WO2017211661A1 - Solid detergent and cleaning agent with amylase, protease and soluble builder - Google Patents

Abstract

The invention relates to a solid detergent and cleaning agent containing an amylase combined with a protease and a water-soluble builder system, which demonstrates improved cleaning performance on starchy stains. The invention also relates to methods for cleaning textiles and uses of this solid detergent and cleaning agent.

Description

 Solid washing and cleaning agent with amylase, protease and soluble builder

The invention relates to a solid detergent and cleaning agent containing an amylase in

Combination with a protease and a water-soluble builder system, which shows improved cleaning performance on starchy stains. The invention further relates

Process for the cleaning of textiles and uses of these solid washing and

Cleaning supplies.

Proteases are among the most technically important enzymes of all. For detergents and cleaners, they are the longest established and contained in virtually all modern, powerful detergents and cleaners enzymes. They cause the degradation of protein-containing stains on the items to be cleaned. Of these, in turn, proteases of the subtilisin type (subtilases, subtilopeptidases, EC 3.4.21 .62) are particularly important, which are serine proteases due to the catalytically active amino acids. They act as nonspecific endopeptidases and hydrolyze any acid amide linkages that are internal to peptides or proteins. Their pH optimum is usually in the clearly alkaline range. An overview of this family is provided, for example, by 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 are naturally occurring 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 targeted by methods known in the art

modified randomly and optimized, for example, for use in detergents and cleaners. These include point mutagenesis, deletion or insertion mutagenesis or fusion with other proteins or protein parts. Thus, correspondingly optimized variants are known for most proteases known from the prior art.

Other enzymes which can be used in detergents and cleaners are amylases. In particular, alpha-amylases are among the industrially important enzymes. Their use for detergents and cleaners is established industrially and they are contained in many modern, powerful detergents and cleaners. An alpha-amylase is an enzyme that catalyzes the hydrolysis of the internal a (1-4) glycoside bonds of amylose but not the cleavage of terminal or a (1-6) -glycoside bonds. Alpha-amylases are therefore a group of esterases (E.C. 3.2.1.1.). Alpha-amylases catalyze the cleavage of starch, glycogen, and other oligo- and polysaccharides that have a (1-4) -glycoside linkage. In this respect, alpha-amylases counteract starch residues in the laundry and catalyze their hydrolysis

(Endohydrolysis). Alpha-amylases with broad substrate spectra are especially there used, where inhomogeneous raw materials or substrate mixtures must be implemented, so for example in detergents and cleaning agents, since contaminants may consist of differently structured starch molecules and oligosaccharides. The alpha-amylases used in the washing or cleaning agents known from the prior art are usually of microbial origin and are generally derived from bacteria or fungi, for example the genera Bacillus, Pseudomonas, Acinetobacter, Micrococcus, Humicola, Trichoderma or Trichosporon, in particular Bacillus , Alpha-amylases are usually produced by biotechnological methods known per se by suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or by filamentous fungi.

Surprisingly, it has now been found that an α-amylase according to the invention in

Combination with a protease according to the invention and a soluble builder system in solid detergents at low pH shows an activity on starch-containing soils, which is markedly improved compared to known agents. In particular, the leachability of starch-containing stains, such as rice or corn starch, as well as the washability of bleach-sensitive stains is increased.

The present invention is therefore in a first aspect containing a solid detergent or cleaning agent

 (a) 5-70% by weight of surfactant;

 (b) at least one α-amylase, said α-amylase being characterized by comprising an amino acid sequence corresponding to that set forth in SEQ ID NO: 1

 Amino acid sequence is at least 89% identical over the entire length and in the count according to SEQ ID NO: 1 at one or more of the positions 180, 181, 182, 183 and 184 deletions;

 (c) at least one protease, said protease comprising an amino acid sequence which is at least 80% identical to that in SEQ ID NO: 2 over its entire length;

 (d) 10-50% by weight of a water-soluble builder system, especially an organic builder system;

 wherein the washing or cleaning agent has a pH of 7.5 to 9.5, preferably 8.0 to 9.0, more preferably about 8.5.

In a further aspect, the present invention relates to the use of a

solid washing or cleaning agent according to the invention for washing textiles or cleaning hard surfaces, in particular for removing starchy

Stains on textiles or hard surfaces. In a further aspect, the present invention relates to a method for cleaning textiles or hard surfaces, characterized in that in at least one

Process step, a solid detergent or cleaning agent according to the invention is used.

These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art from a study of the following detailed description and claims. Any feature of one aspect of the invention may be employed in any other aspect of the invention. Further, it is to be understood that the examples contained herein are intended to describe and illustrate the invention, but not to limit it, and in particular that the invention is not limited to these examples. All percentages are by weight unless otherwise specified, based on the total weight of the compositions / composition.

Numeric ranges specified in the format "from x to y" include the above values.If multiple preferred numeric ranges are specified in this format, it is understood that all ranges resulting from the combination of the various endpoints, also be recorded.

"At least one" as used herein refers to 1, 2, 3, 4, 5, 6, 7, 8, 9 or more In the context of components of the compositions described herein, this indication does not refer to the absolute amount Therefore, for example, one or more of the "at least one anionic surfactant" means, for example, one or more

various anionic surfactants, i. one or more different types of anionic surfactants. Together with quantities, the quantities refer to the

Total quantity of correspondingly designated type of component.

