WO2009021867A2 - Agents containing proteases - Google Patents

Abstract

The invention relates to agent compositions, particularly detergents and cleaning agents, comprising a first protease of the “BLAP” type and a second protease of the “alkaline protease from Bacillus gibsonii (DSM 14391)” type. The invention further relates to cleaning methods, in which said agents are used, to the use of said agents, and to cleaning methods and the use of said proteases.

Description

 Agents containing proteases

The invention relates to middle compositions, in particular detergents and cleaners, containing a first protease and a second protease. Furthermore, the invention relates to purification processes in which these agents are used, uses of these agents and purification processes and uses of these proteases.

Proteases are among the most technically important enzymes of all. Of these, in turn, proteases of the subtilisin type (subtilases, subtilopeptidases, EC 3.4.21.62) are particularly important, which are attributed to the serine proteases due to the catalytically active amino acids. They act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are internal to peptides or proteins. Their pH optimum is usually in the clearly alkaline range. For an overview of this family, see for example the article "Subtilases: Subtilisin-like Proteases" by R. Siezen, pages 75-95 in "Subtilisin enzymes", edited by R. Bott and C. Betzel, New York, 1996. Subtilases become natural formed by microorganisms; Of these, in particular, the subtilisins formed and secreted by Bacillus species are to be mentioned as the most important group within the subtilases.

Proteases are, in addition to other enzymes, established active ingredients of detergents and cleaners. They cause the breakdown of protein-containing stains on the items to be cleaned. At best, there are synergies between the enzymes and the remaining components of the funds concerned. Among the detergent and detergent proteases subtilases occupy an outstanding position due to their favorable enzymatic properties such as stability or pH optimum. They are also suitable for a variety of other technical uses, for example as components of cosmetics or in the organic-chemical synthesis.

Examples of the subtilisin-type proteases preferably used in detergents and cleaners are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, subtilisin DY and those the subtilases, but no longer Enzymes Thermitase, Proteinase K, and Proteases TW3 and TW7, which can be classified as subtilisins in the narrower sense.

The subtilisin BPN ', which is derived from Bacillus amyloliquefaciens, or B. subtilis, is known from the work of Vasantha et al. (1984) in J. Bacteriol., Volume 159, pp. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume 11, pp. 7911-7925. Subtilisin BPN 'is used in particular with regard to the numbering of the positions as reference enzyme of Subtilisins. Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from Novozymes A / S, Bagsvaerd, Denmark. It is described in the publications of EL Smith et al. (1968) in J. Biol. Chem., Volume 243, pp. 2184-2191, and Jacobs et al. (1985) in Nucl. Acids Res., Vol. 13, pp. 8913-8926 and is naturally produced by Bacillus licheniformis. The protease PB92 is naturally derived from the alkaliphilic bacterium Bacillus nov. spec. 92 and was available under the trade name Maxacal® from Gist-Brocades, Delft, The Netherlands. In its original sequence, it is described in the patent application EP 283075 A2. The subtilisins 147 and 309 are sold under the trade names Esperase®, and Savinase® by the company Novozymes. They are originally from Bacillus strains, which are disclosed in the application GB 1243784 A. The protease from Bacillus lentus DSM 5483 (WO 91/02792 A1) is derived from the variants described under the name BLAP®, which are described in particular in WO 92/21760 A1, WO 95/23221 A1, WO 02/088340 A2 and WO 03 / 038082 A2. Subtilisin DY is originally from Nedkov et al. Chem., 1985, Biol. Chem. Hoppe-Seyler, Vol. 366, pp. 421-430. Further useful 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.

The proteases used in the compositions according to the invention are either originally derived from microorganisms, for example from microorganisms of 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.

Complex protein soiling or residues make high demands on the protease contained in the respective agent. For example, soils are not completely or satisfactorily removed by a protease contained in the agent. Also, other contaminant ingredients may decrease the performance of a protease. In order to improve the performance of agents, in particular detergents and cleaners, with regard to their proteolytic activity, it is for example attempted to obtain novel proteases having advantageous properties, for example by removing microorganism-containing samples from natural habitats and under the conditions regarded as suitable - for example, in an alkaline medium - to cultivate. It is also possible to optimize proteases by mutagenesis methods known per se for use in the respective compositions, in particular detergents and cleaners. These include point mutagenesis, deletion, insertion or fusion with other proteins or protein parts or other, in particular chemical modifications. For example, this changes the surface charges and / or the isoelectric point of the molecules and above their interactions with the substrate or increases the stability of the proteases in question and thus their effectiveness. However, the further development possibilities of the proteases which can be used in corresponding agents have the disadvantage that they are complex and time-consuming.

With regard to the use of proteases in detergents and cleaning agents it is known that proteases can be used to improve the washing or cleaning performance together with other enzymes, for example amylases, cellulases, hemicellulases, mannanases, β-glucosidases, oxidases, oxidoreductases or lipases. Likewise, the use of proteases in detergents in combination with other active ingredients such as bleaching agents or soil release agents is known in the art. It is further known from the prior art that corresponding agents, in particular washing and cleaning agents, may contain a plurality of proteases. For example, International Patent Application WO 03/054185 A1 discloses that the Bacillus gibsonii alkaline protease (DSM 14391) can be used in an appropriate composition together with further proteases. However, this application as well as the further prior art contains no indication as to which specific proteases this enzyme is advantageously to be combined in order to achieve a synergistic interaction of the proteases in a corresponding agent.

Surprisingly, it has been found that the performance of agents, in particular detergents and cleaners, is significantly improved with regard to their proteolytic activity, if mixtures of at least two specific proteases with different activity spectrum and / or different sequence are used in these agents. With regard to the interaction of these particular, different proteases results in a synergistic effect, ie a better performance compared to the individual performances of the respective protease in one-component systems (ie agents that contain only each of these proteases) and also to the sum of Individual performances of the proteases, ie the sum of, for example, two one-component systems. Thus, the selected combination of particular proteases is another way to improve the performance of agents, especially detergents, with regard to their proteolytic activity. It is therefore an object of the present invention to provide agents which have improved proteolytic activity.

Relatedly, another object of the present invention is to provide means having improved detergency performance relative to at least one proteinaceous soiling, preferably with respect to multiple proteinaceous soils.

Another particular object of the present invention is to provide agents which have at least a constant, preferably improved, washing or cleaning performance with respect to at least one proteinaceous soiling, preferably with respect to a plurality of proteinaceous soils, but a reduced content Protease enzyme have.

This object is achieved according to the teaching of claim 1 by the provision of agents containing mixtures of proteases with different activity spectra or different sequence. In these compositions according to the invention, the proteases contained develop a synergistic cleaning performance, so that the agents effect a better removal of proteinaceous soils compared to agents containing either only one protease type or compared to the expected cleaning performance of a two-protease agent due to mere addition the jewiligen individual contributions of the contained proteases to the cleaning performance of the agent. Thus, the selected combination of such proteases constitutes an essential aspect of the invention which has a synergistic effect on the removal of proteinaceous residues or soils in compositions of the invention.

