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EP2358858B1 - Produits nettoyants et détergents contenant des protéases de bacillus pumilus - Google Patents

Produits nettoyants et détergents contenant des protéases de bacillus pumilus Download PDF

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Publication number
EP2358858B1
EP2358858B1 EP09756715.0A EP09756715A EP2358858B1 EP 2358858 B1 EP2358858 B1 EP 2358858B1 EP 09756715 A EP09756715 A EP 09756715A EP 2358858 B1 EP2358858 B1 EP 2358858B1
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EP
European Patent Office
Prior art keywords
protease
washing
cleaning
cleaning agent
acid
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EP09756715.0A
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German (de)
English (en)
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EP2358858A2 (fr
Inventor
Petra Siegert
Astrid Spitz
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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Priority to PL09756715T priority Critical patent/PL2358858T3/pl
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Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38609—Protease or amylase in solid compositions only
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38618—Protease or amylase in liquid compositions only

Definitions

  • the present patent application is directed to detergents and cleaners containing a protease from Bacillus pumilus. Furthermore, the application is directed to purification processes in which these agents are used and to uses of these agents. Furthermore, the application is directed to purification processes using these proteases and to the use of these proteases for washing and cleaning purposes.
  • 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 from Bacillus pumilus are also known from the prior art.
  • a protease from Bacillus pumilus is disclosed and also proposed as an ingredient for detergents and cleaners.
  • protease-containing detergents and cleaners with proteases of the prior art A disadvantage of protease-containing detergents and cleaners with proteases of the prior art is that the proteases contained have no satisfactory proteolytic activity, especially at low temperatures, for example between 10 ° C and 50 ° C, especially between 10 ° C and 40 ° C or between 20 ° C and 40 ° C, and the detergent or cleaning agent therefore shows no optimal cleaning performance, especially not in the respective temperature range, and in particular not on protease-sensitive stains.
  • new proteases, especially new microbial proteases for use in detergents and cleaners and to provide corresponding new detergents and cleaners containing such proteases.
  • the present invention is therefore based on the object to provide detergents or cleaners which have an improved cleaning performance, in particular with regard to soiling, which are sensitive to degradation by proteases.
  • a further object of the invention is to provide washing or cleaning compositions which have an improved cleaning performance at lower temperatures, in particular between 10 ° C and 50 ° C and preferably between 10 ° C and 40 ° C, in particular with regard to soiling, the sensitive are for degradation by proteases.
  • These detergents or cleaners should, especially in a temperature range between 10 ° C and 50 ° C, and preferably between 10 ° C and 40 ° C, show improved removal of at least one soiling which is sensitive to degradation by a protease.
  • the detergents or cleaners according to the invention preferably exhibit improved removal of several soiling.
  • these detergents or cleaners should contain proteases, and more preferably naturally occurring proteases, characterized in that their contribution to the cleaning performance of an agent containing the protease is at least approximate to the contribution of a proteolytic enzyme established for this purpose to the cleaning performance of the agent comes and ideally exceeds.
  • An object of the invention is therefore a washing or cleaning agent comprising a protease which comprises an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. At least 97.5%, and more preferably at least 98%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7 %, 98.8%, 98.9%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9% and most preferably 100% identical, as well as at least one other detergent ingredient.
  • a protease which comprises an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. At least 97.5%, and more preferably at least 98%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7 %, 98.8%, 98.9%, 99%
  • such a protease can be used advantageously in a detergent or cleaning agent and gives it an advantageous cleaning performance, especially at low temperatures, for example between 10 ° C and 50 ° C, especially between 10 ° C and 40 ° C. or between 20 ° C and 40 ° C.
  • a detergent or cleaning agent gives it an advantageous cleaning performance, especially at low temperatures, for example between 10 ° C and 50 ° C, especially between 10 ° C and 40 ° C. or between 20 ° C and 40 ° C.
  • Such an agent therefore enables improved removal of at least one, preferably of several protease-sensitive stains on textiles and / or hard surfaces, for example crockery.
  • the protease contained in a washing or cleaning agent according to the invention can be obtained from the culture supernatant of a Bacillus strain, which can be obtained from the examples. Germany) is identified as a Bacillus pumilus strain.
  • the strain or soil sample containing it is from Minneapolis, USA.
  • a plasmid containing the nucleic acid sequence of this protease was deposited with the DSMZ under the accession number DSM 21890.
  • a protease contained in a washing or cleaning agent according to the invention has a proteolytic activity, that is, it is capable of hydrolysing peptide bonds of a polypeptide or protein. It is therefore an enzyme which catalyzes the hydrolysis of peptide bonds and thereby is able to cleave peptides or proteins, in particular a subtilisin.
  • enzymes, proteins, fragments and derivatives are summarized under the generic term proteins or polypeptides, since a protein is a polypeptide.
  • protease present in a washing or cleaning agent according to the invention is suitable for use in laundry detergents because of its proteolytic activity and its further properties, in particular regarding its stability towards surfactants and / or bleaching agents and / or its temperature profile and / or its pH profile. and detergents.
  • proteases used in the compositions according to the invention are suitable for this purpose and, in particular when using a washing and cleaning agent containing them, they effect a satisfactory removal of one or more proteinaceous soils, in particular in the abovementioned temperature ranges. They therefore have under the demanding conditions of use of detergents and cleaners sufficiently high proteolytic activity to reduce proteinaceous soils under the conditions of use of the detergent or cleaning agent.