"About", "approximately." or "approximately" as used herein in reference to a numerical value refers to the corresponding numerical value ± 10%, preferably ± 5%.

When referred to herein, the pH of an agent is the pH of the washing or cleaning liquor available at 20 ° C with the agent when dissolved in distilled water (1: 100 in weight ratio) unless otherwise specified is specified.

The amylases and proteases of the invention are preferably the mature amylase / protease, i. to the catalytically active molecule without signal and / or propeptide (s). Unless otherwise stated, the sequences given refer to each mature enzyme.

In various embodiments, the α-amylase used according to the invention is characterized in that it comprises an amino acid sequence which is at least 89% and increasingly larger than the total amino acid sequence given in SEQ ID NO: 1 over the entire length thereof preferably at least 90%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5% , 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, 99.5% and up to 100% is identical and counted in accordance with SEQ ID NO: 1 one or more of the positions 180, 181, 182, 183 and 184 has deletions. Particularly preferred is a deletion of two positions selected from 180 + 181, 181 + 182, 182 + 183 and 183 + 184, very particularly preferred are deletions at the positions 183 + 184 in the count according to SEQ ID NO: 1, particularly preferred Deletions H183 ^* + G184 ^* .

Preferably, the α-amylase according to the invention in the counting according to SEQ ID NO: 1 furthermore has an amino acid substitution at one or more of the positions 405, 421, 422 and 428. Particularly preferred are the substitutions I405L, A421H, A422P and A428T.

In a particularly preferred embodiment, the α-amylase according to the invention has, in the count according to SEQ ID NO: 1, the deletions H183 ^* + G184 ^* and additionally the substitutions I405L, A421H, A422P and A428T. Such amylase preferably has the

Amino acid sequence according to SEQ ID NO: 3.

The protease according to the invention comprises an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO: 2 over at least 80% of its total length and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%. , 88%, 89%, 90%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99%, or 100% identical.

Preference is given to a protease which has an amino acid sequence which corresponds to the amino acid sequence given in SEQ ID NO: 2 over at least 80% of its total length and more preferably at least 81%, 82%, 83%, 84%, 85%, 86%. , 87%, 88%, 89%, 90%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, Is 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% and 99% identical and in the count according to SEQ ID NO: 2 on at least one of Positions 3, 4 and 199, preferably at two or all three positions, one

Having amino acid substitution. Particular preference is given to proteases which have the amino acid threonine (T) at position 3, the amino acid isoleucine (I) at position 4 and the amino acid isoleucine (I) at position 199. Such a protease preferably has the

Amino acid sequence according to SEQ ID NO: 4.

Amino acid positions which are given in the context of the present invention with the formulation "counting according to SEQ ID NO: X" are as follows: The others

Amino acid positions are determined by an alignment of the amino acid sequence of a

amylase or protease of the invention having the amino acid sequence as set forth in SEQ ID NO: X. Furthermore, the assignment of positions depends on the mature (matures) protein. This assignment is also to be used in particular if the amino acid sequence of a protein according to the invention comprises a higher number of amino acid residues than the amylase or protease in SEQ ID NO: X. Starting from the mentioned

Positions in the amino acid sequence are the change positions in one

amylase or protease according to the invention those which are just assigned to these positions in an alignment.

The identity of nucleic acid or amino acid sequences is determined by a sequence comparison. This sequence comparison is based on the BLAST algorithm established and commonly used in the prior art (see, for example, Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ. (1990) "Basic local alignment search Biol. 215: 403-410; and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs"; Nucleic Acids Res., 25, pp.3389-3402) and is in principle accomplished by similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences of each other be assigned. A tabular assignment of the respective positions is referred to as alignment. Another algorithm available in the prior art is the FASTA algorithm. Sequence comparisons (alignments), in particular multiple sequence comparisons, are created with computer programs. For example, the Clustal series (see, for example, Chenna et al., 2003, Multiple Sequence Alignment with the Clinical Series of Programs, Nucleic Acid Research 31, 3497-3500), T-Coffee (see, for example, Notredame et al (2000): T-Coffee: A novel method for multiple sequence alignments, J. Mol. Biol. 302, 205-217) or programs based on these programs or algorithms. Also possible are alignment comparisons (alignments) with the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the default parameters whose AlignX module for sequence comparisons is based on ClustalW.

Such a comparison also allows a statement about the similarity of the compared sequences to each other. It is usually given in percent identity, that is, the proportion of identical nucleotides or amino acid residues at the same or in an alignment corresponding positions. The broader concept of homology involves conserved amino acid substitutions in the consideration of amino acid sequences, that is, amino acids with similar chemical activity, since these usually have similar chemical properties within the protein

Exercise activities. Therefore, the similarity of the sequences compared may also be stated as percent homology or percent similarity. Identity and / or homology information can be made about whole polypeptides or genes or only over individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by matches in the sequences. Such areas often have identical functions. They can be small and comprise only a few nucleotides or amino acids. Often, such small regions exert essential functions for the overall activity of the protein. It may therefore be useful to relate sequence matches only to individual, possibly small areas. Unless otherwise indicated, identity or homology information in the present application, however, refers to the total length of the particular nucleic acid or amino acid sequence indicated.