An object of the invention thus represent means comprising a first protease and a second protease, which are characterized in that the first protease is selected from a) a protease comprising an amino acid sequence corresponding to the amino acid sequence given in SEQ ID NO.1 at least 80% identical; b) a protease comprising an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2; c) a protease which comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2 and additionally has at least one additional amino acid in comparison with SEQ ID NO. 2; and the second protease comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO.3. It has surprisingly been found that in particular the combination of a protease, as defined above under a) to c) (hereinafter collectively referred to as "BLAP-type protease" or as the first protease) with a protease corresponding to the one described in SEQ ID NO.3 indicated amino acid sequence is at least 80% identical (hereinafter referred to as protease of the type "alkaline protease from Bacillus gibsonii (DSM 14391)" or second protease), in an agent according to the invention leads to a synergistic cleaning performance of the two proteases. The synergistic effect of these two types of proteases in an agent according to the invention is based on the fact that the effects of the first and the second protease complement one another in such a way that an overall increased proteolytic effect is achieved. This can be made possible, for example, by the fact that the proteolytic cleavage of peptide bonds by the first protease makes substrates for the second protease more accessible and, in turn, further substrates for the first protease become accessible by the proteolytic cleavage of the peptide bonds by the second protease. Especially with complex protein-containing substrates, the accessibility of a cleavage site for a protease is often a limiting factor. A different spectrum of action of the two proteases therefore shows, for example, in a different substrate specificity. Likewise, a different spectrum of action may be caused by a different proteolytic activity under defined conditions, in particular with regard to temperature, pH, ionic strength, stability towards oxidizing compounds (for example bleaching agents), etc.

A synergism according to the invention therefore occurs when the first protease differs from the second protease. These differences manifest themselves in the amino acid sequence of the respective proteolytically active enzyme. As for the first protease, it is preferably selected from

a) a protease which comprises an amino acid sequence which is more preferably at least 82.5%, 85%, 87.5%, 90%, 91%, 92%, 93% to the amino acid sequence given in SEQ ID NO.1, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% and most preferably 100% identical. b) a protease comprising an amino acid sequence which is more preferably at least 82.5%, 85%, 87.5%, 90%, 91%, 92%, 93%, of the amino acid sequence given in SEQ ID NO. 94%, 95%, 96%, 97%, 98%, 99%, 99.5% and most preferably 100% identical. c) a protease comprising an amino acid sequence which is more preferably at least 82.5%, 85%, 87.5%, 90%, 91%, 92%, 93% to the amino acid sequence given in SEQ ID NO. Is 94%, 95%, 96%, 97%, 98%, 99%, 99.5% and most preferably 100% identical and has at least one additional amino acid compared to SEQ ID NO.2. In a further preferred embodiment of the invention, the agent is characterized in that the additional amino acid of the first protease is inserted after one of the following positions in the counting manner according to SEQ ID NO.2: 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 95, 96, 97, 98, 99, 100, 101, 102, 103, 125, 126, 127, 126, 129, 130, 131, 132, 153, 154, 155, 156, 157, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 173, 181, 182, 183, 184, 185, 186, 187, 188, 189, 190, 191, 192, 193, 194, 195, 202, 203, 204, 218, 219. For different proteases, which are used according to the invention as the first protease in an agent, have a corresponding insertion of at least one amino acid or of a plurality of amino acids, preferably at one or more of said positions on. This applies, for example, proteases, which are described in the European patent application EP 1 032 655. These have, for example, at least one additional amino acid in the counting method according to SEQ ID NO. 2 (that is to say in the counting method of Savinase®, referred to in the named application as BLSAVI), in positions 33 to 43, 95 to 103, 125 to 132 , 153 to 173, 181 to 195, 202 to 204 and / or position 218 to 219. Further proteases which have an insertion of at least one amino acid and can be used according to the invention as the first protease, are derived from the international patent application WO 00/37599 and the international patent application WO 01/44452.

With regard to the second protease, which is combined in means according to the invention with the first protease, the agent is characterized in that the second protease comprises an amino acid sequence which is more preferably at least 82.5% to the amino acid sequence given in SEQ ID NO. 85%, 87.5%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5%, and most preferably 100% identical is. As already mentioned above, a synergistic proteolytic performance of a composition according to the invention is found, in particular, when a first protease of the BLAP type is combined with a second protease of the type "alkaline protease from Bacillus gibsonii (DSM 14391)." One such protease was obtained from Bacillus gibsonii (DSM 14391) and is described in International Publication WO 03/054185 A1, the disclosure content of which is expressly incorporated into the present patent application.

For the purposes of the present application, an enzyme is to be understood as meaning a protein which has a specific biocatalytic function. For the purposes of the present application, protease is understood as meaning an enzyme which catalyzes the hydrolysis of peptide bonds and is thereby able to cleave peptides or proteins.

For the purposes of the present application, a protein is a largely linear composition composed of the natural amino acids and usually performs one of its functions three-dimensional structure accepting polypeptide. A peptide consists of amino acids that are covalently linked to each other via peptide bonds. The term polypeptide clarifies in this regard the fact that this peptide chain usually consists of many amino acids, which are connected to each other via peptide bonds. Amino acids may be in an L and a D configuration, with the amino acids that make up proteins in the L configuration. They are called proteinogenic amino acids. In the present application, the proteinogenic, naturally occurring L-amino acids are designated by the internationally used 1- and 3-letter codes. Numerous proteins are formed as so-called pre-proteins, ie together with a signal peptide. By this is meant the N-terminal part of the protein, the function of which is usually to ensure the discharge of the protein formed from the producing cell into the periplasm or the surrounding medium and / or its correct folding. Subsequently, the signal peptide is cleaved under natural conditions by a signal peptidase from the rest of the protein, so that this exerts its actual catalytic activity without the initially present N-terminal amino acids. Pro-proteins are inactive precursors of proteins. Their signal sequence precursors are referred to as pre-pro proteins. For technical applications, due to their enzymatic activity, the mature, ie mature, peptides, ie the enzymes processed after their preparation, are preferred over the preproteins. The SEQ ID NO. 1, SEQ ID NO. 2 and SEQ ID NO. The sequences can therefore be modified from the cells producing them after the 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 protein.

By 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.

Such a comparison is accomplished by associating similar sequences in the nucleotide or amino acid sequences of the proteins of interest. This is called homologization. A tabular assignment of the respective positions is referred to as alignment. In the analysis of nucleotide sequences, in turn, both complementary strands and all three possible reading frames are to be taken into account; as well the degeneracy of the genetic code and the organism specific use of the codons (Codon usage). Meanwhile, alignments are created using computer programs, such as the algorithms FASTA or BLAST; This procedure is described, for example, by DJ Lipman and WR Pearson (1985) in Science, Vol. 227, pp. 1435-1441.

All carried out in the present application sequence comparisons and determinations of homology and / or identity values were performed using the computer program Vector NTI ^® Suite 7.0, available from InforMax, Inc., Bethesda, USA with the preset default parameters.

A summary of all matching positions in the compared sequences is called a consensus sequence.

Such a comparison also allows a statement about the similarity or homology of the compared sequences to each other. This is represented in percent identity, that is the proportion of identical nucleotides or amino acid residues at the same or in an alignment corresponding positions. A broader concept of homology includes the conserved amino acid substitutions in this value. It then speaks of percent similarity. Such statements can be made about whole proteins or genes or only over individual areas.

Homologous regions of different proteins are defined by matches in amino acid sequence. These can also be identified by identical function. It goes as far as complete identities in the smallest areas, so-called boxes, which contain only a few amino acids and usually perform essential functions for the overall activity. The functions of the homologous regions are to be understood as the smallest partial functions of the function carried out by the entire protein, such as, for example, the formation of individual hydrogen bonds for the complexation of a substrate or transition complex.

Proteases or enzymes in general can be prepared by various methods, e.g. targeted genetic modification by mutagenesis, further developed and optimized for specific uses or specific properties such as catalytic activity, stability, etc.