  • 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.
  • the whitening performance of a detergent or cleaning agent to stains especially on protease-sensitive soiling and this particular protease-sensitive Wäscheanschmutzieux understood.
  • the cleaning performance is preferably determined as indicated below.
  • proteases and in particular subtilisins are formed as so-called pre-proteins, ie together with a propeptide and a signal peptide, the function of the signal peptide usually being to ensure the release of the protease from the cell producing it into the periplasm or the medium surrounding the cell. and the propeptide is usually necessary for the correct folding of the protease.
  • the signal peptide and the propeptide are usually the N-terminal part of the preprotein. The signal peptide is cleaved from the rest of the protease under natural conditions by a signal peptidase. Subsequently, the correct final production of the protease supported by the propeptide takes place.
  • protease is then in its active form and cleaves off the propeptide itself. After cleavage of the propeptide, the then mature protease, in particular subtilisin, exerts its catalytic activity without the originally present N-terminal amino acids.
  • the mature (mature) proteases i. the enzymes processed after their preparation are preferred over the preproteins.
  • the proteases can be modified by the cells producing them after production of the polypeptide chain, for example by attachment of sugar molecules, formylations, aminations, etc. Such modifications are referred to as post-translational modifications. These post-translational modifications may or may not have an effect on the function of the protease.
  • the nucleic acid sequence of a protease contained in a washing or cleaning agent according to the invention is given under SEQ ID NO.1.
  • This nucleic acid encodes a protease which has a subtilisin typical division into signal peptide, propeptide and mature (mature) protease.
  • the full-length protein is indicated under SEQ ID NO. 2 and the mature protease under SEQ ID NO.
  • the actually active mature protein because this exerts the technically relevant function.
  • Detergents or cleaning agents which are particularly preferred according to the invention therefore contain the mature, active proteases. These have a molecular weight between 25 and 30 kD (kilodaltons), in particular 27 kD, determined by SDS-polyacrylamide gel electrophoresis.
  • nucleic acid or amino acid sequences are determined by a sequence comparison.
  • sequence comparison By such a comparison with known enzymes, which are deposited, for example, in generally accessible databases, the enzymatic activity of a considered enzyme can be deduced from the amino acid or nucleotide sequence. This can be qualitatively or quantitatively modified by other regions of the protein that are not involved in the actual reaction. This could, for example, relate to enzyme stability, activity, reaction conditions or substrate specificity.
  • sequence comparisons and alignments are created by computer programs. For example, Clustal (cf., for example, Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31, 3497-3500 ) or T-Coffee (cf., for example Uldame et al.
  • Such a comparison also allows a statement about the similarity of the compared sequences to each other. It is usually given in percent identity, that is, the proportion of identical nucleotides or amino acid residues at the same or in an alignment corresponding positions.
  • the broader concept of homology involves conserved amino acid substitutions in the consideration of amino acid sequences, that is, amino acids with similar chemical activity, as these usually perform similar chemical activities within the protein. Therefore, the similarity of the sequences compared may also be stated as percent homology or percent similarity.
  • Identity and / or homology information can be made about whole polypeptides or genes or only over individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by matches in the sequences. Such areas often have identical functions.
  • nucleic acid or amino acid sequence can be small and comprise only a few nucleotides or amino acids. Often, such small regions exert an essential influence on the overall activity of the protein Functions off. It may therefore be useful to relate sequence matches only to individual, possibly small areas. Unless stated otherwise, identity or homology information in the present application, however, refers to the total length of the respectively indicated nucleic acid or amino acid sequence.
  • a washing and cleaning agent with a protease preferred according to the invention has an increased cleaning performance compared to a protease-free agent and achieves a very good cleaning performance with regard to protease-sensitive soiling.
  • a preferred liquid detergent for such a washing system is composed as follows (all figures in weight percent): 0.3- 0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerol, 0.3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% nonionic surfactants, 1% boric acid, 1-2% sodium citrate (dihydrate), 2-4% soda, 14-16% coconut Fatty acids, 0.5% HEDP (1-hydroxyethane- (1,1-di-phosphonic acid)), 0-0.4% PVP (polyvinylpyrrolidone), 0-0.05% optical brightener, 0-0.001% dye, Rest demineralized water.
  • the dosage of the liquid detergent is between 4.5 and 6.0 grams per liter of wash liquor, for example, 4.7, 4.9 or 5.9 grams per liter of wash liquor. Preference is given to washing in a pH range between pH 8 and pH 10.5, preferably between pH 8 and pH 9.
  • a preferred powdered detergent for such a washing system is composed as follows (all figures in weight percent): 10% linear alkylbenzenesulfonate (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% carboxymethyl cellulose, 1.0% phosphonate, 25% sodium sulfate, balance: optional foam inhibitors, optical brightener, fragrances and, if necessary, water ad 100%.
  • the dosage of the powdered detergent is between 5.5 and 7.0 grams per liter of wash liquor, for example, 5.6, 5.9 or 6.7 grams per liter of wash liquor.
  • the abovementioned liquid detergent is preferably used to determine the cleaning performance as indicated.