In the context of the present invention, the statement means that a

Therefore, the amino acid position of a numerically designated position in SEQ ID NO: 1 or SEQ ID NO: 2 corresponds to the corresponding position being assigned to the numerically designated position in SEQ ID NO: 1 and SEQ ID NO: 2, respectively, in an alignment as defined above.

In addition to the amino acid changes discussed above, amylases and proteases of the invention may have other amino acid changes, especially amino acid substitutions, insertions or deletions. Such amylases and proteases are, for example, by targeted genetic modification, i. by mutagenesis, further developed and optimized for specific applications or specific properties (for example, in terms of catalytic activity, stability, etc.). Furthermore, nucleic acids according to the invention can be introduced into recombination mixtures and thus used for

Generation of completely novel amylases and proteases or other polypeptides can be used.

The goal is to introduce into the known molecules targeted mutations such as substitutions, insertions or deletions, for example, to improve the cleaning performance of enzymes of the invention. For this purpose, in particular the surface charges and / or the isoelectric point of the molecules and thereby their interactions with the substrate can be changed. Thus, for example, the net charge of the enzymes can be changed in order to influence the substrate binding, in particular for use in detergents and cleaners. Alternatively or additionally, the stability of the amylase or protease can be increased by one or more corresponding mutations, thereby improving its purification performance.

Advantageous properties of individual mutations, e.g. individual substitutions can complement each other. An amylase or protease which has already been optimized with respect to certain properties, for example with respect to its stability towards surfactants and / or bleaching agents and / or other components, can therefore be further developed within the scope of the invention.

For the description of substitutions concerning exactly one amino acid position

(Amino acid exchanges), the following convention is used: first, the naturally occurring amino acid in the form of the international one-letter code is called, then follows the associated sequence position and finally the inserted amino acid. Several exchanges within the same polypeptide chain are separated by slashes separated. For insertions, additional amino acids are named after the sequence position. For deletions, the missing amino acid is replaced by a symbol, such as a star or a dash. For example, A95G describes the substitution of alanine at position 95 by glycine, A95AG the insertion of glycine after the amino acid alanine at position 95 and A95 ^* the deletion of alanine at position 95. This nomenclature is known to those skilled in the art of enzyme technology.

Another object of the present invention is therefore a washing and cleaning agent containing a combination of an α-amylase and a protease, wherein the α-amylase or protease is characterized in that it consists of an amylase according to the invention or

Protease is available as a starting molecule by one or more conservative amino acid substitution. The term "conservative amino acid substitution" means the replacement

(Substitution) of an amino acid residue against another amino acid residue, this exchange does not lead to a change in polarity or charge at the position of the exchanged amino acid, z. Example, the replacement of a nonpolar amino acid residue against another nonpolar amino acid residue. Conservative amino acid substitutions in the context of the invention include, for example: G = A = S, L = V = L = M, D = E, N = Q, K = R, Y = F, S = T,

G = A = I = V = L = M = Y = F = W = P = S = T.

Another object of the present invention is therefore a washing and cleaning agent containing a combination of an α-amylase and a protease, wherein the α-amylase is characterized in that it is obtainable from an amylase according to the invention as the starting molecule by fragmentation, deletion, Insertion or substitution mutagenesis and an amino acid sequence over a length of at least 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300, 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 475, 480, 482, 483, 484 or 485 contiguous amino acids matches the parent molecule. Similarly, the protease may also be characterized in that it is obtainable from a protease according to the invention as the starting molecule by fragmentation, deletion, insertion or substitution mutagenesis and comprises an amino acid sequence which is over a length of at least 50, 60, 70, 80, 90, 100, 1 10, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 262, 264, 265, 266, 267 or 268, respectively

Amino acids coincides with the starting molecule.

Thus, for example, it is possible to delete individual amino acids at the termini or in the loops of the enzyme without thereby losing or reducing the enzymatic activity. Furthermore, such fragmentation, deletion, insertion or substitution mutagenesis can also reduce, for example, the allergenicity of the enzymes concerned and thus improve their overall applicability. Advantageously, the enzymes retain even after the Mutagenesis their enzymatic activity, ie their enzymatic activity is at least equal to that of the starting enzyme. Substitutions can also show beneficial effects. Both single and multiple contiguous amino acids can be substituted for other amino acids.

An enzyme according to the invention may additionally be stabilized, in particular by one or more mutations, for example substitutions, or by coupling to a polymer. For an increase in stability during storage and / or during use, for example during the washing process, causes the enzymatic activity to last longer and thus improve the cleaning performance. Basically, all come in the state of the art

considered and / or appropriate stabilization options into consideration. Preference is given to those stabilizations which are achieved by mutations of the enzyme itself, since such stabilizations do not require any further working steps following the recovery of the enzyme. Sequences suitable for this purpose are known from the prior art.

Other ways of stabilization z. B .:

 Changing the binding of metal ions, in particular the calcium binding sites,

 for example, by replacing one or more of the amino acid (s) involved in the calcium binding with one or more negatively charged amino acids and / or by introducing sequence changes in at least one of the sequences of the two amino acids arginine / glycine;

 Protection against the influence of denaturing agents, such as surfactants, on mutations causing an alteration of the amino acid sequence on or at the surface of the protein;

Replacement of amino acids located near the N-terminus against those likely to contact non-covalent interactions with the rest of the molecule, thus contributing to the maintenance of the globular structure.

Preferred embodiments are those in which the enzyme is stabilized in several ways, as several stabilizing mutations act additive or synergistic.