It is furthermore generally known from the prior art that advantageous properties of individual mutations, for example individual point mutations, can complement one another. A protease already optimized with regard to certain properties, for example with regard to its properties Stability to surfactants or other components can be further developed according to the invention.

Fragments are understood as meaning all proteins or peptides which are smaller than natural proteins and, for example, can be obtained synthetically. Due to their amino acid sequences, they can be assigned to the relevant complete proteins. For example, they may adopt the same structures or perform proteolytic or partial activities, such as the complexation of a substrate. Fragments and deletion variants of starting proteins are in principle similar; while fragments tend to be smaller fragments, the deletion mutants tend to lack only short regions, and thus only individual subfunctions.

For the purposes of the present application, chimeras or hybrid proteins are to be understood as meaning those proteins whose sequence comprises the sequences or partial sequences of at least two starting proteins. The source proteins may be derived from different or from the same organism. Chimeric or hybrid proteins may be obtained, for example, by recombinant mutagenesis. For example, the purpose of such recombination may be to induce or modify a particular enzymatic function using the fused protein portion. For the purposes of the present invention, it is irrelevant whether such a chimeric protein consists of a single polypeptide chain or several subunits on which different functions can be distributed.

By proteins obtained by insertion mutation are meant those variants obtained by inserting a protein fragment into the starting sequences. They are due to their principle similarity to the chimeric proteins. They differ from those only in the size ratio of the unchanged protein part to the size of the entire protein. In such insertionsmutierten proteins, the proportion of foreign protein is lower than in chimeric proteins.

Inversion mutagenesis, ie a partial sequence reversal, can be regarded as a special form of both the deletion and the insertion. The same applies to a new grouping of different parts of the molecule which deviates from the original amino acid sequence. It can be regarded as a deletion variant, as an insertion variant, as well as a shuffling variant of the original protein. For the purposes of the present application, derivatives are understood as meaning those proteins whose pure amino acid chain has been chemically modified. Such derivatizations can be carried out, for example, biologically in connection with protein biosynthesis by the host cell. For this molecular biological methods can be used. However, they can also be carried out chemically, for example by the chemical transformation of a side chain of an amino acid or by covalent binding of another compound to the protein. Such a compound may, for example, also be other proteins which are bound, for example via bifunctional chemical compounds, to proteins according to the invention. Such modifications may, for example, affect the substrate specificity or binding strength to the substrate or cause a temporary blockage of the enzymatic activity when the coupled substance is an inhibitor. This can be useful, for example, for the period of storage. Also, derivatization is understood to mean covalent attachment to a macromolecular carrier, as well as noncovalent inclusion in suitable macromolecular cage structures.

In a further embodiment of the invention, the agent is thus characterized in that the first protease is present in the agent as fragment, deletion variant, chimeric protein or derivative and / or the second protease is present in the agent as a fragment, deletion variant, chimeric protein or derivative, wherein the first and second proteases are still catalytically active.

For the purposes of the present invention, all enzymes, proteins, fragments, chimeric proteins and derivatives, unless they need to be addressed explicitly as such, are summarized under the generic term proteins.

Compositions according to the invention include all types of agents, in particular mixtures, formulations, solutions, etc., whose applicability is improved by addition of the proteases described above. Depending on the field of application, these may be, for example, solid mixtures, for example powders with freeze-dried or encapsulated proteins, or gel or liquid agents. Preferred formulations contain, for example, buffer substances, stabilizers, reaction partners and / or cofactors of the proteases and / or other ingredients synergistic with the proteases. In particular, this appropriation is to be understood as the areas of application set out below. Further fields of application emerge from the prior art and are described, for example, in the manual "Industrial Enzymes and their Applications" by H. Uhlig, Wiley-Verlag, New York, 1998. In preferred embodiments of the invention, an agent according to the invention is characterized in that it comprises a detergent, hand washing detergent, dishwashing detergent, hand dishwashing detergent, machine dishwashing detergent, cleaning agent, denture or contact lens care agent, rinse aid, disinfectant, cosmetic agent, pharmaceutical agent or a means for treating filter media, textiles , Furs, paper, skins or leather, especially a laundry detergent or dishwashing detergent.

This invention includes all conceivable types of detergents or cleaners, both concentrates and undiluted agents to be used on a commercial scale, in the washing machine or in hand washing or cleaning. These include, for example, detergents for textiles, carpets, or natural fibers, for which according to the present invention the term laundry 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 such according to the present invention, the term cleaning agent is used.

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 detergents or cleaning agents according to the invention, which may be in the form of homogeneous solutions or suspensions, especially in powdered solids, may contain, in addition to the active ingredient used according to the invention - a protease combination according to the invention - in principle all known and conventional ingredients in such agents, wherein at least another 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.

In particular, a combination of the protease combination with one or more other ingredients of the compositions proves to be advantageous since such an agent has an improved cleaning performance by resulting synergisms, in particular between a protease or the protease combination and the further ingredient. This means that the agent provides improved removal of stains, such as proteinaceous Stains caused in comparison with an agent which either contains only one of the two components, or even compared to the expected cleaning performance of an agent with both components due to the mere addition of the respective individual contributions of these two components to the cleaning performance of the agent. Such a synergism is achieved, in particular, by the combination of a protease or protease combination according to the invention with one of the surfactants and / or builders and / or bleaches described below.

The 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. Furthermore, corresponding ethoxylation and / or propoxylation of N-alkyl-amines, 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. In particular, however, 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. Preferred ethoxylated alcohols include, for example, Ci ₂ - C ₄ alcohols containing 3 EO or 4 EO, C ₉ -C i-alcohols containing 7 EO, C ₃ -C ₅ alcohols containing 3 EO, 5 EO, 7 EO or 8 EO, Ci ₂ -Ci ₈ alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of Ci ₂ -Ci ₄ alcohol with 3 EO and Ci ₂ -Ci ₈ 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 rank ethoxylates, NRE). In addition to these nonionic surfactants, 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. In particular, agents for use in mechanical processes usually extremely low-foam compounds are used. These preferably include C ₂ -C ₈ -Alkylpolyethylenglykol- polypropylene glycol ethers, each containing up to 8 moles of ethylene oxide and propylene oxide units in the molecule. However, it is also possible to use other known low-foam nonionic surfactants, such as, for example, C 1 -C 6 -alkylpolyethyleneglycol-polybutylene glycol ethers having up to 8 mol of ethylene oxide and butylene oxide units in the molecule and end-capped alkylpolyalkylene glycol mixed ethers. Also particularly preferred are the hydroxyl-containing alkoxylated alcohols, as described in European Patent Application EP 0 300 305, so-called hydroxy 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. Also suitable are polyhydroxy fatty acid amides of the formula (III) in which R ¹ CO is an aliphatic acyl radical having 6 to 22 carbon atoms, R ^{2 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:

R ²

R ¹ -CO-N- [Z] (III)

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 ⁴ -OR ⁵ I (IV)

R ³ -CO-N- [Z]

