WO2009121725A1/fr
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    • 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

Definitions

  • the invention is directed to detergents and cleaners containing a protease from a bacterium of the genus Xanthomonas, to these proteases themselves and to the preparation and use of these proteases. Furthermore, the invention is directed to purification processes in which these agents are used and to uses of these agents.
  • proteases of the subtilisin type have hitherto been used with preference.
  • the proteases used in the detergents or cleaning agents known from the prior art are either originally derived from microorganisms, for example the genera Bacillus, Streptomyces, Humicola or Pseudomonas, and / or are produced according to known biotechnological methods by suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or by filamentous fungi.
  • subtilisins BPN 'and Carlsberg examples of these are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the protease from Bacillus lentus, in particular from Bacillus lentus DSM 5483, subtilisin DY and the subtilases, but no longer the subtilisins in the strict sense attributable enzymes Thermitase, proteinase K and the proteases TW3 and TW7.
  • proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym, Natalase®, Kannase® and Ovozyme® from Novozymes, which are available under the trade names, Purafect®, Purafect® OxP, Purafect® Prime and Properase ® from Genencor, sold under the trade name Protosol® by Advanced Biochemicals Ltd., Thane, India, under the trade name Wuxi® by Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® and Protease P From Amano Pharmaceuticals Ltd., Nagoya, Japan, and that available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan.
  • proteases are used per se in laundry products. From the prior art, therefore, no detergents and cleaners are known in which a protease from a bacterium of the genus Xanthomonas is used.
  • a disadvantage of the proteases hitherto used in detergents and cleaning agents is that they often do not have satisfactory proteolytic activity and therefore the agents containing them have no satisfactory cleaning performance in relation to proteinaceous soils. 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.
  • 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.
  • a further object of the present invention is to provide such protease enzymes which are suitable for use in detergents and cleaners according to the invention and which are distinguished by a good, preferably improved proteolytic activity with respect to at least one soiling, preferably with respect to to several stains, distinguished when they are used in detergents or cleaning agents, in particular in the above-mentioned temperature range.
  • the invention thus provides a washing or cleaning agent comprising a protease which is naturally present in a bacterium of the genus Xanthomonas and at least one further detergent ingredient.
  • proteases derived from a bacterium of the genus Xanthomonas are advantageously used in detergents or cleaning agents and in washing or cleaning agents according to the invention, especially at low temperatures, especially in a temperature range between 20 and 60 0 C, an improved Removal of protease-sensitive residues, such as stains on textiles or dishes allow.
  • 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.
  • 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, in particular, these Xanthomonas species express proteases which show corresponding advantages in detergents or cleaners according to the invention.
  • the protease is a bacterial protease that can be isolated from the bacterium. Therefore, in particular those proteases which have been introduced into a bacterial strain according to the invention by means of genetic engineering methods and are expressed by this recombinant are not included.
  • Proteases known in the art which are produced by means of a bacterial strain according to the invention - i. for the bacteria of the genus Xanthomonas the production organism based on the introduction of the gene coding for the protease in this organism by means of genetic engineering - is, therefore, not the subject of the invention.
  • the classical procedure for obtaining the enzymes is known to the person skilled in the art of enzyme technology and is to cultivate microorganism-containing samples under the conditions considered suitable, for example in an alkaline medium. In this way, enrichment cultures of the microorganisms are obtained which contain the desired enzymes, in this case proteases, which are active under the conditions in question. From this, the microorganisms with the most efficient enzymes are then selected and purified, for example, by plating on proteinaceous agar plates and measuring the lysis farms formed or identified and cloned the genes encoding them. Such an approach is described, for example, in the textbook "Alkalophilic Microorganisms. A new microbial world "by K. Horikoshi and T.
  • any or any protease that is naturally present in a microorganism, in particular a bacterium is also advantageously usable in a washing or cleaning agent, ie has a satisfactory proteolytic activity in these agents on use of the agent results in a satisfactory removal of proteinaceous soils. Therefore, it is all the more surprising that proteases are present in bacteria of the genus Xanthomonas, in particular in the Xanthomonas species described above, which are suitable for use in detergents and cleaners, and in particular when using a washing and cleaning agent containing them a satisfactory Removal of proteinaceous soiling cause.
  • Demanding conditions of use for detergents and cleaners are particularly due to the presence of one or more other ingredients in such agents and in the wash liquor formed by them during the washing process such as bleaching agents, bleach activators, surfactants, builders and / or on Reason for the pH of such agents and the wash liquor formed by them during the washing process and / or due to the ionic strength and / or the temperature of the wash liquor during the washing process.
  • a washing and cleaning agent with a protease from a bacterium of the genus Xanthomonas has an increased performance compared to a protease-free agent and achieves a very good cleaning performance in terms of protease-sensitive soiling.
  • the agent is characterized in that the bacterium is selected from the group consisting of Xanthomonas axonopodis DSM 3585, Xanthomonas axonopodis pvar. Begoniae DSM 50850, Xanthomonas axonopodis pvar.
  • malvacearum DSM 1220 Xanthomonas campestris DSM 1050 (NCPPB 1929), Xanthomonas campestris DSM 19000, Xanthomonas campestris pvar. campestris DSM 3586, Xanthomonas campestris pvar. pelargonii DSM 50857.
  • DSMZ German Collection of Microorganisms and Cell Cultures
  • all solid, liquid or flowable, gelatinous, portion-packed or individually portionable, pulverulent, granulated, compressed into tablets, pasty, sprayable or in other conventional dosage forms ready-made means for mechanical or manual textile washing can serve as detergent.
  • the detergents also include washing aids, which are added to the actual detergent in the manual or machine textile washing, in order to achieve a further effect.
  • Detergents include all hard surface cleaning agents, including manual and machine dishwashing detergents, carpet cleaners, scouring agents, glass cleaners, toilet scavengers, etc., also found in all of these dosage forms.
  • Textile pre- and post-treatment are finally on the one hand such means with which the garment is brought into contact before the actual laundry, for example, for solving stubborn dirt, on the other hand, those in one of the actual textile laundry downstream step the laundry further desirable Give properties such as a comfortable grip, crease resistance or low static charge.
  • the fabric softeners are calculated. "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) are measured and is preferably in the range of 5 to 10,000 mPas.
  • Preferred agents have viscosities of 10 to 8000 mPas, with values between 120 to 3000 mPas being particularly preferred. In the present application, all washing and cleaning agents are also summarized as an agent.
  • an agent according to the invention contains the protease in an amount of from 2 ⁇ g to 20 mg, preferably from 5 ⁇ g to 17.5 mg, more preferably from 20 ⁇ g to 15 mg and most preferably from 50 ⁇ g to 10 mg per g of the agent.
  • the washing or cleaning agents according to the invention contain, in addition to a protease from a bacterium of the genus Xanthomonas, at least one further detergent ingredient.