Another object of the invention is an enzyme as described above, which is characterized in that it has at least one chemical modification. An enzyme with such a change is called a derivative, i. the enzyme is derivatized.

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 made, for example, in vivo by the host cell expressing the protein. In this regard, couplings of low molecular weight compounds such as lipids or oligosaccharides are particularly noteworthy. However, derivatizations can also be carried out in vitro be carried out by, for example, the chemical transformation of a side chain of an amino acid or by covalent attachment of another compound to the protein. For example, the coupling of amines to carboxyl groups of an enzyme to alter the isoelectric point is possible. Such another compound may also be another protein that is bound to a protein of the invention via bifunctional chemical compounds, for example. Similarly, derivatization is the covalent bond to a

to understand macromolecular carrier, or even a non-covalent inclusion in suitable macromolecular cage structures. Derivatizations 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. Such modifications may further affect stability or enzymatic activity. They can also serve to reduce the allergenicity and / or immunogenicity of the protein and thus, for example, increase its skin compatibility. For example, couplings with macromolecular compounds, for example, polyethylene glycol, can improve the protein in terms of stability and / or skin tolerance.

Derivatives of a protein according to the invention can also be used in the broadest sense

Preparations of these proteins are understood. Depending on the extraction, processing or preparation, a protein may be associated with various other substances, for example from the culture of the producing microorganisms. A protein may also have been deliberately added to other substances, for example to increase its storage stability.

Therefore, all preparations of a protein according to the invention are also according to the invention. This is also independent of whether or not it actually exhibits this enzymatic activity in a particular preparation. Because it may be desired that it has no or only low activity during storage, and unfolds its enzymatic function only at the time of use. This can be controlled, for example, via appropriate accompanying substances.

The inventive combination of an α-amylase according to the invention with a

protease according to the invention in solid detergents and cleaners causes an improved cleaning performance of the solid detergent and cleaner to starchy soils and also to protease-sensitive stains. In particular, α-amylases according to the invention have a performance-improving effect on the protease likewise contained in the washing and cleaning agent and thus, inter alia, by their protease-stabilizing action, enable improved removal of at least one, preferably of several protease-sensitive soils on textiles and / or hard Surfaces, for example dishes. Particularly advantageous cleaning performances show preferred embodiments of washing and cleaning agents according to the invention on blood-containing Stains, for example on the Blood / Milk / Ink stain: Product No. CFT C-05 available from CFT (Center for Test Materials) BV Viaardingen, the Netherlands.

The combination of amylase, protease, soluble builder and low pH further provides improved cleaning performance on starchy soils, especially improved washability over the same enzyme combinations with less or no soluble builder and higher pH.

Preferred embodiments of the invention amylase and protease combinations achieve such advantageous cleaning performance even at low temperatures, especially in the temperature ranges between 10 ° C and 60 ° C, preferably between 15 ° C and 50 ° C and more preferably between 20 ° C and 40 ° C. , Further preferred

Embodiments of the invention amylase and protease combinations achieve such advantageous cleaning performance in a wide temperature range, for example between 15 ° C and 90 ° C, preferably between 20 ° C and 60 ° C.

By preferred embodiments of the present invention, solid detergents and cleaners having improved cleaning performance are produced specifically with regard to starchy and protease-sensitive soiling.

In the context of the invention, cleaning performance is understood to mean the whitening performance of one or more stains, in particular laundry or dishes. In the context of the invention, both the washing or cleaning agent, which comprises the combination of amylase and protease or the washing or cleaning liquor formed by this agent, as well as the protease and amylase itself have a respective cleaning performance. The cleaning performance of the enzymes thus contributes to the cleaning performance of the agent

or the washing or cleaning liquor formed by the agent. The

Cleaning performance is preferably determined as indicated below.

The cleaning performance is determined in a washing system containing a detergent in a dosage between 3.5 and 6.5 grams per liter of wash liquor as well as the amylase and the protease. The amylases to be compared are used with the same concentration (based on active protein). The cleaning performance of the enzymes are compared

corresponding enzyme-sensitive stains determined by measuring the whiteness of the washed textiles. The washing is carried out for 70 minutes at a temperature of 40 ° C, the water has a water hardness between 13.5 and 16.5 ° (German hardness). The concentration of the protease in the detergent intended for this washing system is from 0.001 to 0.1% by weight, preferably from 0.01 to 0.06% by weight, based on active protein. The concentration of the amylase in the detergent intended for this washing system is from 0.001-0, 15% by weight, preferably from 0.005 to 0.012% by weight, based on active protein.

Preferably, the dosage of the solid detergent is between 3.5 and 6.0 grams per liter of wash liquor, for example, 4.7, 4.9 or 5.9 grams per liter of wash liquor. Washing is carried out in a pH range between pH 7.5 and pH 9.5, preferably between pH 8 and pH 9, more preferably at approximately pH 8.5.

A preferred powdered detergent for such a washing system is composed as follows (all figures in weight percent): 10-15% linear alkyl benzene sulfonate (sodium salt), 0-1, 5% C12-C18 fatty alcohol sulfate (sodium salt), 2-5% C12-C18 fatty alcohol with 7 EO, 0-2% soaps, 5-15% sodium carbonate, 4-10% amorphous sodium disilicate, 0.5-2% phosphonate (eg HEDP-Na4), 1-4 % Polyacrylate, 1-2% carboxymethylcellulose, balance: sodium sulfate,

Foam inhibitors, optical brighteners, fragrances, etc. Preferably, the dosage of the powdered detergent is between 4.5 and 7.0 grams per liter of wash liquor, for example, and more preferably 4.7 grams per liter of wash liquor, or 5.5, 5.9 or 6.7 grams per liter of wash liquor or about 65g / job.