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 dC 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 this rest stands. [Z] is also here preferably by reductive amination of a sugar such as glucose, fructose, maltose, lactose, galactose, mannose or Get 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. Another class of preferred 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. The amount of these nonionic surfactants is preferably not more than that of the ethoxylated fatty alcohols, especially not more than half thereof. Other suitable 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. Thus, 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. However, it is also possible to use gemini-polyhydroxy fatty acid amides or poly-polyhydroxy fatty acid amides. Also suitable are the Schwefelsäuremonoester the ethoxylated with 1 to 6 moles of ethylene oxide, linear or branched C ₇ -C ₂ i-alcohols such as 2-methyl-branched C ₉ -CN alcohols containing on average 3.5 mol ethylene oxide (EO) or C ₂ - Ci ₈ fatty alcohols 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 the monoesters and / or diesters of sulfosuccinic acid with 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 particularly important prefers. Likewise, it is also possible to use 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). Particularly preferred are the sarcosides or the sarcosinates and here especially sarcosinates of higher and optionally monounsaturated or polyunsaturated fatty acids such as oleyl sarcosinate. As further 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, including soaps, 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 methylglycine diacetic 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) carboxylic acids, in particular the accessible by oxidation of polysaccharides or dextrins polycarboxylates, polymeric acrylic acids, methacrylic acids, maleic acids and copolymers thereof, which also small amounts of polymerizable substances without carboxylic acid functionality may contain polymerized. 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 the Acrylic acid or methacrylic acid with vinyl ethers, such as vinylmethyl ethers, vinyl esters, ethylene, propylene and styrene, in which the proportion of the acid is at least 50% by weight. It is also possible to use terpolymers which contain two unsaturated acids and / or salts thereof as monomers and also vinyl alcohol and / or an esterified vinyl alcohol or a carbohydrate as the third monomer as water-soluble organic builder substances. 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 substituted in the 2-position with 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.

If desired, such 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. Examples of these are trisodium phosphate, tetra sodium diphosphate, disodium dihydrogen diphosphate, pentasodium triphosphate, so-called sodium hexametaphosphate, oligomeric trisodium phosphate with degrees of oligomerization of from 5 to 1000, in particular from 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. used. Among these, preferred are the 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) , Amounts near the above upper limit are preferably used in solid, particulate agents. In particular, 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. Your calcium binding capacity, which can be determined according to the specifications of German Patent DE 24 12 837, is 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 according to the invention preferably have a molar ratio of alkali metal 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 β- and δ-sodium disilicates (Na ₂ Si ₂ O ₅ y H ₂ O) are preferred. Also prepared from 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. In a further preferred embodiment of the composition according to the invention, 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 of 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 XH 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). Of these, especially Na-SKS-5 (OC-Na ₂ Si ₂ O ₅ ), Na-SKS-7 (β-Na ₂ Si ₂ 0 ₅ , natrosilite), Na-SKS-9 (NaHSi ₂ O ₅ 3H ₂ O), Na-SKS-10 (NaHSi ₂ O ₅ 3H ₂ O, kanemite), Na-SKS-11 (t-Na ₂ Si ₂ 0 ₅₎ and Na-SKS-13 (NaHSi ₂ O _5), but especially Na-SKS-6 (5-Na ₂ Si ₂ O ₅ ). In a preferred embodiment of the 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 ,

Builder substances 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.

Suitable peroxygen compounds for use in compositions according to the invention are, in particular, organic peracids or persistent salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and under the washing conditions hydrogen peroxide-releasing inorganic salts, which include perborate, percarbonate, persilicate and / or persulfate such as caroate into consideration. If 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. If 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. The addition of small amounts of known bleach stabilizers such as phosphonates, borates or metaborates and metasilicates and magnesium salts such as magnesium sulfate may be useful.

As 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. Preference is given to 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 and also acetylated sorbitol and mannitol or mixtures thereof (SORMAN), acylated sugar derivatives, in particular pentaacetylglucose (PAG), pentaacetylfruktose, tetraacetylxylose and octaacetyllactose as well as acetylated, optionally N-alkylated glucamine and gluconolactone, and / or N- acylated lactams, for example N-benzoyl-caprolactam. The 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-supplied 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.

In addition to the conventional bleach activators or in their place, sulfone imines and / or bleach-enhancing transition metal salts or transition metal complexes may also be present as so-called bleach catalysts. Among the solvents according to the invention, in particular when they are in liquid or pasty form, 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 -Ato- men, in particular ethylene glycol and propylene glycol, and mixtures thereof and derived from the said classes of compounds ethers. 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.

In order to establish a desired pH, which does not naturally result from the mixture of the other components, the compositions according to the invention may contain 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. Such 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. Also, water-soluble polyamides containing acidic groups are suitable for this purpose. Furthermore, other than the above-mentioned starch derivatives can be used, for example aldehyde starches. Preference is given to using 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. 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 are used instead of the morpholino Group carry a diethanolamino group, a methylamino group, an anilino group or a 2-methoxyethylamino group. Further, 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. In particular, when used in mechanical processes, it may be advantageous to add conventional foam inhibitors to the compositions. As 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. Preferably, the foam inhibitors, in particular silicone and / or paraffin-containing foam inhibitors, are bound to a granular, water-soluble or dispersible carrier substance. In particular, mixtures of paraffins and bistearylethylenediamide are preferred.

In further embodiments of agents according to the invention, in particular detergents or cleaners, the proteases are combined, for example, with one or more of the following ingredients: nonionic, anionic and / or cationic surfactants, (optionally further) bleaches, bleach activators, bleach catalysts, builders and / or cobuilders, Acids, alkaline substances, hydrotropes, solvents, thickeners, sequestering agents, electrolytes, optical brighteners, grayness inhibitors, corrosion inhibitors, in particular silver protectants (silver corrosion inhibitors), disintegration aids, soil release agents, color transfer (or transfer) inhibitors, foam inhibitors, abrasives, Dyes, fragrances, perfumes, antimicrobial agents, UV protectants or absorbents, antistatic agents, pearlescers and skin protection agents, enzymes such as protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthine anase, β-glucosidase, carrageenase, oxidase, oxidoreductase, pectin degrading enzyme or a lipase, stabilizers, especially enzyme stabilizers, and other components known in the art. In a further embodiment of the invention, an agent according to the invention is therefore characterized in that it contains at least one further component selected from the group consisting of surfactants, builders, acids, alkaline substances, hydrotropes, solvents, thickeners, bleaching agents, dyes, perfumes, corrosion inhibitors , Sequestering agents, electrolytes, optical brighteners, grayness inhibitors, silver corrosion inhibitors, color transfer inhibitors, foam inhibitors, disintegration aids, abrasives, UV absorbers, solvents, antistatic agents, pearlescers and skin protection agents.

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. So are usual Temperatures for detergents and cleaning agents in areas of 1O ⁰ C for manual compositions over 4O ⁰ C and 6O ⁰ C to 95 ° for machine agents or industrial applications. Since the temperature is usually infinitely adjustable in modern washing machines and dishwashers, all intermediate stages of the temperature are included. Preferably, the ingredients of the respective agents are coordinated. Synergies in terms of cleaning performance are preferred. Particularly preferred in this regard are synergies resulting from the interaction of the two proteases in the composition according to the invention with at least one or more further ingredients. In a further preferred embodiment, these synergies are present in a temperature range between 2O ⁰ C and 6O ⁰ C, as well as the proteases contained in the inventive compositions are catalytically active in this temperature range.