  • the detergent ingredient is selected from the group consisting of builder, surfactant, organic and / or inorganic peroxygen bleach, bleach activator, organic solvent, acid, grayness inhibitor, optical brightener, polymeric thickener, and combinations thereof.
  • a combination of a protease present naturally in a bacterium of the genus Xanthomonas with one or more other ingredients of the compositions proves to be advantageous, as such agent provides improved cleaning performance by resulting synergisms, especially between the protease and the protease the further ingredient.
  • the agent effects an improved removal of stains, for example proteinaceous stains, in comparison with an agent which either contains only one of the two components or also in comparison to the expected cleaning performance of an agent with both components on the basis of the simple Addition of the respective individual contributions of these two components to the cleaning performance of the agent.
  • Suitable surfactants are, in particular, anionic surfactants, nonionic surfactants and mixtures thereof, but also cationic, zwitterionic and amphoteric surfactants.
  • Suitable nonionic surfactants are in particular alkyl glycosides and ethoxylation and / or propoxylation of alkyl glycosides or linear or branched alcohols each having 12 to 18 carbon atoms in the alkyl moiety and 3 to 20, preferably 4 to 10 alkyl ether groups. Also suitable are ethoxylation and / or propoxylation products of N-alkylamines, vicinal diols, fatty acid esters and fatty acid amides which correspond to said long-chain alcohol derivatives with respect to the alkyl moiety and of alkylphenols having 5 to 12 carbon atoms in the alkyl radical.
  • Nonionic surfactants are preferably alkoxylated, advantageously ethoxylated, especially primary alcohols having preferably 8 to 18 carbon atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol used, in which the alcohol radical may be linear or preferably methyl-branched in the 2-position or may contain linear and methyl-branched radicals in the mixture, as they are usually present in Oxoalkoholresten.
  • EO ethylene oxide
  • alcohol ethoxylates with linear radicals of alcohols of natural origin having 12 to 18 carbon atoms, for example of coconut, palm, tallow or oleyl alcohol, and on average 2 to 8 EO per mole of alcohol are preferred.
  • the preferred ethoxylated alcohols include, for example, C 12 -C 14 -alkoxy with 3 EO or 4 EO, C 9 -C 11 -alkyl 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 with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C 12 -C 14 -alcohol with 3 EO and C 12 -C 18 - Alcohol with 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 given represent statistical means which, for a particular product, may be an integer or a fractional number.
  • Preferred alcohol ethoxylates have a narrow homolog distribution (narrow rank ethoxylates, NRE).
  • fatty alcohols with more than 12 EO can also be used. Examples of these are (TaIg) fatty alcohols with 14 EO, 16 EO, 20 EO, 25 EO, 30 EO or 40 EO.
  • agents for use in mechanical processes usually extremely low-foam compounds are used. These include preferably C 12 -C 18 -alkylpolyethylenglykol-polypropylene glycol ethers with in each case at to 8 mol ethylene oxide and propylene oxide units in the molecule.
  • C 12 -C 18 -alkylpolyethylenglykol-polypropylene glycol ethers with in each case at to 8 mol ethylene oxide and propylene oxide units in the molecule.
  • other known low-foam nonionic surfactants such as, for example, C 12 -C 18 -alkyl polyethylene glycol-polybutylene glycol ethers having up to 8 moles of ethylene oxide and butylene oxide units in the molecule and end-capped alkylpolyalkylene glycol mixed ethers.
  • the nonionic surfactants also include alkyl glycosides of the general formula RO (G) x in which R is a primary straight-chain or methyl-branched, in particular 2-methyl-branched aliphatic radical having 8 to 22, preferably 12 to 18 carbon atoms and G represents a glycose unit having 5 or 6 C atoms, preferably glucose.
  • the degree of oligomerization x which indicates the distribution of monoglycosides and oligoglycosides, is an arbitrary number - which, as a variable to be determined analytically, may also assume fractional values - between 1 and 10; preferably x is 1, 2 to 1, 4.
  • the polyhydroxy fatty acid amides are preferably derived from reducing sugars having 5 or 6 carbon atoms, in particular from glucose.
  • the group of polyhydroxy fatty acid amides also includes compounds of the formula (IV)
  • R 3 is a linear or branched alkyl or alkenyl radical having 7 to 12 carbon atoms
  • R 4 is a linear, branched or cyclic alkylene radical or an arylene radical having 2 to 8 carbon atoms
  • R 5 is a linear, branched or cyclic alkyl radical or a Aryl radical or an oxy-alkyl radical having 1 to 8 carbon atoms, wherein C- ⁇ -C 4 alkyl or phenyl radicals are preferred
  • [Z] is a linear polyhydroxyalkyl radical whose alkyl chain is substituted with at least two hydroxyl groups, or alkoxylated, preferably ethoxylated or propoxylated derivatives of this group.
  • [Z] is also obtained here preferably by reductive amination of a sugar such as glucose, fructose, maltose, lactose, galactose, mannose or xylose.
  • a sugar such as glucose, fructose, maltose, lactose, galactose, mannose or xylose.
  • the N-alkoxy- or N-aryloxy-substituted compounds can then be converted into the desired polyhydroxy fatty acid amides, for example, by reaction with fatty acid methyl esters in the presence of an alkoxide as catalyst.
  • nonionic surfactants used either as the 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 esters, preferably from 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 alkanolamides may also be suitable.
  • nonionic surfactants are so-called gemini surfactants. These are generally understood as meaning those compounds which have two hydrophilic groups per molecule. These groups are usually separated by a so-called "spacer". This spacer is typically a carbon chain that should be long enough for the hydrophilic groups to be spaced sufficiently apart for them to act independently of each other. Such surfactants are generally characterized by an unusually low critical micelle concentration and the ability to greatly reduce the surface tension of the water. In exceptional cases, the term gemini surfactants not only such "dimer”, but also corresponding to "trimeric” surfactants understood.
  • Suitable gemini surfactants are, for example, sulfated hydroxy mixed ethers or dimer alcohol bis and trimer alcohol tris sulfates and ether sulfates.
  • End-capped dimeric and trimeric mixed ethers are characterized in particular by their bi- and multi-functionality.
  • the end-capped surfactants mentioned have good wetting properties and are low in foaming, so that they are particularly suitable for use in machine washing or cleaning processes.
  • gemini-polyhydroxy fatty acid amides or poly-polyhydroxy fatty acid amides it is also possible to use gemini-polyhydroxy fatty acid amides or poly-polyhydroxy fatty acid amides.
  • sulfuric acid monoesters of the straight-chain or branched C 7 -C 2 -substituted alcohols ethoxylated with from 1 to 6 mol of ethylene oxide such as 2-methyl-branched C 9 -C 12 -alcohols having on average 3.5 mol of ethylene oxide (EO) or C 12 -C 18 -FeHaIkOhOIe with 1 to 4 EO.
  • the preferred anionic surfactants also include the salts of alkylsulfosuccinic acid, which are also referred to as sulfosuccinates or as sulfosuccinic acid esters, and which are monoesters and / or diesters of sulfosuccinic acid with alcohols, preferably fatty alcohols and in particular ethoxylated fatty alcohols.