The degree of whiteness, i. the brightening of soiling, as a measure of the cleaning performance is preferably determined by optical measuring method, preferably photometrically. A suitable device for this purpose is for example the spectrometer Minolta CM508d. Usually, the devices used for the measurement are previously calibrated with a white standard, preferably a supplied white standard.

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 determination of the active protein concentration in this regard can be carried out by titration of the active sites using a suitable irreversible inhibitor (for proteases, for example phenylmethylsulfonyl fluoride (PMSF)) and determination of the residual activity (see M. Bender et al., J. Am. Chem. Soc 24 (1966), pp. 5890-5913).

In various embodiments of the invention, the concentration of protease in the solid detergent or cleaning agent is 0.001-0.5% by weight, preferably 0.01 to 0.1% by weight, based on active protein. The concentration of the amylase in the washing or cleaning agent is 0.0005-0.5 wt .-%, preferably 0.001 to 0.2 wt .-%, based on active protein. The solid detergent also contains a soluble builder system. "Soluble" or "water soluble," as used interchangeably in this context, means that the builder, under conditions of use, is at the concentration determined by the amount of the agent containing it at the usual conditions results in completely dissolving in the wash liquor, ie, the residual of the builder remaining as a solid constitutes less than 1% of the total amount of the builder.

The water-soluble builder system contains at least one water-soluble, preferably organic, builder. The water-soluble organic builder substances include polycarboxylic acids, in particular citric acid and sugar acids, monomeric and polymeric aminopolycarboxylic acids, in particular methylglycinediacetic acid, glutamic 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 by oxidation of polysaccharides or dextrins accessible polycarboxylates, and / or 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 5,000 and 200,000, of the copolymers between 2,000 and 200,000, preferably 50,000 to 120,000, each based on the free acid. A particularly preferred acrylic acid-maleic acid copolymer has a molecular weight of 50,000 to 100,000. Suitable, although less preferred, compounds of this class are copolymers of acrylic or methacrylic acid with vinyl ethers, such as vinylmethyl ethers, vinyl esters, ethylene, propylene and styrene, in which the acid content is at least 50% by weight. Terpolymers which contain two unsaturated acids and / or their salts as monomers and also vinyl alcohol and / or an esterified vinyl alcohol or a carbohydrate as the third monomer may also be used as water-soluble organic builder substances. The first acidic monomer or its salt is derived from a monoethylenically unsaturated C3-Cs-carboxylic acid and preferably from a C3-C4-monocarboxylic acid, in particular from (meth) -acrylic acid. The second acidic monomer or its salt may be a derivative of a C4-Cs-dicarboxylic acid, with maleic acid being particularly preferred, and / or a derivative of an allylsulfonic acid which is substituted in the 2-position by an alkyl or aryl radical. Such polymers generally have a molecular weight between 1,000 and 200,000. Further preferred copolymers are those which have as monomers acrolein and acrylic acid / acrylic acid salts or vinyl acetate. All the acids mentioned can be 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 50% by weight, in particular up to 25% by weight and preferably from 10% by weight to 20% by weight.

In preferred embodiments, citric acid and / or citrate is used as the water-soluble, organic builder. Particularly preferred is the use of 5 wt .-% to 25 wt .-%, preferably 7.5 to 12.5 wt .-% citric acid and / or 5 wt .-% to 25 wt .-%,

preferably 7.5 to 12.5% by weight of citrate, preferably alkali citrate, more preferably

Sodium citrate. Citric acid / citrate can each be used in the form of their hydrates, for example, citric acid in the form of monohydrate, citrate in the form of

Trisodium citrate dihydrate are used.

In addition to the above-mentioned water-soluble organic builders, the agents of the invention may further contain inorganic water-soluble builders. Suitable water-soluble inorganic builder materials are, in particular, alkali metal silicates. Suitable examples are crystalline alkali metal silicates, which may be present alone or in a mixture with amorphous silicates. The alkali metal silicates useful as builders in the compositions according to the invention preferably have a molar ratio of alkali metal oxide to SiO 2 below 0.95, in particular from 1: 1, 1 to 1: 12, and may be present in amorphous or crystalline form. Preferred alkali metal silicates are

Sodium silicates, in particular the amorphous sodium silicates, with a molar ratio Na20: SiO 2 of 1: 1, 8 to 1: 2.8. Crystalline silicates which may be present alone or in a mixture with amorphous silicates are preferably crystalline phyllosilicates of the general formula Na.sub.2SixO.sub.2.sup.x + H.sub.2O.sub.2, in which x, the so-called modulus, is a number from 1.9 to 4 and y is a number from 0 is up to 20 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 beta- and delta-sodium disilicates (Na 2 Si 2 O 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 invention means a crystalline sodium layer silicate is used with a modulus of 2 to 3, as it can be prepared from sand and soda. Crystalline sodium silicates with a modulus in the range of 1.9 to 3.5 are used in a further preferred embodiment of compositions according to the invention. In agents containing both amorphous and crystalline alkali metal silicates, the weight ratio of amorphous alkali metal silicate to crystalline alkali metal silicate is preferably 1: 2 to 2: 1 and especially 1: 1 to 2: 1.