  • the degree of whiteness i. the brightening of the stains, as a measure of the cleaning performance is preferably determined by optical measurement methods, preferably photometrically.
  • a suitable device for this purpose is for example the spectrometer Minolta CM508d.
  • the devices used for the measurement are previously calibrated with a white standard, preferably a supplied white standard.
  • the activity-equivalent use of the respective protease ensures that even if the ratio of active substance to total protein (the values of the specific activity) diverge, the respective enzymatic properties, for example the cleaning performance of certain soils, are compared. Generally, that applies a low specific activity can be compensated by adding a larger amount of protein.
  • Methods for the determination of protease activity are familiar to the expert in the field of enzyme technology and are routinely used by him. For example, such methods are disclosed in Surfactants, Vol. 7 (1970), pp. 125-132 ,
  • the protease activity can be determined via the release of the chromophore para-nitroaniline (pNA) from the substrate suc-L-Ala-L-Ala-L-Pro-L-Phe-p-Nitroanilide (AAPF).
  • the protease cleaves the substrate and releases pNA.
  • the release of pNA causes an increase in absorbance at 410 nm, the time course of which is a measure of enzymatic activity (see Del Mar et al., 1979).
  • the measurement is carried out at a temperature of 25 ° C, at pH 8.6, and a wavelength of 410 nm.
  • the measuring time is 5 min and the measuring interval 20s to 60s.
  • protease activity is usually indicated in protease units (PE). Suitable protease activities are, for example, 2.25, 5 or 10 PE per ml wash liquor. However, the protease activity is not equal to zero.
  • Detergents or cleaners according to the invention include all conceivable types of detergents or cleaners, both concentrates and undiluted agents, for use on a commercial scale, in the washing machine or in hand washing or cleaning. These include detergents for textiles, carpets, or natural fibers, for which the term detergent is used. These include, for example, dishwashing detergents for dishwashers or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood or leather, for which the term detergent is used.
  • 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.
  • An agent according to the invention can be either a means for large consumers or technical users as well as a product for the private consumer, wherein all types of detergents and cleaning agents established in the prior art also constitute embodiments of the present invention.
  • the washing or cleaning agents according to the invention which may be in the form of homogeneous solutions or suspensions in particular as pulverulent solids, in post-compacted particle form, can in principle all except the proteases used according to the invention contain known and commonly used in such agents ingredients, preferably at least one further ingredient is present in the agent.
  • the agents according to the invention may in particular be builders, surface-active surfactants, bleaches based on organic and / or inorganic peroxygen compounds, bleach activators, water-miscible organic solvents, enzymes, sequestering agents, electrolytes, pH regulators and other auxiliaries such as optical brighteners, grayness inhibitors, foam regulators and dyes and fragrances and combinations thereof.
  • a combination of a protease contained in a washing or cleaning agent according to the invention with one or more further ingredients of the compositions proves to be advantageous since such an agent provides improved cleaning performance by resulting synergisms, in particular between the protease and the further ingredient, having.
  • 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 with the expected cleaning performance of an agent with both components due to the mere addition of respective individual contributions of these two components to the cleaning performance of the agent.
  • the combination of a protease contained in a detergent or cleaning agent according to the invention with one of the surfactants and / or builders and / or bleaches described below achieves such a synergism.
  • compositions according to the invention may comprise one or more surfactants, 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.
  • the nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, in particular primary, alcohols having preferably 8 to 18 carbon atoms and on average 1 to 12 moles of ethylene oxide (EO) per mole of alcohol, in which the alcohol radical can 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.
  • alcohol ethoxylates with linear radicals of alcohols of natural origin having 12 to 18 carbon atoms, for example from 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 -alcohols with 3 EO or 4 EO, C 9 -C 11 -alcohols 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.
  • 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 range ethoxylates, NRE).
  • fatty alcohols with more than 12 EO can also be used. Examples include (tallow) 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.
  • 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.
  • 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 is hydrogen, an alkyl or hydroxyalkyl radical having 1 to 4 carbon atoms and [Z] is a linear or branched polyhydroxyalkyl radical having 3 to 10 carbon atoms and 3 to 10 hydroxyl groups:
  • 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) in the 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 and 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 1 -C 4 alkyl or phenyl radicals are preferred, and [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-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 straight-chain or branched C 7 -C 21 -alcohols ethoxylated with from 1 to 6 mol of ethylene oxide such as 2-methyl-branched C 9 -C 11 -alcohols having on average 3.5 mol of ethylene oxide (EO) or C 12 - C 18 -fatty alcohols with 1 to 4 EO.
  • EO ethylene oxide
  • the preferred anionic surfactants also include the salts of alkylsulfosuccinic acid, which are also referred to as sulfosuccinates or as sulfosuccinic acid esters, and the 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) ylsuccinic 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 inventive compositions in proportions of preferably 5 wt .-% to 50 wt .-%, in particular from 8 wt .-% to 30 wt .-%.
  • 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 also polymeric (poly) carboxylic acids, in particular those obtainable by oxidation of polysaccharides or dextrins Polycarboxylates, polymeric acrylic acids, methacrylic acids, maleic acids and copolymers thereof, which may also contain polymerized small amounts of polymeriz
  • 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 allylsulfonic 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 percent by weight 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 paste-form or liquid, in particular water-containing, agents according to the invention.