In a further embodiment, an agent according to the invention, in particular a washing or cleaning agent, further comprises

- 5 wt .-% to 70 wt .-%, in particular 5 wt .-% to 30 wt .-% of surfactants and / or

From 10% by weight to 65% by weight, in particular from 12% by weight to 60% by weight, of water-soluble or water-dispersible inorganic builder material and / or

From 0.5% by weight to 10% by weight, in particular from 1% by weight to 8% by weight, of water-soluble organic builders and / or

0.01 to 15% by weight of solid inorganic and / or organic acids or acid salts and / or

0.01 to 5% by weight complexing agent for heavy metals and / or

0.01 to 5% by weight of grayness inhibitor and / or

0.01 to 5% by weight of color transfer inhibitor and / or

- 0.01 to 5 wt .-% foam inhibitor.

Optionally, the agent may further comprise optical brighteners, preferably from 0.01% to 5% by weight.

The preparation of solid 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 such as, for example, bleaching agents optionally being added separately later. For the preparation of 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.

For the preparation of 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. Particularly in the case of multilayer tablets, it may be advantageous if at least one layer is pre-compressed. This is preferably carried out at pressing forces between 5 and 20 kN, in particular at 10 to 15 kN. This gives fracture-resistant, yet sufficiently rapidly soluble tablets under application conditions with fracture and flexural strengths of normally 100 to 200 N, but preferably above 150 N. Preferably, a tablet produced in this way has a weight of 10 g to 50 g, in particular 15 g up to 40 g. The spatial form of the tablets is arbitrary and can be round, oval or angular, with intermediate forms are also possible. Corners and edges are advantageously rounded. Round tablets preferably have a diameter of 30 mm to 40 mm. In particular, 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 such 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. Of course, means according to the invention may also consist of several phases. In a further embodiment of the invention, the washing or cleaning agent is therefore 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. Alternatively, 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.

In a further embodiment of the invention, the agent, in particular 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 agent according to the invention, in particular washing or cleaning agent, can be packaged in a container, preferably an air-permeable container, from which it is released shortly before use or during the washing process. In particular, at least one, preferably both, of the proteases contained in the agent and / or further ingredients of the agent may be coated with a substance impermeable to the enzyme (s) at room temperature or in the absence of water, which under application conditions of the agent is permeable to the enzyme / the enzymes becomes. Such an embodiment of the invention is therefore characterized in that at least one protease is coated with a substance that is impermeable to the protease at room temperature or in the absence of water.

Preferably, an agent according to the invention is characterized in that it contains the proteases in an amount of from 0.1 μg to 100 mg, preferably from 1 μg to 50 mg, more preferably from 10 μg to 50 mg, particularly preferably from 25 μg to 25 mg and most preferably from 50 μg to 20 mg per g of the agent. Thus, given in weight percent, the agent contains the proteases in an amount of 0.00001 weight percent to 10 weight percent, preferably 0.0001 weight percent to 5 weight percent, more preferably 0.001 weight percent to 5 weight percent, most preferably 0.00025 weight percent to 2.5 Percent by weight and most preferably from 0.005% to 2% by weight. The quantities shown contain the first protease and the second protease.

Compositions according to the invention may contain exclusively the two proteases described above. Alternatively, they may also contain other proteases 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. As other enzymes preferably used are all enzymes that can develop a catalytic activity in the agent of the invention, in particular proteases, amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, ß-glucosidases, carrageenases, oxidases, oxidoreductases, pectin-degrading Enzymes (pectinases) or lipases, 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. Compositions according to the invention preferably contain enzymes in total amounts of 1 × 10 ^-8 to 5 percent by weight, based on active protein. Preferably, the enzymes are from 0.00001 to 5 Wt .-%, more preferably from 0.0001 to 2.5 wt .-%, even more preferably from 0.0001 to 1 wt .-% and particularly preferably from 0.0001 to 0.072 wt .-% in inventive compositions , Wherein each enzyme contained can be present in the stated proportions.

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 further enzymes particularly preferably support the effect of the agent, for example the cleaning performance of a washing or cleaning agent, with regard to certain stains or stains. Most preferably, 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. 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. In a further preferred embodiment of the invention, the agent according to the invention is therefore characterized in that it contains at least one further enzyme which comprises a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, β-glucosidase, carrageenase, oxidase, oxidoreductase , Pectin degrading enzyme or lipase.

When comparing the performance of two enzymes, a distinction must be made between protein-like and activity-like use. Particularly in the case of genetically engineered, largely side-activity-free preparations, the use of the same protein is appropriate. Because this is a statement on whether the same amounts of protein - for example, as a measure of the yield of a fermentative production - lead to comparable results. If the respective ratios of active substance to total protein (the values of the specific activity) diverge, then an activity-equivalent comparison is recommended because this compares the respective enzymatic properties. In general, a low specific activity can be compensated by adding a larger amount of protein. This is ultimately an economic consideration.

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) accordingly.

The enzymes used in the compositions according to the invention are either originally derived from microorganisms, for example the genera Bacillus, Streptomyces, Humicola or Pseudomonas, and / or are prepared by suitable biotechnological processes Microorganisms produced, for example, by transgenic expression hosts of the genera Bacillus or by filamentous fungi.

A separate subject of the invention is the use of an above-described agent according to the invention for the removal of protease-sensitive stains on textiles or hard surfaces, i. for cleaning textiles or hard surfaces.

For agents according to the invention can be used, in particular in accordance with the properties described above, to remove proteinaceous impurities from textiles or from hard surfaces. Embodiments include, for example, hand washing, manual removal of stains from fabrics or hard surfaces, or use in conjunction with a machine process.

In a preferred embodiment of this use, the relevant agents according to the invention, preferably detergents or cleaning agents, are provided according to one of the above-described embodiments.

A further subject of the invention are processes for the cleaning of textiles or of hard surfaces, in which an agent according to the invention is used at least in one of the process steps. The process for the cleaning of textiles or hard surfaces is accordingly characterized in that an agent according to the invention is used in at least one process step.

This includes both manual and mechanical processes, with mechanical processes being preferred on account of their more precise controllability, for example with regard to the quantities and reaction times 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 of this agent. The same applies to processes for cleaning all other materials than textiles, which are summarized by the term hard surfaces. All conceivable washing or cleaning methods can be enriched in at least one of the method steps by an agent according to the invention, and then represent embodiments of the present invention. Since preferred protease combinations according to the invention naturally already have a protein-dissolving activity and also unfold them in media which otherwise have no cleaning power, for example in bare buffer, a single substep of such a process may be for cleaning, in particular for machine cleaning, textiles or hard surfaces therein If desired, in addition to stabilizing compounds, salts or buffer substances, an enzyme mixture according to the invention is applied as sole cleaning-active component. This represents a particularly simplified embodiment 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 first protease and a second protease are proteolytically active, wherein the first protease is selected from a) a protease, the an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO.1; b) a protease comprising an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2; c) a protease which comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2 and additionally has at least one additional amino acid in comparison with SEQ ID NO. 2; and the second protease comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO.3.