  • alcohols preferably fatty alcohols and in particular ethoxylated fatty alcohols.
  • Preferred sulfosuccinates contain C 8 to C 18 fatty alcohol residues or mixtures of these.
  • Particularly preferred sulfosuccinates contain a fatty alcohol residue derived from ethoxylated fatty alcohols, which by themselves are nonionic surfactants.
  • Sulfosuccinates whose fatty alcohol residues are derived from ethoxylated fatty alcohols with a narrow homolog distribution, are again particularly preferred.
  • alk (en) yl-succinic acid having preferably 8 to 18 carbon atoms in the alk (en) yl chain or salts thereof.
  • Suitable further anionic surfactants are fatty acid derivatives of amino acids, for example N-methyltaurine (Tauride) and / or N-methylglycine (sarcosides).
  • sarcosides or the sarcosinates and here especially sarcosinates of higher and optionally monounsaturated or polyunsaturated fatty acids such as oleyl sarcosinate.
  • anionic surfactants are particularly soaps into consideration.
  • 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, soap mixtures derived from natural fatty acids, for example coconut, palm kernel or tallow fatty acids. Together with these soaps or as a substitute for soaps, it is also possible to use the known alkenylsuccinic acid salts.
  • the anionic surfactants may be in the form of their sodium, potassium or ammonium salts and as soluble salts of organic bases, such as mono-, di- or triethanolamine.
  • the anionic surfactants are preferably present 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 proportions of from 5% by weight to 50% by weight, in particular from 8% by weight to 30% by weight.
  • An agent according to the invention preferably contains at least one water-soluble and / or water-insoluble, organic and / or inorganic builder.
  • the water-soluble organic builder substances include polycarboxylic acids, in particular 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-hydroxyethane-1, 1-diphosphonic acid, polymeric hydroxy compounds such as dextrin and polymeric (poly) carbon acids, in particular the polycarboxylates obtainable by the oxidation of polysaccharides or dextrins, polymeric acrylic acids, methacrylic acids, maleic acids and mixed polymers thereof, which may also contain polymerized small amounts of polymerizable substances without
  • the molecular weight of the homopolymers of unsaturated carboxylic acids is generally between 3,000 and 200,000, of the copolymers between 2,000 and 200,000, preferably 30,000 to 120,000, each based on the free acid.
  • a particularly preferred acrylic acid-maleic acid copolymer has a molecular weight of from 30,000 to 100,000.
  • Commercially available products are, for example, Sokalan® CP 5, CP 10 and PA 30 from BASF.
  • Suitable, although less preferred, compounds of this class are copolymers of acrylic or methacrylic acid with vinyl ethers, such as vinylmethyl ethers, vinyl esters, ethylene, propylene and styrene, in which the acid content is at least 50% by weight.
  • 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 from (meth) -acrylic acid.
  • the second acidic monomer or its salt may be a derivative of a C 4 -C 8 -dicarboxylic acid, with maleic acid being particularly preferred, and / or a derivative of an alkylsulfonic acid which is substituted in the 2-position by an alkyl or aryl radical ,
  • Such polymers generally have a molecular weight between 1,000 and 200,000.
  • Further preferred copolymers are those which preferably have as monomers acrolein and acrylic acid / acrylic acid salts or vinyl acetate.
  • the organic builder substances can be used, in particular for the preparation of liquid agents, in the form of aqueous solutions, preferably in the form of 30 to 50 weight percent aqueous solutions. All of the acids mentioned are generally used in the form of their water-soluble salts, in particular their alkali metal salts.
  • organic builder substances may be present in amounts of up to 40% by weight, in particular up to 25% by weight and preferably from 1% by weight to 8% by weight. Quantities close to the stated upper limit are preferably used in pasty or liquid, in particular hydrous, agents.
  • Suitable water-soluble inorganic builder materials are, in particular, alkali metal silicates, alkali metal carbonates and alkali metal phosphates, which may be in the form of their alkaline, neutral or acidic sodium or potassium salts.
  • alkali metal silicates alkali metal carbonates
  • alkali metal phosphates which may be in the form of their alkaline, neutral or acidic sodium or potassium salts.
  • examples of these are trisodium phosphate, tetrasodium diphosphate, disodium dihydrogen diphosphate, pentasodium triphosphate, so-called sodium hexametaphosphate, oligomeric trisodium phosphate with degrees of oligomerization of 5 to 1000, in particular 5 to 50, and the corresponding potassium salts or mixtures of sodium and potassium salts.
  • crystalline or amorphous alkali metal aluminosilicates in amounts of up to 50% by weight, preferably not more than 40% by weight, are used as water-insoluble, water-dispersible inorganic builder materials. and in liquid agents, in particular from 1 wt .-% to 5 wt .-%, used.
  • detergent grade crystalline sodium aluminosilicates particularly zeolite A, P and optionally X, alone or in mixtures, for example in the form of a cocrystal of zeolites A and X (Vegobond® AX, a commercial product of Condea Augusta SpA)
  • zeolites A and X a cocrystal of zeolites A and X
  • Amounts near the above upper limit are preferably used in solid, particulate agents.
  • suitable aluminosilicates have no particles with a particle size greater than 30 .mu.m and preferably consist of at least 80% by weight of particles having a size of less than 10 .mu.m.
  • Their calcium binding properties which can be determined according to the specifications of German Patent DE 24 12 837, are generally in the range of 100 to 200 mg CaO per gram.
  • Suitable substitutes or partial substitutes for the said aluminosilicate are crystalline alkali silicates which may be present alone or in a mixture with amorphous silicates.
  • the alkali metal silicates useful as builders in the compositions preferably have a molar ratio of alkali oxide to SiO 2 of less than 0.95, in particular of 1: 1, 1 to 1: 12, and may be amorphous or crystalline.
  • Preferred alkali metal silicates are the sodium silicates, in particular the amorphous sodium silicates, with a molar ratio of 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 to 22, in particular 1, 9 to 4 and y is a number from 0 to 33 and preferred values for x are 2, 3 or 4.
  • Preferred crystalline phyllosilicates are those in which x in the abovementioned general formula assumes the values 2 or 3. In particular, both ⁇ - and ⁇ -sodium disilicates (Na 2 Si 2 O 5 y H 2 O) are preferred.
  • amorphous alkali metal silicates can be used in agents according to the invention.
  • a crystalline sodium layer silicate with a modulus of 2 to 3 is used, as it can be prepared from sand and soda.
  • Crystalline sodium silicates with a modulus in the range of 1.9 to 3.5 are used in a further preferred embodiment of the composition.
  • Crystalline layer-form silicates of formula (I) given above are sold by Clariant GmbH under the trade name Na-SKS, eg 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).