  • 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 and 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, and in liquid agents, in particular from 1% by weight to 5% by weight, are particularly suitable as water-insoluble, water-dispersible inorganic builder materials.
  • 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 capacity is usually 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 according to the invention preferably have a molar ratio of alkali metal oxide to SiO 2 below 0.95, in particular from 1: 1.1 to 1:12, and may be present in amorphous or crystalline form.
  • 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 of Na 2 Si x O 2x + 1 ⁇ y H 2 O used in the x, known as the modulus, an integer of 1, 9 to 22, especially 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 silicates practically anhydrous crystalline alkali silicates of the abovementioned general formula in which x is a number from 1.9 to 2.1, can be used in inventive compositions.
  • a crystalline sodium layer silicate with a modulus of 2 to 3 is used, as can be prepared from sand and soda. Crystalline sodium silicates with a modulus in the range from 1.9 to 3.5 are used in a further preferred embodiment of compositions according to the invention.
  • 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 .H 2 O, Kenyaite), Na-SKS-2 (Na 2 Si 14 O 29 .xH 2 O, magadiite), Na-SKS-3 (Na 2 Si 8 O 17 .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 .H 2 O, Kenyaite)
  • Na-SKS-2 Na 2 Si 14 O 29 .xH 2 O, magadiite
  • Na-SKS-3 Na 2 Si 8 O 17 .xH 2 O
  • Na-SKS-4 Na 2 Si 4 O 9 .xH 2 O, makatite
  • Na-SKS-5 ⁇ -Na 2 Si 2 O 5
  • Na-SKS-7 ⁇ -Na 2 Si 2 O 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 O 5
  • Na-SKS-13 NaHSi 2 O 5
  • Na-SKS-6 ⁇ -Na 2 Si 2 O 5
  • composition according to the invention 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, such as, for example, commercially available under the name Nabion® 15, is used ,
  • Builders are preferably present in the compositions according to the invention in amounts of up to 75% by weight, in particular 5% by weight to 50% by weight.
  • 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 according to the invention contains peroxygen compounds, they are present in amounts of preferably up to 50% by weight, in particular from 5% by weight to 30% by weight.
  • bleach stabilizers such as phosphonates, borates or metaborates and metasilicates and magnesium salts such as magnesium sulfate may be useful.
  • 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 can, in particular in the presence of the abovementioned hydrogen peroxide-producing bleach, in the usual amount range, preferably in amounts of from 0.5 wt .-% to 10 wt .-%, in particular 1 wt .-% to 8 wt .-%, based on However, total agent, be included, missing when using percarboxylic acid as the sole bleach, preferably completely.
  • sulfone imines and / or bleach-enhancing transition metal salts or transition metal complexes may also be present as so-called bleach catalysts.
  • organic solvents which can be used in addition to water include alcohols having 1 to 4 C atoms, in particular methanol, ethanol, isopropanol and tert-butanol, diols having 2 to 4 C -Atomen, in particular ethylene glycol and propylene glycol, and mixtures thereof and from the said classes of compounds-derived ether.
  • Such water-miscible solvents are preferably present in the compositions according to the invention in amounts of not more than 30% by weight, in particular from 6% by weight to 20% by weight.
  • compositions of the invention system and environmentally acceptable acids, in particular 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.
  • environmentally acceptable acids in particular 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.
  • pH regulators are present in the compositions according to the invention 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 compositions.
  • Detergents according to the invention 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.
  • Suitable salts are, for example, 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, 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.
  • foam inhibitors are, for example, soaps of natural or synthetic origin, which have a high proportion of C 18 -C 24 fatty acids.
  • Suitable non-surfactant foam inhibitors are, for example, organopolysiloxanes and mixtures thereof with microfine, optionally silanized silica and paraffins, waxes, microcrystalline waxes and mixtures thereof with silanated silicic acid or bis-fatty acid alkylenediamides. It is also advantageous to use mixtures of various foam inhibitors, for example those of silicones, paraffins or waxes.
  • the foam inhibitors, in particular silicone- and / or paraffin-containing foam inhibitors are preferably bound to a granular, water-soluble or dispersible carrier substance. In particular, mixtures of paraffins and bistearylethylenediamide are preferred.
  • the ingredients to be selected as well as the conditions under which the agent is used, such as temperature, pH, ionic strength, redox ratios or mechanical influences, should be optimized for the particular cleaning problem.
  • the usual temperatures for detergents and cleaners range from 10 ° C over 40 ° C and 60 ° C up to 95 ° for mechanical or technical applications. Since the temperature is usually infinitely adjustable in modern washing machines and dishwashers, all intermediate stages of the temperature are included.
  • the ingredients of the respective agents are coordinated. Synergies in terms of cleaning performance are preferred.
  • synergies which are present in a temperature range between 10 ° C and 60 ° C, in particular in a temperature range of 10 ° C to 60 ° C, from 10 ° C to 50 ° C, from 10 ° C to 40 ° C. , from 10 ° C to 30 ° C, from 15 ° C to 30 ° C from 10 ° C to 25 ° C and from 15 ° C to 25 ° C.
  • compositions according to the invention presents no difficulties and can be carried out in a known manner, for example by spray-drying or granulation, enzymes and possibly other thermally sensitive ingredients, for example bleaching agents, if appropriate be added separately later.