In a preferred embodiment of the method, the first protease is selected from a) a protease which comprises an amino acid sequence which is increasingly preferably at least 82.5%, 85%, 87.5% to the amino acid sequence given in SEQ ID NO. 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5%, and most preferably 100% identical. b) a protease comprising an amino acid sequence which is more preferably at least 82.5%, 85%, 87.5%, 90%, 91%, 92%, 93%, of the amino acid sequence given in SEQ ID NO. 94%, 95%, 96%, 97%, 98%, 99%, 99.5% and most preferably 100% identical. c) a protease comprising an amino acid sequence which is more preferably at least 82.5%, 85%, 87.5%, 90%, 91%, 92%, 93% to the amino acid sequence given in SEQ ID NO. Is 94%, 95%, 96%, 97%, 98%, 99%, 99.5% and most preferably 100% identical and has at least one additional amino acid compared to SEQ ID NO.2. In a further preferred embodiment, the method is characterized in that the additional amino acid of the first protease is inserted in one of the following positions in the counting manner according to SEQ ID NO. 2: 33, 34, 35, 36, 37, 38, 39, 40 , 41, 42, 43, 95, 96, 97, 98, 99, 100, 101, 102, 103, 125, 126, 127, 126, 129, 130, 131, 132, 153, 154, 155, 156, 157 , 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 173, 181, 182, 183, 184, 185, 186, 187, 188, 189 , 190, 191, 192, 193, 194, 195, 202, 203, 204, 218, 219. For different proteases, which are used according to the invention as the first protease in a corresponding method, have a corresponding insertion of at least one amino acid or of a plurality of amino acids, preferably at one or more of said positions on. This applies - as already described above for agents according to the invention - for example for proteases, which are described in the European patent application EP 1 032 655. These have, for example, at least one additional amino acid in the counting method according to SEQ ID NO. 2 (that is to say in the counting method of Savinase®, referred to in the named application as BLSAVI), in positions 33 to 43, 95 to 103, 125 to 132 , 153 to 173, 181 to 195, 202 to 204 and / or position 218 to 219. Further proteases which have an insertion of at least one amino acid and can be used according to the invention as the first protease, are derived from the international patent application WO 00/37599 and the international patent application WO 01/44452.

With regard to the second protease which is combined in the method according to the invention with the first protease, the method is characterized in that the second protease comprises an amino acid sequence which is increasingly preferably at least 82.5% to the amino acid sequence given in SEQ ID NO. 85%, 87.5%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5%, and most preferably 100% identical is.

The proteases are preferably used in an amount of from 40 μg to 4 g, preferably from 50 μg to 3 g, particularly preferably from 100 μg to 2 g and very particularly preferably from 200 μg to 1 g per application. The quantities shown contain the first protease and the second protease.

Further embodiments of this subject matter of the invention are processes for the treatment of textile raw materials or for textile care in which a protease combination according to the invention becomes active in at least one of the process steps.

Among these, 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. Because of the above-described effect of proteases on natural, proteinaceous raw materials, in preferred embodiments, they are processes for the treatment of textile raw materials, fibers or textiles with natural constituents, in particular with wool or silk.

A further inventive subject matter is the use of a first protease and a second protease for the purification of textiles or hard surfaces, characterized in that the first protease is selected from a) a protease comprising an amino acid sequence corresponding to the amino acid sequence shown in SEQ ID NO. 1 amino acid sequence is at least 80% identical; b) a protease comprising an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2; c) a protease which comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2 and additionally has at least one additional amino acid in comparison with SEQ ID NO. 2; and the second protease comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO.3.

Because combinations of proteases according to the invention can be used, in particular because of the properties described above, to eliminate proteinaceous impurities from textiles or from hard surfaces. Embodiments include, for example, hand washing, manual removal of stains from fabrics or hard surfaces, or use in conjunction with a machine process. In a preferred embodiment of this use, the subject combinations of proteases of this invention are provided according to any of the above recipes.

In a preferred embodiment of this use, the first protease is selected from a) a protease which comprises an amino acid sequence which is more preferably at least 82.5%, 85%, 87.5% to the amino acid sequence given in SEQ ID NO. 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5%, and most preferably 100% identical. b) a protease which comprises an amino acid sequence which is more preferably at least 82.5%, 85%, 87.5% to the amino acid sequence given in SEQ ID NO. 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5%, and most preferably 100% identical. c) a protease comprising an amino acid sequence which is more preferably at least 82.5%, 85%, 87.5%, 90%, 91%, 92%, 93% to the amino acid sequence given in SEQ ID NO. Is 94%, 95%, 96%, 97%, 98%, 99%, 99.5% and most preferably 100% identical and has at least one additional amino acid compared to SEQ ID NO.2.

In a further preferred embodiment, the use is characterized in that the additional amino acid of the first protease is inserted in one of the following positions in the counting manner according to SEQ ID NO.2: 33, 34, 35, 36, 37, 38, 39, 40 , 41, 42, 43, 95, 96, 97, 98, 99, 100, 101, 102, 103, 125, 126, 127, 126, 129, 130, 131, 132, 153, 154, 155, 156, 157 , 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 173, 181, 182, 183, 184, 185, 186, 187, 188, 189 , 190, 191, 192, 193, 194, 195, 202, 203, 204, 218, 219. For different proteases, which are useful according to the invention as the first protease, have a corresponding insertion of at least one amino acid. Examples of such enzymes which have a corresponding insertion are already discussed above in the present application for the agents according to the invention and the methods according to the invention.

With regard to the second protease which is combined in a use according to the invention with the first protease, the use is characterized in that the second protease comprises an amino acid sequence which is increasingly preferably at least 82.5% to the amino acid sequence given in SEQ ID NO. , 85%, 87.5%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% and most preferably 100% is identical.

A preferred use of a combination of proteases according to the invention is characterized in that the proteases are present in an amount of from 40 μg to 4 g, preferably from 50 μg to 3 g, more preferably from 100 μg to 2 g and most preferably from 200 μg to 1 g per application are used. The quantities shown contain the first protease and the second protease.

The following examples serve to further illustrate the invention without, however, limiting it to: Example 1 Synergistic Performance of the Protease Variant S99SD + S99A According to WO 01/44452 and the Alkaline Protease from Bacillus Gibsonii (DSM 14391)

For comparison of inventive mixtures with the prior art, the following frame formulation for a solid machine dishwashing detergent was first prepared:

Ingredient Content [wt%]

Na tripolyphosphate 30-45

Nonionic surfactant 3 - 8

Acrylic acid / sulfonic acid copolymer 5 - 10

Acrylic acid polymer 5-10

Na-percarbonate 8-12

Na carbonate 10 - 15

Amylase granules according to DE 102005062984.9 0.5-1.5

Zinc acetate 0.5-1.5

Proteases (see below)

Water, salts, dyes ad 100%

In such a formulation, the pure enzyme granules and mixtures of the protease disclosed as Subtilase 309 (also referred to as Subtilisin 309 or Savinase®) variant S99SD + S99A are disclosed in international patent application WO 01/44452 (see especially Examples 1 and 2 of WO 01/44452) as a representative of the first protease and the alkaline protease from Bacillus gibsonii (DSM 14391) as a representative of the second protease. The mixture was calculated in proportion to the insertions of the single enzymes. The granules of the alkaline protease from Bacillus gibsonii (DSM 14391) were prepared according to WO 97/40128 A1 and coated according to WO 98/26037 A2.

From the formulations were pressed in a tableting press of Paul-Otto Weber Maschinen + Apparatebau GmbH (Remshalden, Germany) under a pressure of 25 N single-phase tablets. Vessels with hard, smooth surfaces were standardized with an egg / milk soiling (according to SÖFW (Soaps Oils Fat Waxes) Journal 132 3-2006) and rinsed with a commercial household dishwasher, namely at 5O ⁰ C with the normal program of the dishwasher Type Bosch SGS 59 A02. Each rinse used 23 g of rinse each. The water hardness was 21 ° German hardness. The performance was determined as removal of soft sheets according to SÖFW-Journal issue 3-2006, p. 132 (IKW-Arbeitskreis Maschinengeschirrspüimittei: Methods for determining the cleaning performance of automatic dishwashing agents (Part B. updated 2005)). After rinsing, the removal of soiling was determined gravimetrically in percent. That was the difference the weight of the contaminated and subsequently rinsed vessel and the initial weight of the vessel in relation to the weight difference of the non-rinsed vessel to the initial weight set. This relation can be regarded as percent removal. The results obtained are summarized in Table 1 below. Indicated there are the mean values from 9 measurements each.