  • Na-SKS eg 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
  • Na-SKS-4 Na 2 Si 4 O 9 XH 2 O, makatite
  • Na-SKS-5 OC-Na 2 Si 2 O 5
  • Na-SKS-7 ⁇ -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
  • Na-SKS-13 NaHSi 2 O 5
  • Na-SKS-6 5-Na 2 Si 2 O 5 .
  • a granular compound of crystalline phyllosilicate and citrate, of crystalline phyllosilicate and of the above-mentioned (co-) polymeric polycarboxylic acid, or of alkali silicate and alkali metal carbonate, as described, for example, under the name Nabion® 15 is commercially available.
  • Builders are preferably present in the compositions in amounts of up to 75% by weight, in particular 5% by weight to 50.
  • suitable peroxygen compounds are in particular organic peracids or pers acid salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and under the washing conditions hydrogen peroxide donating inorganic salts, which include perborate, percarbonate, persilicate and / or persulfate Caroat belong into consideration.
  • organic peracids or pers acid salts of organic acids such as phthalimidopercaproic acid, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and under the washing conditions hydrogen peroxide donating inorganic salts, which include perborate, percarbonate, persilicate and / or persulfate Caroat belong into consideration.
  • solid peroxygen compounds are to be used, they can be used in the form of powders or granules, which can also be enveloped in a manner known in principle.
  • an agent contains peroxygen compounds, they are present in amounts of preferably up to 50% by weight, especially from 5% to 30% by weight.
  • bleach stabilizers such as, for example, phosphonates, borates or metaborates and metasilicates and also magnesium salts such as magnesium sulfate may be expedient.
  • bleach activators it is possible to use compounds which, under perhydrolysis conditions, give aliphatic peroxycarboxylic acids having preferably 1 to 10 C atoms, in particular 2 to 4 C atoms, and / or optionally substituted perbenzoic acid.
  • Suitable substances are those which carry O- and / or N-acyl groups of the stated C atom number and / or optionally substituted benzoyl groups.
  • polyacylated alkylenediamines in particular tetraacetylethylenediamine (TAED), acylated triazine derivatives, in particular 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 phenolsulfonates, in particular n-nonanoyl or isononanoyloxybenzenesulfonate (n- or iso-NOBS), carboxylic anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate, 2,5-diacetoxy- 2,5-dihydrofuran and enol esters
  • TAED
  • hydrophilic substituted acyl acetals and the acyl lactams are also preferably used.
  • Combinations of conventional bleach activators can also be used.
  • Such bleach activators may, in particular in the presence of the abovementioned hydrogen peroxide-supplying bleach, in the usual amount range, preferably in amounts of 0.5 wt .-% to 10 wt .-%, in particular 1 wt .-% to 8 wt .-%, based on the total
  • agents which are included are preferably completely absent when using percarboxylic acid as the sole bleaching agent.
  • organic solvents which can be used in addition to water include alcohols having 1 to 4 carbon atoms, in particular methanol, ethanol, isopropanol and tert-butanol, diols having 2 to 4C -Atomen, in particular ethylene glycol and propylene glycol, and mixtures thereof and derived from the classes of compounds mentioned ether.
  • water-miscible solvents are preferably present in the compositions in amounts not exceeding 30% by weight, in particular from 6% by weight to 20% by weight.
  • the agents systemic and environmentally friendly acids especially citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid and / or adipic acid, but also, mineral acids, in particular sulfuric acid, or bases, in particular ammonium or alkali metal hydroxides.
  • Such pH regulators are present in the compositions in amounts of preferably not more than 20% by weight, in particular from 1.2% by weight to 17% by weight.
  • Graying inhibitors have the task of keeping suspended from the textile fiber dirt suspended in the fleet.
  • Water-soluble colloids of mostly organic nature are suitable for this purpose, for example starch, glue, gelatin, salts of ether carboxylic acids or ether sulfonic acids of starch or of cellulose or salts of acidic sulfuric acid esters of cellulose or starch.
  • water-soluble polyamides containing acidic groups are suitable for this purpose.
  • starch derivatives can be used, for example aldehyde starches.
  • cellulose ethers such as carboxymethylcellulose (Na salt), methylcellulose, hydroxyalkylcellulose and mixed ethers, such as methylhydroxyethylcellulose, methylhydroxypropylcellulose, methylcarboxymethylcellulose and mixtures thereof, for example in amounts of from 0.1 to 5% by weight, based on the agent.
  • Laundry detergents may contain, for example, derivatives of diaminostilbenedisulfonic acid or their alkali metal salts as optical brighteners, although they are preferably free of optical brighteners for use as color detergents.
  • salts of 4,4'-bis (2-anilino-4-morpholino-1, 3,5-triazinyl-6-amino) stilbene-2,2'-disulphonic acid or compounds of similar construction which are used instead of the morpholino Group carry a diethanolamino group, a methylamino group, an anilino group or a 2-methoxyethylamino group.
  • brighteners of the substituted diphenylstyrene type may be present, for example, the alkali salts of 4,4'-bis (2-sulfostyryl) -diphenyl, 4,4'-bis (4-chloro-3-sulfostyryl) -diphenyl, or 4 - (4-chlorostyryl) -4 '- (2-sulfostyryl).
  • Mixtures of the aforementioned optical brightener can be used.
  • the agent may contain one or more polymeric thickeners.
  • Polymeric thickeners are the polyelectrolytes thickening polycarboxylates, preferably homopolymers and copolymers of acrylic acid, in particular acrylic acid copolymers such as acrylic acid Methacrylic acid copolymers, and the polysaccharides, in particular heteropolysaccharides, and other conventional thickening polymers.
  • Suitable polysaccharides or heteropolysaccharides are the polysaccharide gums, for example gum arabic, agar, alginates, carrageenans and their salts, guar, guar gum, tragacanth, gellan, Ramzan, dextran or xanthan and their derivatives, for example propoxylated guar, and also their mixtures.
  • polysaccharide thickeners such as starches or cellulose derivatives
  • starches or cellulose derivatives may alternatively or preferably be used in addition to a polysaccharide gum, for example starches of various origins and starch derivatives, for example hydroxyethyl starch, starch phosphate esters or starch acetates, or carboxymethylcellulose or its sodium salt, methyl, ethyl, hydroxyethyl, Hydroxypropyl, hydroxypropyl methyl or hydroxyethyl methyl cellulose or cellulose acetate.
  • starches of various origins and starch derivatives for example hydroxyethyl starch, starch phosphate esters or starch acetates, or carboxymethylcellulose 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 is available, for example, from Kelco under the trade name Keltrol®, eg as cream colored Powder Keltrol® T (transparent) or as white granules Keltrol® RD (Readily Dispersable).
  • Keltrol® eg as cream colored Powder Keltrol® T (transparent) or as white granules Keltrol® RD (Readily Dispersable).
  • acrylic acid polymers which are suitable as polymeric thickeners are high molecular weight homopolymers of acrylic acid (INCI Carbomer) crosslinked with a polyalkenyl polyether, in particular an allyl ether of sucrose, pentaerythritol or propylene (INCI Carbomer), which are also referred to as carboxyvinyl polymers.