  • inventive compositions having an increased bulk density in particular in the range from 650 g / l to 950 g / l, a process comprising an extrusion step is preferred.
  • compositions according to the invention in tablet form, which may be monophasic or multiphase, monochromatic or multicolor and in particular consist of one or more layers, in particular two layers
  • the procedure is preferably such that all constituents - if appropriate one per layer - in one Mixer mixed together and the mixture by means of conventional tablet presses, such as eccentric or rotary presses, pressed with compressive forces in the range of about 50 to 100 kN, preferably at 60 to 70 kN.
  • a tablet produced in this way has a weight of 10 g to 50 g, in particular 15 g up to 40 g.
  • the Räumformen of the tablets is arbitrary and can be round, oval or angular, whereby intermediate forms are possible. Corners and edges are advantageously rounded. Round tablets preferably have a diameter of 30 mm to 40 mm.
  • the size of rectangular or cuboid-shaped tablets, which are introduced predominantly via the metering device, for example the dishwasher, is dependent on the geometry and the volume of this metering device.
  • Exemplary preferred embodiments have a base area of (20 to 30 mm) x (34 to 40 mm), in particular of 26x36 mm or 24x38 mm.
  • Liquid or pasty compositions according to the invention in the form of customary solvent-containing solutions are generally prepared by simply mixing the ingredients, which can be added in bulk or as a solution in an automatic mixer.
  • Embodiments of the present invention thus comprise all solid, powdered, liquid, gelatinous or paste-like administration forms of the agents, which if appropriate can also consist of several phases and can be present in compressed or uncompressed form.
  • a further embodiment of the invention therefore represents agents which are characterized in that they are present as a one-component system. Such means preferably consist of one phase. In contrast, means consisting of several phases are characterized in that it is divided into several components.
  • the solid dosage forms according to the invention also include extrudates, granules, tablets or pouches, which may be present both in large packages and in portions.
  • An agent according to the invention can be 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.
  • a further embodiment of the invention is therefore characterized in that the washing or cleaning agent is in liquid, gel or pasty form, in particular 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.
  • the washing or cleaning agent according to the invention may 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 and / or in the absence of water.
  • Detergents or cleaning agents according to the invention can exclusively contain a protease as described. Alternatively, they may also contain other hydrolytic enzymes or other enzymes in a concentration effective for the effectiveness of the agent.
  • a further subject of the invention thus represents agents which further comprise one or more further enzymes, wherein in principle all enzymes established in the prior art for these purposes can be used.
  • Preferred enzymes which can be used as enzymes are all enzymes which can develop a catalytic activity in the agent according to the invention, in particular a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, ⁇ -glucosidase, carrageenase, perhydrolase, oxidase, Oxidoreductase or a lipase, and preferably mixtures thereof.
  • These enzymes are basically of natural origin; Starting from the natural molecules, improved variants are available for use in detergents and cleaners, which are preferably used accordingly.
  • Agents according to the invention preferably contain enzymes in total amounts of 1 ⁇ 10 -8 to 5 percent by weight, based on active protein.
  • 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.
  • the enzymes may be adsorbed to carriers and / or embedded in encapsulants to protect against premature inactivation.
  • 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 ( Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 ).
  • BCA method bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid
  • the biuret method Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 .
  • the enzymes exhibit synergistic effects on their action against certain soils or stains, i. 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.
  • Synergism between the protease according to the invention and another enzyme of an agent according to the invention, including in particular between said protease and an amylase and / or a mannanase and / or a lipase.
  • Synergistic effects can occur not only between different enzymes, but also between one or more enzymes and other ingredients of the composition according to the invention.
  • subtilisin type those of the subtilisin type are preferable.
  • subtilisins BPN 'and Carlsberg the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, subtilisin DY and the enzymes thermitase, proteinase K and the subtilases, but not the subtilisins in the narrower sense Proteases TW3 and TW7.
  • Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from Novozymes A / S, Bagsva ⁇ rd, 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 Novozymes, which are available under the trade names, Purafect®, Purafect® OxP, Purafect® Prime, Excellase® and Properase® from Genencor, sold under the tradename Protosol® by Advanced Biochemicals Ltd., Thane, India, under the tradename Wuxi® by Wuxi Snyder Bioproducts Ltd., China, under the names Trade names Proleather® and Protease P® from Amano Pharmaceuticals Ltd., Nagoya, Japan, and the enzyme available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan. Particular preference is also given to using the proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in the international patent applications WO2008 / 086916 and WO2007 / 131656 ,
  • amylases which can be prepared according to the invention are the ⁇ -amylases from Bacillus licheniformis, B. amyloliquefaciens or B. stearothermophilus, and also their further developments improved for use in detergents or cleaners.
  • the B. licheniformis enzyme is available from Novozymes under the name Termamyl® and from Genencor under the name Purastar®ST. Further development products of this ⁇ -amylase are available from Novozymes under the trade names Duramyl® and Termamyl®ultra, from Genencor under the name Purastar®OxAm, and from Daiwa Seiko Inc., Tokyo, Japan, as Keistase®. B.
  • amyloliquefaciens ⁇ -amylase is sold by Novozymes under the name BAN®, and variants derived from B. stearothermophilus ⁇ -amylase under the names BSG® and Novamyl®, also from Novozymes.
  • the ⁇ -amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from B. agaradherens (DSM 9948).