Furthermore, the carbonates (and hyo-hydrogencarbonates), in particular sodium carbonate, and the phosphonic acids / phosphonates are also important as water-soluble inorganic builder substances. Under phosphonic acids are also optionally substituted

Understood alkylphosphonic, which also have several phosphonic acid groups could (so-called polyphosphonic acids). They are preferably selected from the hydroxy and / or aminoalkylphosphonic acids and / or their alkali metal salts, for example dimethylaminomethanediphosphonic acid, 3-aminopropane-1-hydroxy-1,1-diphosphonic acid, 1-amino-1-phenylmethanediphosphonic acid, 1 Hydroxyethane-1, 1-diphosphonic acid (HEDP), amino tris (methylenephosphonic acid), N, N, N ', N'-ethylenediamine tetrakis (methylenephosphonic acid),

Diethylentriaminpenta (methylenephosphonic acid) (DTPMP) and acylated derivatives of phosphorous acid, which can also be used in any mixtures.

In various embodiments, the builder system is preferably composed of the components, based in each case on the total mass of the composition:

 a) 5 wt .-% to 25 wt .-%, preferably 7.5 to 12.5 wt .-% citric acid;

 b) 5 wt .-% to 25 wt .-%, preferably 7.5 to 12.5 wt .-% citrate, preferably

 alkali metal citrate;

 c) 0 to 40 wt .-%, preferably 0 to 15 wt .-% alkali carbonate, which may be at least partially replaced by alkali metal bicarbonate, in particular sodium carbonate; d) 0 to 20 wt .-%, preferably 3 to 10 wt .-% alkali metal silicate;

 e) 0.005 to 10 wt .-%, preferably 0.02 to 2 wt .-% phosphonic acid and / or

 Alkali phosphonate, especially HEDP and / or DTPMP; and

 f) 0 to 10 wt .-%, preferably 0.5 to 3 wt .-% polymeric polycarboxylate, in particular polyacrylate.

With regard to component f), for example, the alkali metal salts of polyacrylic acid or polymethacrylic acid, for example, those having a molecular weight of 500 to 70,000 g / mol are suitable. This class of substances has already been described in detail above. The (co) polymeric polycarboxylates can be used either as a powder or as an aqueous solution.

The agents of the invention are preferably free of phosphate builder, i. contain less than 1 wt .-% preferably no deliberately added phosphate builder.

The agents may also contain water-insoluble builders. In this case, in particular the aluminosilicates and in this case preferably the zeolites are of importance.

The subject matter of the invention includes all conceivable solid types of washing or cleaning agents, both concentrates and undiluted agents, for use on a commercial scale, in the washing machine or in hand washing or cleaning. These include detergents for textiles, carpets, or natural fibers for which the

Label detergent is used. These include, for example, dishwashing detergents for dishwashers or manual dishwashing detergents or hard surface cleaners As metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood or leather, for which the term detergent is used, so in addition to manual and automatic dishwashing detergents, for example, scouring agents, glass cleaner, toilet scenters, etc. Zu den solid detergents and cleaning agents in the context of the invention also include washing aids which are metered into the actual detergent during manual or automatic textile washing in order to achieve a further effect. Furthermore, laundry detergents and cleaners in the context of the invention also include textile pre-treatment and post-treatment agents, ie those agents with which the laundry item is brought into contact before the actual laundry, for example to dissolve stubborn soiling, and also agents which are in one of the actual Textile laundry downstream step to give the laundry further desirable properties such as comfortable grip, crease resistance or low static charge. Amongst others, the fabric softeners are calculated.

The solid detergents or cleaners according to the invention may contain, in addition to the amylase and the protease, further enzymes. For example, lipases or cutinases can be used as further enzymes, in particular because of their triglyceride-splitting activities, but also in order to generate peracids in situ from suitable precursors. These include, for example, the lipases originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or further developed, in particular those with the amino acid exchange D96L. These include, for example, the lipases which are obtainable or further developed from Humicola lanuginosa (Thermomyces lanuginosus), in particular those having one or more of the following amino acid substitutions starting from said lipase in positions D96L, T213R and / or N233R, particularly preferably T213R and N233R. Furthermore, for example, the cutinases can be used, which were originally isolated from Fusarium solani pisi and Humicola insolens. It is also possible to use lipases, or cutinases, whose initial enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii.

The agents according to the invention may also contain cellulases or hemicellulases such as mannanases, xanthan lyases, pectin lyases (= pectinases), pectin esterases, pectate lyases, xyloglucanases (= xylanases), pullulanases or β-glucanases.

Oxidoreductases, for example oxidases, oxygenases, catalases, peroxidases, such as halo, chloro, bromo, lignin, glucose or manganese peroxidases, dioxygenases or laccases (phenol oxidases, polyphenol oxidases) can be used according to the invention to increase the bleaching effect. Advantageously, it is additionally preferred to add organic, particularly preferably aromatic, compounds which interact with the enzymes in order to enhance the activity of the relevant oxidoreductases (enhancers) or in the case of strong different redox potentials between the oxidizing enzymes and the soiling to ensure the flow of electrons (mediators).