Table 1: Results of the performance comparison of a mixture of proteases compared to the pure proteases in a machine dishwashing detergent.

By comparing the two approaches 1 and 2 with the approach 3 it is clear that by the proportional combination of the two proteases subtilase 309 - variant S99SD + S99A according to WO 01/44452 and alkaline protease from Bacillus gibsonii (DSM 14391) with a lower enzyme protein content in comparison to test assays with sole subtilase 309 variant S99SD + S99A according to WO 01/44452 or alkaline protease from Bacillus gibsonii (DSM 14391) a significantly better, synergistic performance is obtained.

For a calculation of the expected cleaning performance of a combination of the subtilase 309 variant S99SD + S99A according to WO 01/44452 and alkaline protease from Bacillus gibsonii (DSM 14391), first the respective amounts of total protease are set in relation to each other, whereby a factor of 0 , 52437 (44 mg + 18.4 mg enzyme protein (batch 3) divided by 74 mg enzyme protein (batch 1) + 45 mg enzyme protein (batch 2)). It follows that the theoretical removal of a combination of the subtilase 309 variant S99SD + S99A according to WO 01/44452 and the alkaline protease from Bacillus gibsonii (DSM 14391) (64% + 71%) x 0.52437 = 70.8% is. Compared to this, the actual stock removal is 84%. The comparison of these two values illustrates the presence of a synergistic cleaning performance by the two proteases used.

Example 2: Synergistic Performance of the Bacillus lentus F49 Alkaline Protease and the

Alkaline protease from Bacillus gibsonii (DSM 14391)

For comparison of inventive mixtures with the prior art was first following frame formulation for a solid machine dishwashing detergent prepared:

Ingredient Content [wt%]

Na tripolyphosphate 30-45

Nonionic surfactant 3 - 8

Acrylic acid / sulfonic acid copolymer 5 - 10

Acrylic acid polymer 5-10

Na-percarbonate 8-12

Na carbonate 10 - 15

Amylase granules according to DE 102005062984.9 0.5-1.5

Zinc acetate 0.5-1.5

Proteases (see below)

Water, salts, dyes ad 100%

In such a formulation, the pure enzyme granules and mixtures of the alkaline protease from Bacillus lentus F49 were incorporated as a representative of the first protease and the alkaline protease from Bacillus gibsonii (DSM 14391) as a representative of the second protease. The mixture was calculated in proportion to the insertions of the single enzymes. The granules of the alkaline protease from Bacillus gibsonii (DSM 14391) were prepared according to WO 97/40128 A1 and coated according to WO 98/26037 A2.

From the formulations were pressed in a tabletting press of Paul-Otto Weber Maschinen + Apparatebau GmbH under a pressure of 25 N single-phase tablets. Vessels with hard, smooth surfaces were standardized with an egg / milk soiling and rinsed with a commercial household dishwasher, namely at 4O ⁰ C with the standard program of the dishwasher Bosch SGS 59 A 02. Per rinse, each 23 g of detergent were used. The water hardness was 21 ° German hardness. The performance was determined as removal of soft sheets according to SÖFW-Journal 132 3-2006. After rinsing, the removal of soiling was determined gravimetrically in percent. For this, the difference between the weight of the contaminated and subsequently rinsed vessel and the initial weight of the vessel was set in relation to the weight difference of the non-rinsed vessel to the initial weight. This relation can be regarded as percent removal. The results obtained are summarized in Table 2 below. Indicated there are the mean values from in each case 9 measurements for approaches 1 and 3 as well as 8 measurements for approach 2.

Table 2: Results of the performance comparison of higher concentrated granules with low concentrated granules in a machine dishwashing detergent.

By comparing the two approaches 1 and 2 with the approach 3 it is clear that by the proportional combination of the two proteases (Bacillus lentus alkaline protease F49 and alkaline protease from Bacillus gibsonii (DSM 14391)) with a lower enzyme protein content compared to experimental approaches with only one the proteases mentioned alone a significantly better, synergistic performance is obtained.

For a calculation of the expected purification performance of a combination of the alkaline protease from Bacillus lentus F49 as a representative of the first protease and the alkaline protease from Bacillus gibsonii (DSM 14391) as a representative of the second protease, first the respective amounts of total protease are compared resulting in a factor of 0.5 (20 mg + 10 mg enzyme protein (batch 3) divided by 40 mg enzyme protein (batch 1) + 20 mg enzyme protein (batch 2)). It follows that the theoretical removal of a combination of Bacillus lentus F49 alkaline protease and Bacillus gibsonii alkaline protease (DSM 14391) (53.2% + 52.8%) is x 0.5 = 53.0%. In comparison, the actual stock removal is 56.7%. The comparison of these two values illustrates the presence of a synergistic cleaning performance by the two proteases used.

EXAMPLE 3 Application According to the Invention in Automatic Dishwashing Detergents (MGSM) MGSM formulations which obey the following general recipe were produced in the context of the invention:

Ingredient Content [wt%]

Na tripolyphosphate 30-45

Nonionic surfactant 3 - 8

Acrylic acid / sulfonic acid copolymer 5 - 10

Acrylic acid polymer 5-10

Na-percarbonate 10-15

Na carbonate 10 - 15 Amylase granules according to DE 102005062984.9 0.5-1.5

Zinc acetate 0.5 - 1

Mn bleach catalyst compound 0.52

Proteases s.u.

Water, salts, dyes ad 100%

Example 4: Use according to the invention in solid detergents

Formulations for solid detergents which obey the following outline recipe have been published in the

Frame of the invention produced.

Ingredient Content [% by weight] Linear alkyl benzene sulfonate (sodium salt) 5-15

Ci _Σ- Cis fatty alcohol sulfate (sodium salt) 1-2

Ci ₂ -Ci ₈ fatty alcohol with 7 EO 1-3

Sodium carbonate 15-30

Sodium bicarbonate 2 - 10 amorphous sodium disilicate 2.5 - 8

Sodium carbonate peroxohydrate 10 - 22

TAED 2 - 8

Polyacrylate 0.5 - 5

Carboxymethyl cellulose 0-2

Phosphonate 0.5 - 2

Sodium sulfate 20-30

Proteases 0.001-0.072 (pure protein)

Amylase 0 - 0.072 (pure protein)

Cellulase 0 - 0.072 (pure protein)

Lipase 0 - 0.072 (pure protein)

Mannanase 0 - 0.072 (pure protein)

Pectinase 0 - 0.072 (pure protein) Balance: foam inhibitors, optical brightener, fragrances

Furthermore, formulations of solid detergents with this framework formulation were produced within the scope of the invention:

Ingredient Content [% by weight] Linear alkyl benzene sulfonate (sodium salt) 2-6

C12-C18 fatty alcohol sulfate (sodium salt) 2-6 C12-C18 fatty alcohol with 7 EO 3-7

Sodium soap 0.5-2

Sodium carbonate 7-30 amorphous sodium disilicate 0.5-4

Sodium perborate tetrahydrate 0-30

TAED 0-20

Zeolite A 10-35

Polycarboxylate 2.5-7

Phosphonate 0-1.5

Foam inhibitor granules 0.5-4

Sodium sulfate 2.5-8

Proteases 0.001-0.072 (pure protein)

Amylase 0 - 0.072 (pure protein)

Cellulase 0 - 0.072 (pure protein)

Lipase 0 - 0.072 (pure protein)

Mannanase 0 - 0.072 (pure protein)

Pectinase 0 - 0.072 (pure protein)

Remainder: water, optical brightener, salts

Example 5: Inventive Use in Liquid Detergents

Formulations for liquid detergents which obey the following outline recipe have been published in the

Frame of the invention produced.