  • polyalkenyl polyether in particular an allyl ether of sucrose, pentaerythritol or propylene
  • carboxyvinyl polymers Such polyacrylic acids are available, inter alia, from BFGoodrich under the trade name Carbopol®, eg Carbopol® 940 (molecular weight about 4,000,000), Carbopol® 941 (molecular weight about 1,250,000) or Carbopol® 934 (molecular weight about 3,000. 000).
  • the content of polymeric thickener is usually not more than 8% by weight, preferably between 0.1 and 7% by weight, more preferably between 0.5 and 6% by weight, in particular between 1 and 5% by weight. and most preferably between 1, 5 and 4% by weight, for example between 2 and 2.5% by weight.
  • ingredients to be selected of the agent according to the invention as well as the conditions under which it is used according to the invention, such as temperature, pH, ionic strength, redox ratios or mechanical influences, are usually optimized for the respective field of application.
  • the solid dosage forms of a composition according to the invention include, in particular, extrudates, granules, tablets or pouches, which may be present both in bulk and in portions.
  • the agent is present as a free-flowing powder, in particular with 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.
  • agents according to the invention may also be liquid, gelatinous or pasty, in particular they may 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.
  • a washing or cleaning agent according to the invention can also be packaged in a container, preferably an air-permeable container, from which it is released shortly before use or during the washing process.
  • the protease contained in the composition and / or other ingredients of the composition may be coated with a substance which is impermeable to the enzyme at room temperature or in the absence of water, which becomes permeable to the enzyme under conditions of use of the composition.
  • Such an embodiment of the invention is thus characterized in that the protease is coated with a substance which is impermeable to the protease at room temperature or in the absence of water.
  • compositions according to the invention may contain only one protease as described. Alternatively, however, they may contain other proteases or other enzymes in a concentration effective for the effectiveness of the agent.
  • a further subject of the invention thus represents a washing or cleaning agent which is characterized in that it comprises at least one further enzyme, in particular a protease, amylase, cellulase, glycosidase, hemicellulase, mannanase, xylanase, pectinase, ⁇ -glucosidase, carrageenase , Lipase, oxidase, oxidoreductase or combinations thereof, wherein in principle all known in the art for this purpose enzymes can be used.
  • the enzymes may be adsorbed to carriers and / or embedded in encapsulants to protect against premature inactivation. They are contained in the detergents or cleaners according to the invention preferably in amounts of 1 ⁇ 10 -8 to 5 percent by weight, based on active protein (dry substance). Preferably, the enzymes are from 0.001 to 5% by weight, more preferably from 0.01 to 5% by weight, even more preferably from 0.05 to 4% by weight and most preferably from 0.075 to 3.5% by weight. -%, wherein each enzyme contained may be present in the said amount.
  • the weight of the liquid agent is determined so that the data are based on weight of enzyme and weight of agent. If several enzymes are used in the agent according to the invention, they may be present in the agent separately or together, for example as individual granules or as granules containing at least two different enzymes.
  • the protein concentration can be determined by known methods, for example, the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method (AG Gornall, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766).
  • the protease activity in such agents can be determined by the method described in Tenside, Vol. 7 (1970), pp. 125-132. It is given in PE (protease units).
  • the enzymes show synergistic effects with respect to their action against certain stains or stains, ie the enzymes contained in the middle composition mutually support each other in their cleaning performance.
  • the enzymes contained in the middle composition mutually support each other in their cleaning performance.
  • Very particular preference is given to such a synergism between the protease according to the invention and another enzyme of an agent according to the invention, including in particular between the protease according to the invention and another protease and / or an amylase and / or a mannanase and / or a lipase.
  • proteases are the subtilisins BPN 'from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, the protease PB92, the subtilisins 147 and 309, the protease from Bacillus lentus, subtilisin DY and the subtilases, but no longer the subtilisins in the strict sense attributable enzymes Thermitase, proteinase K and the proteases TW3 and TW7.
  • Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from the company Novozymes A / S, Bagsvaerd, Denmark.
  • subtilisins 147 and 309 are sold under the trade names Esperase®, and Savinase® by the company Novozymes. From the protease from Bacillus lentus DSM 5483 derived under the name BLAP® protease variants derived.
  • proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase® and Ovozyme® from the company Novozymes, which are sold under the trade names, Purafect®, Purafect® OxP, Purafect® Prime, Excellase® and Properase® from Danisco / Genencor, sold under the tradename Protosol® by Advanced Biochemicals Ltd., Thane, India, under the tradename Wuxi® by Wuxi Snyder Bioproducts Ltd.
  • proteases from Bacillus gibsonii and Bacillus pumilus disclosed in international patent applications WO 08/086916 and WO 07/131656. Further advantageous proteases are disclosed in 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.
  • Stenotrophomonas maltophilia in particular Stenotrophomonas maltophilia K279a, Bacillus intermedius and Bacillus sphaericus.
  • amylases are the ⁇ -amylases from Bacillus licheniformis, from Bacillus amyloliquefaciens or from Bacillus stearothermophilus and, in particular, also their improved developments for use in detergents or cleaners.
  • the enzyme from Bacillus licheniformis is available from the company Novozymes under the name Termamyl® and from the company Danisco / Genencor under the name Purastar®ST.
  • this ⁇ -amylase is available from the company Novozymes under the trade name Duramyl® and Termamyl®ultra, from the company Danisco / Genencor under the name Purastar®OxAm and from the company Daiwa Seiko Inc., Tokyo, Japan, as Keistase®.
  • the Bacillus amyloliquefaciens ⁇ -amylase is sold by the company Novozymes under the name BAN®, and variants derived from the Bacillus stearothermophilus ⁇ -amylase under the names BSG® and Novamyl®, also from the company Novozymes. Furthermore, for this purpose, the ⁇ -amylase from Bacillus sp.
  • a 7-7 (DSM 12368) and cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948).
  • CCTase cyclodextrin glucanotransferase
  • DSM 9948 Bacillus agaradherens
  • amylolytic enzymes disclosed in International Patent Applications WO 03/002711, WO 03/054177 and WO07 / 079938.
  • fusion products of all the molecules mentioned can be used.
  • those are under the trade names Fungamyl® available from the company Novozymes further developments of ⁇ -amylase from Aspergillus niger and A. oryzae suitable.
  • Amylase-LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus® are also from the company Novozymes.
  • variants of these enzymes obtainable by point mutations can be used according to the invention.
  • a cellulase is the fungal, endoglucanase (EG) -rich cellulase preparation or its further developments, which is offered by the company Novozymes under the trade name Celluzyme®. Endolase® and Carezyme®, also available from Novozymes, are based on the 50 kD EG or 43 kD EG from Humicola insolens DSM 1800. Further commercial products of this company are Cellusoft®, Renozyme® and Celluclean®. Furthermore, for example, the 20 kD-EG from Melanocarpus, which are available from the company AB Enzymes, Finland, under the trade names Ecostone® and Biotouch®.