  • the amylolytic enzymes belonging to the sequence space of ⁇ -amylases which can be used in the international patent application WO 03/002711 A2 is defined, and the ones in the application WO 03/054177 A2 to be discribed.
  • fusion products of said molecules can be used.
  • lipases or cutinases which can be synthesized according to the invention, which are contained in particular because of their triglyceride-splitting activities, but also in order to generate in situ peracids from suitable precursors, are the lipases which are originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or further developed, 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 which are likewise useful are sold by Amano under the names Lipase CE®, Lipase P®, Lipase B® or Lipase CES®, Lipase AKG®, Bacillis sp. Lipase®, Lipase AP®, Lipase M-AP® and Lipase AML®.
  • Lipases or cutinases can be used, the initial enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii. Further important commercial products are the preparations M1 Lipase.RTM.
  • Lipomax.RTM which were originally sold by Gist-Brocades, and the enzymes marketed by Meito Sangyo KK, Japan, under the name Lipase MY-30®, Lipase OF® and Lipase PL® to mention also the product Lumafast® from the company Genencor.
  • Detergents or cleaning agents according to the invention may also contain cellulases, depending on the purpose, as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components advantageously supplement each other in terms of their various performance aspects.
  • These performance aspects include, in particular, contributions to the primary washing performance, the secondary washing performance of the composition (anti-redeposition effect or grayness inhibition) and softening (fabric effect), up to the exercise of a "stone washed" effect.
  • EG fungal endoglucanase
  • Novozymes under the trade name Celluzyme®.
  • the products Endolase® and Carezyme® which are also available from Novozymes, are based on the 50 kD EG or the 43 kD EG from H. insolens DSM 1800. Further commercial products of this company are Cellusoft®, Renozyme® and Celluclean®. Also usable are, for example, the 20 kD-EG from Melanocarpus available from AB Enzymes, Finland, under the trade names Ecostone® and Biotouch®. Further commercial products of AB Enzymes are Econase® and Ecopulp®.
  • Suitable cellulases are from Bacillus sp. CBS 670.93 and CBS 669.93, those derived from Bacillus sp. CBS 670.93 from the company Genencor under the trade name Puradax® is available.
  • Other commercial products of Genencor are "Genencor detergent cellulase L" and IndiAge®Neutra.
  • Suitable enzymes for this purpose are, for example, under the names Gamanase® and Pektinex AR® from Novozymes, under the name Rohapec® B1 L from AB Enzymes and under the name Pyrolase® from Diversa Corp., San Diego, CA, USA available.
  • the from Bacillus subtilis-derived ⁇ -glucanase is available under the name Cereflo® from Novozymes.
  • Hemicellulases which are particularly preferred 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 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.
  • advantageous systems for enzymatic perhydrolysis can be applied to the applications WO 98/45398 A1 .
  • WO 2005/056782 A2 such as WO 2004/058961 A1 directed.
  • a combined enzymatic bleaching system comprising an oxidase and a perhydrolase describes the application WO 2005/124012 ,
  • organic, particularly preferably aromatic, compounds which interact with the enzymes in order to enhance the activity of the relevant oxidoreductases (enhancers) or to ensure the flow of electrons (mediators) at greatly varying redox potentials between the oxidizing enzymes and the soils.
  • the enzymes used according to the invention are either 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.
  • the purification of the relevant enzymes is conveniently carried out by conventional methods, for example by precipitation, sedimentation, concentration, filtration of the liquid phases, microfiltration, ultrafiltration, exposure to chemicals, deodorization or suitable combinations of these steps.
  • the enzymes can be formulated according to the invention together with accompanying substances, for example from the fermentation or with stabilizers.
  • 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 cleaning textiles or hard surfaces.
  • agents according to the invention can be advantageously used, in particular because of the above-described properties of the contained protease, to eliminate impurities from textiles or from hard surfaces.
  • Embodiments of this subject invention include, for example, hand washing, manual removal of stains from fabrics or hard surfaces, or use in conjunction with a machine process.
  • the respective detergents or cleaning agents according to the invention are provided according to one of the described embodiments.
  • a further subject of the invention are processes for the cleaning of textiles or of hard surfaces, in which at least in one of the process steps an inventive washing or cleaning agent is used.
  • the process for the cleaning of textiles or hard surfaces is accordingly characterized in that in at least one process step an inventive washing or cleaning agent is used.
  • Methods for cleaning textiles are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned in a plurality of process steps and washed off after the action time, or that the items to be cleaned are otherwise treated with a detergent or a solution or dilution of this agent , The same applies to processes for cleaning all other materials than textiles, especially hard surfaces. All conceivable 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.
  • Another object of the invention are methods for the purification of textiles or hard surfaces, which are characterized in that in at least one method step, a protease is catalytically active, which comprises an amino acid sequence corresponding to the in SEQ ID NO. At least 97.5%, and more preferably at least 98%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7 %, 98.8%, 98.9%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9% and most preferably 100% identical, in particular such that the protease in an amount of 40 micrograms to 4 g, preferably from 50 micrograms to 3 g, more preferably from 100 micrograms to 2 g and most preferably from 200 micrograms to 1 g per application is used. All facts, objects and embodiments described for washing or cleaning agents according to the invention are also applicable to this
  • a single and / or the sole step of such a method may be that, if desired, alone cleaning-active component such a protease is brought into contact with the soiling, preferably in a buffer solution or in water.