Ingredient Content [wt%]

Polyacrylate thickener 0-5%

Anti-foaming agent 0-4%

Glycerine 0-12%

Propylene glycol 0-14%

Ethanol 0-5%

FAEOS 0-7%

Linear alkylbenzene sulfonic acid 0-20%

Alyklpolyglycoside 0-5%

Nonionic surfactants 5-25%

Boric acid 1-2%

Sodium citrate (dihydrate) 0.5-7%

Soda 2-8%

Coconut fatty acids 0-12% HEDP 0-1%

DTPMP 0-2%

PVP 0-0.4

PVP / PVI 0-1% optical brightener 0-0.2%

Dye 0-0.001

Proteases 0.001-0.072 (pure protein)

Amylase 0 - 0.072 (pure protein)

Cellulase 0 - 0.072 (pure protein)

Lipase 0 - 0.072 (pure protein)

Mannanase 0 - 0.072 (pure protein)

Pectinase 0 - 0.072 (pure protein) demineralized water ad 100%

Example 6 Application According to the Invention in Solid, High-Foaming Detergents Formulations for solid high-foaming detergents which obey the following general formula were produced in the context of the invention.

Ingredient Content [wt%] Linear alkyl benzene sulfonate (sodium salt) 10-30

C12-C18 fatty alcohol sulfate (sodium salt) 0.01 -5

C12-C18 fatty alcohol with 7 EO 0.01 -5

Sodium carbonate 0-30

Sodium silicate 0-10

Sodium perborate 0-10

TAED 0-8

Zeolite A 0-15

Na tripolyphosphate 5-35

Na-percarbonate 0-20

Polycarboxylate 1 -7

Polyacrylate 0.5-5

Phosphonate 0-2

Carboxymethylcellulose 0-2

Sodium sulfate 10-50

Proteases 0.001-0.072 (pure protein)

Amylase 0 - 0.072 (pure protein)

Cellulase 0 - 0.072 (pure protein) Lipase 0 - 0.072 (pure protein)

Mannanase 0 - 0.072 (pure protein)

Pectinase 0 - 0.072 (pure protein) Balance: water, optical brightener, salts

Claims

claims

A composition comprising a first protease and a second protease, characterized in that the first protease is selected from a) a protease which comprises an amino acid sequence which is at least 80% to the amino acid sequence given in SEQ ID NO. 1 at least 80% at least 82.5%, 85%, 87.5%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% and most preferably 100% identical; b) a protease comprising an amino acid sequence which is at least 80%, more preferably at least 82.5%, 85%, 87.5%, 90%, 91%, 92% of the amino acid sequence given in SEQ ID NO %, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5%, and most preferably 100%, is identical; c) a protease which comprises an amino acid sequence which is at least 80%, more preferably at least 82.5%, 85%, 87.5%, 90%, 91%, 92, of the amino acid sequence given in SEQ ID NO %, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% and most preferably 100%, is identical and additionally at least one additional amino acid in comparison with SEQ ID NO. 2 has; and the second protease comprises an amino acid sequence which is at least 80%, more preferably at least 82.5%, 85%, 87.5%, 90%, 91%, 92%, of the amino acid sequence given in SEQ ID NO. 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99,5% and most preferably 100%, in particular a detergent, hand washing detergent, dishwashing detergent, hand dishwashing detergent, machine dishwashing detergent, cleaning agent, Denture or contact lens care product, rinse aid, disinfectant, cosmetic agent, pharmaceutical agent or a means for the treatment of filter media, textiles, furs, paper, skin or leather, is particularly preferably a laundry detergent or a dishwashing detergent.

2. Composition according to claim 1, characterized in that the additional amino acid of the first protease is inserted after one of the following positions in the counting manner according to SEQ ID NO.2: 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 95, 96, 97, 98, 99, 100, 101, 102, 103, 125, 126, 127, 126, 129, 130, 131, 132, 153, 154, 155, 156, 157, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 173, 181, 182, 183, 184, 185, 186, 187, 188, 189, 190, 191, 192, 193, 194, 195, 202, 203, 204, 218, 219.

3. Composition according to one of claims 1 or 2, characterized in that the first protease is present in the agent as a fragment, deletion variant, chimeric protein or derivative and / or the second protease is present in the agent as a fragment, deletion variant, chimeric protein or derivative, wherein the first and second proteases are still catalytically active.

4. Composition according to one of claims 1 to 3, characterized in that it is present as a one-component system or that it is divided into several components, and in particular one which contains the proteases in an amount of 0.1 .mu.g to 100 mg, preferably from 1 μg to 50 mg, more preferably from 10 μg to 50 mg, more preferably from 25 μg to 25 mg and most preferably from 50 μg to 20 mg per g of the agent.

5. Composition according to one of claims 1 to 4, characterized in that it is in solid form, in particular as a free-flowing powder having a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l, or that it is in pasty or liquid form.

6. A composition according to any one of claims 1 to 5, characterized in that at least one protease is coated with a at room temperature or in the absence of water for the protease impermeable substance.

7. Composition according to one of claims 1 to 6, further comprising one or more further enzymes, in particular a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, ß-glucosidase, carrageenase, oxidase, oxidoreductase, pectin-degrading Enzyme or lipase.

8. Composition according to one of claims 1 to 7, characterized in that it contains at least one further component selected from the group consisting of surfactants, builders, acids, alkaline substances, hydrotropes, solvents, thickeners, bleaching agents, dyes, perfumes, corrosion inhibitors , Sequestering agents, electrolytes, optical brighteners, grayness inhibitors, silver corrosion inhibitors, color transfer inhibitors, foam inhibitors, disintegration aids, abrasives, UV absorbers, solvents, antistatic agents, pearlescers and skin protection agents.

9. Use of a composition according to any one of claims 1 to 8 for the removal of protease-sensitive stains on textiles or hard surfaces.

10. A method for cleaning textiles or hard surfaces, characterized in that in at least one method step, an agent according to any one of claims 1 to 8 is applied.

11. A process for the purification of textiles or hard surfaces, characterized in that in at least one process step, a first protease and a second protease are proteolytically active, wherein the first protease is selected from a) a protease comprising an amino acid sequence corresponding to the at least 80% identical in amino acid sequence given in SEQ ID NO. 1; b) a protease comprising an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2; c) a protease which comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2 and additionally has at least one additional amino acid in comparison with SEQ ID NO. 2; and the second protease comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO.3.

12. The method according to claim 1 1, characterized in that the proteases 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 are used per application.

13. Use of a first protease and a second protease for purifying textiles or hard surfaces, characterized in that the first protease is selected from a) a protease which comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO is 80% identical; b) a protease comprising an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2; c) a protease which comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO. 2 and additionally has at least one additional amino acid in comparison with SEQ ID NO. 2; and the second protease comprises an amino acid sequence which is at least 80% identical to the amino acid sequence given in SEQ ID NO.3.

14. Use according to claim 13, characterized in that the proteases in an amount of 40 ug 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 are used.