  • hydrolytic enzymes are those which are grouped under the term glycosidases (E.C. 3.2.1.X). These include, in particular, arabinases, fucosidases, galactosidases, galactanases, arabico-galactan galactosidases, mannanases (also referred to as mannosidases or mannases), glucuronosidases, agarase, carrageenases, pullulanases, ⁇ -glucosidases, xyloglucanases (xylanases) and pectin-degrading enzymes (pectinases ).
  • Hemicellulases include, in particular, mannanases, xyloglucanases (xylanases), ⁇ -glucosidases and carrageenases, and also pectinases, pullulanases and ⁇ -glucanases.
  • Pectinases are pectin-degrading enzymes, wherein the hydrolytic pectin-degrading enzymes belong in particular 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.
  • pectin esterase pectin methethoxylase, pectin methoxylase, pectin methyl esterase, pectase, pectin methyl esterase, pectin esterase, pectin pectyl hydrolase, pectin polymerase, endopolygalacturonase, pectolase, pectin hydrolase, pectin polygalacturonase, endo-polygalacturonase, poly- ⁇ -1, 4-galacturonide glycanohydrolase, endogalacturonase, endo D-galacturonase, galacturan 1, 4- ⁇ -galacturonidase, exopolygalacturonase, poly (galacturonate) hydrolase, exo-D-galacturonase, exo-D-galacturonanase, exopoly-D-galacturonase, exo-poly-
  • Suitable enzymes for this purpose are, for example, under the name Gamanase® and Pektinex AR® from the company Novozymes, under the name Rohapec® B1 L from the company AB Enzymes and under the name Pyrolase® from Diversa Corp., San Diego, CA, USA available.
  • the ⁇ -glucanase obtained from Bacillus subtilis is available under the name Cereflo® from the company Novozymes.
  • Particularly preferred glycosidases or hemicellulases according to the invention are mannanases which are sold, for example, under the trade names Mannaway® by the company Novozymes or Purabrite® by the company Danisco / Genencor.
  • lipases or cutinases are the lipases originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or developed therefrom, in particular those with the amino acid exchange D96L. They are sold, for example, by the company Novozymes under the trade names Lipolase®, Lipolase®Ultra, LipoPrime®, Lipozyme® and Lipex®. Furthermore, for example, the cutinases can be used, which were originally isolated from Fusarium solani pisi and Humicola insolens.
  • lipases are from the company Amano under the names Lipase CE®, Lipase P®, Lipase B®, and Lipase CES®, lipase AKG®, Bacillis sp. Lipase®, Lipase AP®, Lipase M-AP® and Lipase AML®. From the company Danisco / Genencor, for example, the lipases or cutinases can be used, the initial enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii.
  • Lipase® and Lipomax® are prepared by Gist-Brocades (now Danisco / Genencor), and Lipase MY-30®, Lipase OF®, by Meito Sangyo KK of Japan and Lipase PL® distributed enzymes, further the product Lumafast® from the company Danisco / Genencor.
  • oxidoreductases such as oxidases, oxygenases, catalases (which react at low H 2 O 2 concentrations as peroxidase), peroxidases, such as halo, chloro, bromo, lignin, glucose or Manganese peroxidases, dioxygenases or laccases (phenol oxidases, polyphenol oxidases).
  • Suitable commercial products are Denilite® 1 and 2 from Novozymes.
  • WO 98/45398 A1 As example systems for enzymatic perhydrolysis which can be used advantageously, reference is made to the applications WO 98/45398 A1, WO 2005/056782 A2 and WO 2004/058961 A1.
  • a combined enzymatic bleaching system comprising an oxidase and a perhydrolase describes the application WO 2005/124012.
  • the enzymes used according to the invention are preferably originally derived from microorganisms, such as the genera Bacillus, Streptomyces, Humicola or Pseudomonas, and / or are produced by biotechnological methods known per se by suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or by filamentous fungi. It is emphasized that it may in particular also be technical enzyme preparations of the particular hydrolytic enzyme, ie accompanying substances may be present. Therefore, the enzymes can be formulated and used together with accompanying substances, for example from the fermentation or with stabilizers.
  • Table 1 below shows formulations for detergents and cleaners according to the invention.
  • Each formulation in this case comprises a protease from the bacterium mentioned and at least the particular detergent ingredient specified in the stated range of amounts.
  • All formulations shown in Table 1 may comprise one or more other detergent ingredients.
  • the formulations of Table 1 are given as basic formulations with a detergent ingredient additionally present in the respective base formulation in the stated amount.
  • each base formulation with each ingredient represents a further, independent formulation.
  • formulation 1 with an organic solvent (in particular an alcohol), with an acid, with an optical brightener and with a graying inhibitor are to be understood as four mutually independent egg recipes.
  • a separate subject of the invention is the use of a washing or cleaning agent according to the invention for the removal of stains, in particular protease-sensitive stains, on textiles or hard surfaces, i. for the cleaning of textiles or of hard surfaces.
  • agents according to the invention can be advantageously used, in particular because of the above-described properties of the contained protease, to remove impurities from textiles or from hard surfaces.
  • Embodiments of this subject invention include, for example, hand washing, manual removal of stains from textiles or hard surfaces, or use in conjunction with a machine process. All of the facts, subjects, and embodiments described for washing or cleaning compositions of the present invention are also contemplated this subject invention applicable. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive use.
  • the respective washing or cleaning agents according to the invention are provided according to one of the embodiments described above.
  • a further subject of the invention is a method for the cleaning of textiles or hard surfaces, which is characterized in that in at least one method step, a washing or cleaning agent according to the invention is used.
  • a washing or cleaning agent according to the invention is used.
  • Processes for cleaning textiles or hard surfaces are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned and washed off after the action time, or the items to be cleaned are otherwise treated with a detergent or a solution or dilution of this Is treated by means.
  • washing or cleaning methods can be enriched in at least one of the method steps to the application of a washing or cleaning agent according to the invention and then represent embodiments of the present invention. All facts, objects and embodiments described for washing or cleaning agents according to the invention are also applicable to this subject invention. Therefore, at this point is explicitly on the Revelation in the appropriate place with the reference that this disclosure also applies to the above inventive method.
  • 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 proteolysis index of at least 1.1 in an aqueous solution in the presence of at least one surfactant.
  • the surfactant may also be a surfactant mixture.
  • the proteolysis index has at least 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.
  • This proteolysis index is determined on the basis of standardized polluted textiles that can be obtained from the Eidgenössische Materialologies-und-Versuchsweg, St. Gallen, Switzerland (EMPA) or Center For Testmaterials BV, Viaardingen, the Netherlands.
  • EMPA Eidgenössische Materialismes-und-Versuchsweg, St. Gallen, Switzerland
  • C blood / milk / India 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.
  • detergent formulations can be used to determine the proteolysis index.
  • the presence of a surfactant is primarily important.