The compositions contain 5-70% by weight of surfactant, by which is meant one or more surfactants. Preferably, the agents comprise 5-55% by weight, more preferably 5-35% by weight of surfactant. In particular, anionic surfactants, nonionic surfactants and mixtures thereof are suitable, but it is also possible for cationic, zwitterionic and / or amphoteric surfactants to be present.

As anionic surfactants, for example, those of the sulfonate type and sulfates are used. As surfactants of the sulfonate type preferably come C9-13-Alkylbenzolsul- fonate, Olefinsulfonate, i. Mixtures of alkene and hydroxyalkanesulfonates and disulfonates, as obtained for example from C12-18 monoolefins with terminal or internal double bond by sulfonating with gaseous sulfur trioxide and subsequent alkaline or acidic hydrolysis of the sulfonation, into consideration. Also suitable are alkanesulfonates which are obtained from C12-18-alkanes, for example by sulfochlorination or sulfoxidation with subsequent hydrolysis or neutralization. Likewise, the esters of α-sulfo fatty acids (ester sulfonates), e.g. the α-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids suitable.

Preferably, the agent comprises 5-55% by weight, preferably 5-35% by weight, of anionic surfactant. Most preferably, the agent comprises 5-35% by weight of alkylbenzenesulfonate. In addition, the agent may preferably contain other anionic surfactants, in particular alkyl ether sulfates, and

nonionic surfactants, especially fatty alcohol alkoxylates. These can then make up the rest of the surfactants.

Suitable alkylbenzenesulfonates are preferably selected from linear or branched alkylbenzenesulfonates of the formula

in which R ^' and R ^"are independently H or alkyl and together contain from 6 to 19, preferably from 7 to 15, and in particular from 9 to 13, carbon atoms A particularly preferred representative is sodium dodecylbenzylsulfonate.

Alk (en) ylsulfates are the alkali metal and in particular the sodium salts of

Sulfuric acid half esters of C12-C18 fatty alcohols, for example from coconut fatty alcohol,

Tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or the C10-C20 oxo alcohols and those half-esters of secondary alcohols of these chain lengths are preferred. Further preferred Alk (en) ylsulfates of said chain length, which contain a synthetic, petrochemical-based straight-chain alkyl radical having an analogous degradation behavior as the adequate compounds based on oleochemical raw materials. Out

In terms of washing technology, preference is given to the C 12 -C 16 -alkyl sulfates and C 12 -C 15 -alkyl sulfates and C 14 -C 15 -alkyl sulfates.

Also, the sulfuric monoesters of ethoxylated with 1 to 6 moles of ethylene oxide straight-chain or branched C7-21 alcohols, such as 2-methyl-branched C9-1 1 alcohols having an average of 3.5 moles of ethylene oxide (EO) or C12-18 fatty alcohols 1 to 4 EO, are suitable. suitable

Alkyl ether sulfates are, for example, compounds of the formula

R1-0- (AO) _n -S0 ₃ - X ⁺

In this formula, R 1 is a linear or branched, substituted or unsubstituted alkyl radical, preferably a linear, unsubstituted alkyl radical, particularly preferably a fatty alcohol radical. Preferred radicals R 1 are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, where the representatives with even number of C atoms are preferred. Particularly preferred radicals R 1 are derived from C 12 -C 18 -fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or from C 10 -C 20 oxo alcohols. AO represents an ethylene oxide (EO) or propylene oxide (PO) moiety, preferably an ethylene oxide moiety. The index n stands for an integer from 1 to 50, preferably from 1 to 20 and especially from 2 to 10. Most preferably, n stands for the numbers 2, 3, 4, 5, 6, 7 or 8. X stands for a monovalent cation or the nth part of an n-valent cation, the alkali metal ions are preferred, and Na + or K + including Na, with Na + being extremely preferred. Further cations X + can be selected from NH4 +, Ζνίλ +,

Ca2 +, ¹ ^ Mn2 +, and mixtures thereof.

In various embodiments, the alkyl ether sulfate may be selected from

Fatty alcohol ether sulfates of the formula

with k = 1 1 to 19, n = 2, 3, 4, 5, 6, 7 or 8. Very particularly preferred representatives are Na-C 12-14 fatty alcohol ether sulfates with 2 EO (k = 1 1-13, n = 2) , The stated degree of ethoxylation represents a statistical average that may be an integer or a fractional number for a particular product. The indicated degrees of alkoxylation represent statistical averages, which may be an integer or a fractional number for a particular product. preferred Alkoxylates / ethoxylates have a narrow homolog distribution (narrow rank ethoxylates, NRE).

It has proved to be advantageous for the cold washing performance if the detergents additionally contain soap (s). Preferred detergents are therefore characterized as containing soap (s). 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 of natural fatty acids, e.g. Coconut, palm kernel or tallow fatty acids, derived soap mixtures.

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 linear and methyl-branched radicals in the mixture can contain, as they are usually present in Oxoalkoholresten. In particular, however, alcohol ethoxylates having linear radicals of alcohols of native origin having 12 to 18 carbon atoms, e.g. from coconut, palm, tallow or oleyl alcohol, and on average from 2 to 8 EO per mole of alcohol. The preferred ethoxylated alcohols include, for example, C12-14 alcohols with 3 EO or 4 EO, C9-1 1 alcohol with 7 EO, C13-15 alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C12-18 Alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C12-14 alcohol with 3 EO and C12-18 alcohol with 5 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 include tallow fatty alcohol with 14 EO, 25 EO, 30 EO or 40 EO.