  • Alternative embodiments of this subject matter of the invention are also processes for the treatment of textile raw materials or for textile care, in which in at least one process step a protease used in agents according to the invention becomes active.
  • a protease used in agents according to the invention becomes active.
  • methods for textile raw materials, fibers or textiles with natural components are preferred, and especially for those with wool or silk.
  • These may be, for example, processes in which materials for processing in textiles are prepared, for example for anti-fungal finishing, or, for example, for processes which enrich the cleaning of worn textiles with a nourishing component.
  • processes in which materials for processing in textiles are prepared for example for anti-fungal finishing, or, for example, for processes which enrich the cleaning of worn textiles with a nourishing component.
  • they are processes for the treatment of textile raw materials, fibers or textiles with natural constituents, in particular with wool or silk.
  • Proteases used in compositions according to the invention can advantageously be used in detergents and cleaners according to the invention and processes, in particular washing and cleaning processes, in accordance with the above statements. They can therefore be used to remove proteinaceous or protease-sensitive stains from textiles or hard surfaces.
  • a further subject of the invention is therefore the use of a protease which comprises an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. At least 97.5%, and more preferably at least 98%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7 %, 98.8%, 98.9%, 99%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9% and most preferably 100% identical, for cleaning textiles or hard surfaces.
  • the protease is used in an amount of from 40 ⁇ g 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.
  • All facts, objects and embodiments described for washing or cleaning agents according to the invention are also applicable to this subject of the invention. 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 relevant enzymes are provided in the context of a washing or cleaning agent according to the invention.
  • proteolytically active bacterial strain 0.1 g of a soil sample were suspended in 1 ml sterile 0.9% NaCl solution and on agar plates containing milk powder (1.5% agar, 0.1% K 2 HPO 4 , 0.5% yeast extract, 1% peptone, 1% Milk powder, 0.02% MgSO 4 .7H 2 O, 0.4% Na 2 CO 3 , pH 10) and incubated at 30 ° C.
  • a proteolytically active bacterium was isolated on the basis of a clarification laboratory, which was identified by the German Collection of Microorganisms and Cell Cultures (DSMZ) as Bacillus pumilus (ID 08-101).
  • the proteolytically active bacterium was cultured in TBY medium (0.5% NaCl, 0.5% yeast extract, 1% tryptone, pH 7.4) for 16 h at 30 ° C.
  • the total DNA of this bacterium was prepared by standard methods, treated with the restriction enzyme Sau 3A and transferred to a Bacillus vector (derivative of pBC16; Bernhard et al. (1978), J. Bacteriol., Vol. 133 (2), p. 897 et seq. ) cloned.
  • This vector was inserted into the protease-negative host strain Bacillus subtilis DB 104 ( Kawamura and Doi (1984), J. Bacteriol., Vol. 160 (1), pp. 442-444 ).
  • the transformants were first regenerated on DM3 medium and then seeded on milk powder agar plates (TBY Skimmilk plates, see Example 1). Proteolytically active clones were identified by their lysis sites. One of the resulting proteolytically active clones was selected, the plasmid (vector) of which was isolated and the gene fragment (insert) contained in this vector was sequenced by standard methods.
  • the insert contains an approximately 1.2 kb open reading frame whose DNA sequence encodes a subtilisin-type protease.
  • the sequence was amplified by PCR, cloned in the E. coli vector pUC19 and deposited under the Budapest Treaty with the DSMZ under the number DSM 21890.
  • the control detergent used was a detergent base formulation of the following composition (all figures in percent by weight): 0.3- 0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerol , 0.3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% nonionic surfactants, 1% boric acid, 1-2% sodium citrate (dihydrate), 2-4% soda, 14-16% Coconut fatty acids, 0.5% HEDP (1-hydroxyethane- (1,1-di-phosphonic acid)), 0-0.4% PVP (polyvinyl pyrrolidone), 0-0.05% optical brightener, 0-0.001% dye , Rest demineralized water.
  • xanthan gum 0.2-0.4% anti-foaming agent
  • 6-7% glycerol 0.3-0.5% ethanol
  • FAEOS fatty alcohol ether sulfate
  • nonionic surfactants 1% boric acid, 1-2% sodium citrate (dihydrate),
  • the detergent base formulation was treated with the same activity (5 PE / ml final concentration) with the following proteases for the various test series: protease comprising an amino acid sequence according to SEQ ID NO. 3 (batch 1), protease from Bacillus pumilus according to WO2007 / 131656 (Approach 2) and performance-improved variant F49 of the protease from Bacillus lentus according to WO 95/23221 (Approach 3).
  • a detergent according to the invention shows a better cleaning performance compared to a detergent with a protease from Bacillus pumilus, which has a similar amino acid sequence, and even in comparison with a detergent containing an already performance-enhanced protease variant which is not a wild-type molecule is.