  • the detergent or the surfactant-containing solution may, but does not necessarily have to contain bleach.
  • the water to be used is city water with a water hardness of about 16 ° German hardness.
  • a particularly suitable detergent formulation is composed as follows (all figures in weight percent): 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, balance: foam inhibitors, optical brightener, fragrances, if necessary water. Their dosage is 5.9 g of the detergent per liter of wash liquor.
  • the surfactant or surfactant mixture is preferably selected from the surfactants described above.
  • the surfactant is contained in the solution in an amount of at least 0.5 g / L and preferably at least 0.75 g / L.
  • the measurement of the degree of whiteness is carried out on a previously calibrated with a white standard spectrometer in a conventional manner known in the art.
  • the proteolysis index is then defined as the quotient of the measured value of the whiteness of the surfactant-containing solution with a Xanthomonas protease according to the invention and the measurement of the whiteness of the surfactant-containing solution without a protease of Xanthomonas according to the invention over a pH range of at least 0.5 and more preferably of 0.75, from 1, from 1, 25, from 1, 5, from 1, 75 and from 2 pH units.
  • This pH range is preferably in a neutral or alkaline pH range, ie the smallest pH in this pH range is greater than or equal to pH 7.
  • the proteolysis index therefore expresses the fact that a protease according to the invention has a corresponding cleaning performance over a relatively large pH range, ie catalytic performance, which makes it particularly advantageous for use in detergents and cleaners.
  • the protease is naturally present in a bacterium 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.
  • 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.
  • the protease is naturally present in a bacterium selected from the group consisting of Xanthomonas axonopodis DSM 3585, Xanthomonas axonopodis pvar. Begoniae DSM 50850, Xanthomonas axonopodis pvar. malvacearum DSM 1220, Xanthomonas campestris DSM 1050 (NCPPB 1929), Xanthomonas campestris DSM 19000, Xanthomonas campestris pvar. campestris DSM 3586, Xanthomonas campestris pvar. pelargonii DSM 50857.
  • a bacterium selected from the group consisting of Xanthomonas axonopodis DSM 3585, Xanthomonas axonopodis pvar. Begoniae DSM 50850, Xanthomonas axonopodis
  • the protease is not the proteases PRT1 and PRT2 from Xanthomonas campestris (according to Dow et al., Applied and Environmental Microbiology 1990, 2994-2998 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).
  • a further subject of the invention is a nucleic acid which codes for a protease according to the invention as well as a vector containing such a nucleic acid.
  • nucleic acids are understood to mean the molecules which are naturally constructed from nucleotides and serve as information carriers, which code for the linear amino acid sequence in proteins or enzymes. It may be DNA or RNA, each of which may be present as a single strand, as a single strand complementary to this single strand or as a double strand. In the case of DNA, in particular the sequences of both complementary strands must be taken into account in all three possible reading frames.
  • codon triplets may encode the same amino acids so that a particular amino acid sequence may be derived from a plurality of different and possibly low identity nucleotide sequences, which is referred to as the degeneracy of the genetic code.
  • both amino acid sequences and nucleotide sequences must be included in the consideration of the scope. Therefore, all nucleotide sequences are in the invention with included, which can encode an enzyme described above. The person skilled in the art is able to determine these nucleotide sequences unequivocally since, despite the degeneracy of the genetic code, individual codons can be assigned to defined amino acids.
  • a person skilled in the art will be able to produce the corresponding nucleic acids by methods known today, such as, for example, chemical synthesis or polymerase chain reaction (PCR) in combination with molecular biological and / or proteinchemical standard methods, using known DNA and / or amino acid sequences.
  • methods known today such as, for example, chemical synthesis or polymerase chain reaction (PCR) in combination with molecular biological and / or proteinchemical standard methods, using known DNA and / or amino acid sequences.
  • PCR polymerase chain reaction
  • vectors are understood as consisting of nucleic acids which contain a nucleic acid according to the invention as a characteristic nucleic acid region. They can establish these in a species or cell line over several generations or cell divisions as a stable genetic element.
  • Vectors especially when used in bacteria, are special plasmids, ie circular genetic elements.
  • the nucleic acid is suitably cloned into a vector.
  • Vectors may be derived from bacterial plasmids, viruses or bacteriophages, or may be predominantly synthetic vectors or plasmids with elements of various origins. With the other genetic elements in each case, vectors are able to establish themselves as stable units in host cells over several generations.
  • telomeres For the purposes of the invention, it is irrelevant whether they establish themselves as extrachomosomal units or integrate them into a chromosome.
  • the selection of a vector is carried out for example on the basis of the achievable copy number, the available selection systems, including above all antibiotic resistance, or based on the cultivability of the host cells into which the vector is to be introduced.
  • the vector is an expression vector.
  • Expression vectors are capable of replicating in the host cells or host organisms and there to express the contained nucleic acid, for example as a transgene.
  • Preferred embodiments are expression vectors which themselves carry the genetic elements necessary for expression.
  • the expression is influenced, for example, by promoters which regulate the transcription of the nucleic acid.
  • the expression can be carried out by the natural, originally located in front of the expressed nucleic acid promoter, but also after genetic engineering by both provided on the expression vector promoter of the host cell as well as by a modified or completely different promoter of another organism or another host cell ,
  • expression vectors can be regulatable.
  • the host cells may well belong to different organisms or come from different organisms. Also, homologous protein recovery 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 translational-related modification reactions on the resulting protein are performed exactly as they would naturally occur.
  • a further subject of the invention is thus a non-human host cell which contains a protease according to the invention or a fragment thereof or which contains a nucleic acid according to the invention or which contains a vector according to the invention, in particular one which has a cell nucleus or one which is a bacterium.
  • all cells that is to say prokaryotic or eukaryotic cells, are suitable as host cells.
  • those host cells which can be genetically advantageously handled, for example, the transformation with the expression vector and its stable establishment, for example, unicellular fungi or bacteria.
  • those host cells are preferred, which are characterized in that they have been obtained after transformation with one of the vectors described above.
  • Preferred embodiments represent such host cells, which are regulatable in their activity due to genetic regulatory elements which are provided, for example, on the expression vector, but may also be present in these cells from the outset.
  • the host cells may be altered in their culture conditions requirements, have different or additional selection markers, or express other or additional proteins.
  • these may be those host cells which, in addition to the protein produced according to the invention, also express further, in particular economically interesting, proteins.
  • Preferred host cells are prokaryotic or bacterial cells.
  • bacteria are distinguished from eukaryotes by shorter generation times and lower demands on culturing conditions.
  • cost-effective methods for obtaining proteins according to the invention can be established.
  • gram-negative bacteria such as Escherichia coli (E. coli)
  • E. coli Escherichia coli
  • a large number of proteins are secreted into the periplasmic space, ie into the compartment between the two membranes enclosing the cells. This can be advantageous for special applications.
  • Gram-positive bacteria such as, for example, Bacilli or Actinomycetes or other representatives of the Actinomycetales
  • Gram-positive bacteria have no outer membrane, so that secreted proteins are released into the nutrient medium surrounding the cells, from which the expressed proteins according to the invention can be directly purified.
  • the host cell secretes the protein of the invention into the surrounding medium.
  • the host cell according to the invention is characterized in that it is a bacterium, in particular one which is selected from a) the group of the 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.
  • a bacterium in particular one which is selected from a) the group of the genera of Escherichia, Bacillus and Arthrobacter, Streptomyces, Stenotrophomonas, Xanthomonas and Pseudomonas or b) the group of Escherichi
  • Particularly suitable as host cells are bacteria of the genus Xanthomonas and very particularly preferably a Xanthomonas species mentioned in Table 1 or a Xanthomonas strain mentioned in Table 1.
  • the host cell may also be a eukaryotic cell, which is characterized in that it has a cell nucleus.
  • eukaryotic cells are capable of post-translationally modifying the protein formed. Examples thereof are fungi such as Actinomycetes or yeasts such as Saccharomyces or Kluyveromyces. This may be particularly advantageous, for example, if the proteins are to undergo specific modifications in the context of their synthesis that enable such systems. These include, for example, the binding of low molecular weight compounds such as membrane anchors or oligosaccharides.
  • the host cells according to the invention are cultured and fermented in a manner known per se, for example in discontinuous or continuous systems.
  • a suitable nutrient medium is inoculated with the host cells and the product is harvested from the medium after an experimentally determined period of time.
  • Continuous fermentations are characterized by achieving a flow equilibrium in which over a relatively long period of time cells partly die off but also regrow and at the same time product can be removed from the medium.
  • the media components which are consumed by the continuous cultivation are usually fed in, whereby increases in both the cell density and in the dry biomass and / or, above all, the activity of the protein of interest are achieved.
  • the fermentation can also be designed so that unwanted metabolites are filtered out or neutralized by the addition of buffer or matching counterions.
  • Another object of the invention is thus a process for the preparation of a protease according to the invention.
  • this includes any process which is suitable for the preparation of a protease according to the invention described above or which makes it possible to obtain a protease according to the invention.
  • this also includes chemical synthesis methods.
  • preferred are fermentative production processes which comprise, as a process step, the cultivation of a host cell according to the invention.
  • a preferred method for producing a protease according to the invention therefore comprises the method steps a) culturing a host cell according to the invention b) isolating the protease from the cultured host cells and / or from the medium surrounding the host cells c) optionally purifying the isolated protease.
  • Another object of the invention is a process for the purification of textiles or hard surfaces, which is characterized in that in at least one process step, a protease according to the invention is catalytically active, in particular such that the protease in an amount of 40 micrograms to 4 g, preferably from 50 ⁇ g to 3 g, more preferably from 100 ⁇ g to 2 g and most preferably from 200 ⁇ g to 1 g per application.
  • Another object of the invention is the use of a protease according to the invention for cleaning textiles or hard surfaces.
  • the protease in this use is preferably used in an amount of from 40 ⁇ g to 4 g, preferably from 50 ⁇ g to 3 g, particularly preferably from 100 ⁇ g to 2 g and very particularly preferably from 200 ⁇ g to 1 g.
  • the proteolytic activity of bacteria of the Xanthomonas strains Xanthomonas axonopodis DSM 3585, Xanthomonas axonopodis pvar. Begoniae DSM 50850, Xanthomonas axonopodis pvar. malvacearum DSM 1220, Xanthomonas campestris DSM 1050 (NCPPB 1929), Xanthomonas campestris DSM 19000, Xanthomonas campestris pvar. campestris DSM 3586 and Xanthomonas campestris pvar. pelargonii DSM 50857.
  • Example 2 Determination of the cleaning performance at 3O 0 C
  • Standardized soiled textiles were used with a blood / milk / ink soiling (C-05, Center For Test Materials BV, Viaardingen, The Netherlands). With this test material, different detergent formulations, which differed by the particular protease contained, were examined for their cleaning performance. For the approaches were for 60 minutes at a temperature of 3O 0 C washed. The dosage was 5.9 g of the detergent per liter of wash liquor. It was washed with city water having a water hardness of 16 ° German hardness (DH) in a pH range between pH 8 and pH 9.
  • the detergent formulation was composed as follows (all figures in weight percent): 10% linear alkylbenzenesulfonate (sodium).
  • the detergent formulation was in each case mixed in the same manner with the proteolytic activities from the Xanthomonas strains of Example 1 given in Table 3 for the various test series.
  • the comparison formulation contained a variant of the alkaline protease from Bacillus lentus DSM 5483 ("Comparison"), which was established for detergents and improved in performance according to WO 92/21760 and which did not originate from a bacterium of the genus Xanthomonas After washing, the absorption of the wash liquor (as marker In addition, the proteolytic activity of the particular protease preparation used was determined. The result clearly shows that the detergents with proteases from Xanthomonas achieve a comparable or even better cleaning performance despite lower proteolytic activity as the comparison, the agents with the Xanthomonas proteases are thus the more powerful agents.
  • Example 3 Determination of the cleaning performance on 4O 0 C
  • Standardized soiled textiles were used which had been purchased from the Eidgenössische Material developmentss-und-Versuchsweg, St. Gallen, Switzerland (EMPA), or the Center For Testmaterials BV, Viaardingen, The Netherlands.
  • the following stains and textiles were used: A (grass on cotton, EMPA 164), B (wholegrain / soot on cotton, 10N), C (blood / milk / ink on cotton, C-05).
  • various detergent formulations as described in Example 2 were tested for their cleaning performance with the exception that at 4O 0 C was washed.
  • the detergent formulation was treated in an activity-identical manner with the various proteases from the Xanthomonas strains for the various test series.
  • the protease activity used was either 5 or 10 PE (protease units) per ml wash liquor. The same procedure was followed with reference formulations, provided that they contained proteases. Comparative formulations contained either no protease or a protease that does not originate from a bacterium of the genus Xanthomonas. After washing, the whiteness of the laundered fabrics, ie the brightening of the soils, was measured. The measurement was carried out on a Minolta CM508d spectrometer (illuminant D65, 10 °). The device was previously calibrated with a supplied white standard.
  • the detergents with Xanthomonas proteases in turn showed a high to very high cleaning performance on the mentioned soiling, especially over a pH range of one pH unit.
  • the proteases from Xanthomonas therefore have a proteolysis index of at least 1.1. This was determined as the quotient of the measurement results obtained in a washing process with a detergent containing a protease and a parallel control wash with the detergent without protease.

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Abstract

Les performances de lavage d'agents de lavage et de nettoyage sont améliorées en leur ajoutant une protéase sécrétée par une bactérie du genre Xanthomonas.
PCT/EP2009/053283 2008-04-02 2009-03-20 Agents de lavage et de nettoyage contenant des protéases sécrétées par xanthomonas Ceased WO2009121725A1 (fr)

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