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Claims (10)

  1. Agent de lavage ou de nettoyage comprenant une protéase qui comprend une séquence d'acides aminés qui est identique à la séquence d'acides aminés indiquée dans la SEQ ID NO: 3 à concurrence d'au moins 97,5 % et de manière plus préférée à concurrence d'au moins 98 %, 98,1 %, 98,2 %, 98,3 %, 98,4 %, 98,5 %, 98,6 %, 98,7 %, 98,8 %, 98,9 %, 99 %, 99,1 %, 99,2 %, 99,3 %, 99,4 %, 99,5 %, 99,6 %, 99,7 %, 99,8 %, 99,9 %, et de manière tout particulièrement préférée à concurrence de 100 %, ainsi qu'au moins un constituant d'agent de lavage supplémentaire.
  2. Agent de lavage ou de nettoyage selon la revendication 1, caractérisé en ce que le constituant d'agent de lavage supplémentaire est choisi parmi le groupe constitué par des substances faisant office de builders, des agents tensioactifs, des agents de blanchiment à base de composés de peracides organiques et/ou inorganiques, des activateurs du blanchiment, des solvants organiques miscibles à l'eau, des enzymes, des agents de séquestration, des électrolytes, des régulateurs du pH et d'autres adjuvants tels que des azurants optiques, des inhibiteurs du grisaillement, des régulateurs de mousse ainsi que des colorants et des parfums, de même que leurs combinaisons.
  3. Agent de lavage ou de nettoyage selon l'une quelconque des revendications 1 ou 2, caractérisé en ce qu'il est présent sous forme solide, en particulier sous la forme d'une poudre apte à l'écoulement possédant un poids volumique apparent de 300 g/l à 1200 g/l, en particulier de 500 g/l à 900 g/l.
  4. Agent de lavage ou de nettoyage selon l'une quelconque des revendications 1 ou 2, caractérisé en ce qu'il est présent sous forme liquide, sous la forme d'un gel ou sous la forme d'une pâte.
  5. Agent de lavage ou de nettoyage selon l'une quelconque des revendications 1 à 4, caractérisé en ce que la protéase est enrobée d'une substance imperméable pour la protéase à la température ambiante et/ou en l'absence d'eau.
  6. Agent de lavage ou de nettoyage selon l'une quelconque des revendications 1 à 5, caractérisé en ce qu'il comprend au moins une enzyme supplémentaire, en particulier une protéase, une amylase, une cellulase, une hémicellulase, une mannanase, une tannase, une xylanase, une xanthanase, une β-glucosidase, une carraghénase, une perhydrolase, une oxydase, une oxydoréductase ou une lipase, ainsi que, de préférence leurs mélanges.
  7. Utilisation d'un agent de lavage ou de nettoyage selon l'une quelconque des revendications 1 à 6 pour l'élimination de saletés sensibles aux protéases sur des textiles ou sur des surfaces dures.
  8. Procédé pour le nettoyage de textiles ou de surfaces dures, caractérisé par le fait que, dans au moins une étape opératoire, on utilise un agent de lavage ou de nettoyage selon l'une quelconque des revendications 1 à 6.
  9. Procédé pour le nettoyage de textiles ou de surfaces dures, caractérisé par le fait que, dans au moins une étape opératoire, une protéase est active du point de vue catalytique, qui comprend une séquence d'acides aminés qui est identique à la séquence d'acides aminés indiquée dans la SEQ ID NO: 3 à concurrence d'au moins 97,5 % et de manière plus préférée à concurrence d'au moins 98 %, 98,1 %, 98,2 %, 98,3 %, 98,4 %, 98,5 %, 98,6 %, 98,7 %, 98,8 %, 98,9 %, 99 %, 99,1 %, 99,2 %, 99,3 %, 99,4 %, 99,5 %, 99,6 %, 99,7 %, 99,8 %, 99,9 %, et de manière tout particulièrement préférée à concurrence de 100 %, en particulier de telle sorte que l'on met en oeuvre la protéase en une quantité de 40 µg à 4 g, de préférence de 50 µg à 3 g, de manière particulièrement préférée de 100 µg à 2 g et de manière tout particulièrement préférée de 200 µg à 1 g par utilisation.
  10. Utilisation d'une protéase qui comprend une séquence d'acides aminés qui est identique à la séquence d'acides aminés indiquée dans la SEQ ID NO: 3 à concurrence d'au moins 97,5 % et de manière plus préférée à concurrence d'au moins 98 %, 98,1 %, 98,2 %, 98,3 %, 98,4 %, 98,5 %, 98,6 %, 98,7 %, 98,8 %, 98,9 %, 99 %, 99,1 %, 99,2 %, 99,3 %, 99,4 %, 99,5 %, 99,6 %, 99,7 %, 99,8 %, 99,9 %, et de manière tout particulièrement préférée à concurrence de 100 %, pour le nettoyage de textiles ou de surfaces dures, en particulier de telle sorte que l'on met en oeuvre la protéase en une quantité de 40 µg à 4 g, de préférence de 50 µg à 3 g, de manière particulièrement préférée de 100 µg à 2 g et de manière tout particulièrement préférée de 200 µg à 1 g par utilisation.
EP09756715.0A 2008-11-27 2009-11-16 Produits nettoyants et détergents contenant des protéases de bacillus pumilus Not-in-force EP2358858B1 (fr)

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DE102008059447A1 (de) 2010-06-02
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EP2358858A2 (fr) 2011-08-24
PL2358858T3 (pl) 2014-10-31
WO2010060821A3 (fr) 2010-07-29
US20110230384A1 (en) 2011-09-22
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