Another class of preferred nonionic surfactants used either as the sole nonionic surfactant or in combination with other nonionic surfactants are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated

Fatty acid alkyl esters, preferably having 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters.

Another class of nonionic surfactants that can be used to advantage are the alkyl polyglycosides (APG). Usable alkylpolyglycosides satisfy the general formula RO (G) z, in which R is a linear or branched, in particular in the 2-position methyl-branched, saturated or unsaturated, aliphatic radical having 8 to 22, preferably 12 to 18 carbon atoms and G is the Is a symbol which represents a glycose unit having 5 or 6 C atoms, preferably glucose. The glycosidation degree z is between 1, 0 and 4.0, preferably between 1, 0 and 2.0 and in particular between 1, 1 and 1, 4. Preferably used are linear alkylpolyglycosides, ie alkyl polyglycosides in which the polyglycosyl is a glucose residue and the alkyl radical is an n-alkyl radical.

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.

Suitable amphoteric surfactants are, for example, betaines of the formula (R 1, XR 1) XR 3 NTC 3 COO- in which R ^{i is} an alkyl radical optionally interrupted by hetero atoms or heteroatom groups having 8 to 25, preferably 10 to 21 carbon atoms and R ^iv and R ^{v are} identical or different Alkyl radicals having 1 to 3 carbon atoms, in particular Cio-Cis-alkyl dimethylcarboxymethylbetain and Cn-Ci7-alkylamidopropyl-dimethylcarboxymethylbetain.

Suitable cationic surfactants are i.a. the quaternary ammonium compounds of the formula

(R ^VI ) (R ^vii ) (R ^viii ) (R ^ix ) N ⁺ X ^" , in which R ^vi to R ^ix for four identical or different, in particular two long and two short-chain, alkyl radicals and X ^" for an anion , in particular a halide ion, for example, didecyldimethylammonium chloride, Alkylbenzyldidecylammoniumchlorid and mixtures thereof. Further suitable cationic surfactants are the quaternary surface-active compounds, in particular with a sulfonium, phosphonium, iodonium or

Arsonium group, which are also known as antimicrobial agents. Through the use of quaternary surface-active compounds with antimicrobial action, the agent can be designed with an antimicrobial effect or its possibly existing antimicrobial effect due to other ingredients can be improved.

In addition to the abovementioned constituents, the compositions according to the invention may in principle comprise all known ingredients customary in such agents. These include, but are not limited to, bleaching agents based on organic and / or inorganic peroxygen compounds, bleach activators, bleach catalysts, water-miscible organic solvents, sequestering agents, electrolytes, pH regulators, and other adjuvants such as optical brighteners, grayness inhibitors, foam regulators, and colorants Perfumes and combinations thereof.

The solid detergents or cleaners according to the invention can be provided in the form of dressings known to the person skilled in the art. A fabric, e.g. a composition or agent, as defined by the invention, is solid when in the solid state at 25 ° C and 1013 mbar. The solid dosage forms according to the invention include

Extrudates, granules, tablets or pouches containing solid agents which may be present both in bulk and in portions packaged. Alternatively, the agent is as free-flowing Powder, in particular having a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l.

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 compositions according to the invention 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.

The solid detergents or cleaners according to the invention preferably have less than 10% by weight, preferably less than 5% by weight, of water, based on their total weight.

Another subject of the invention is a process for the cleaning of textiles or hard surfaces, which is characterized in that in at least one process step, an inventive agent is used and the use of a solid detergent or cleaning agent according to the invention for washing textiles or cleaning hard surfaces, in particular For removing starchy soiling on textiles or hard surfaces.

These include both manual and mechanical processes, with mechanical processes being preferred. Methods for cleaning textiles are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned and washed off after the contact time, or that the items to be cleaned are otherwise treated with a detergent or a solution or dilution of this product. The same applies to processes for cleaning all other materials than textiles, especially hard surfaces. All conceivable washing or cleaning methods can be enriched in at least one of the method steps to the application of a washing or cleaning agent according to the invention and then provide

Embodiments of the present invention. All aspects, objects and embodiments described for means according to the invention are also applicable to this subject of the invention. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive method. Examples

Example 1: Washing test

Used detergent matrix

Table 1 shows a powder detergent B according to the invention with a soluble builder (builder mixture) in comparison with the reference powder detergent A.

Table 1 :

 All data in% by weight

Wash test to demonstrate improved stain removal

Used substances: For the washing tests were household washing machines (Miele W 1935) with 3.5 kg

Accompanied underwear and the soiled cloth rag loaded. In addition, 65 g / l 15 ml of the detergent to be tested were added and washed at 30 ^° C. Detergent A from Table 1 was used as reference and compared with Detergent B according to the invention. After hanging drying and lack of cloth rags their whiteness

spectrophotometrically (Minolta CR200-1).

The values given (Table 2) are mean values of 6 determinations. The soiled textiles were bought. The remission values in Table A and the differences between the remission values for the standard detergent and the errors in the 6-fold determination (HSD) in Table 3 are shown. The use of the combination of the amylase according to the invention (SEQ ID NO: 3) with the protease according to the invention (SEQ ID NO: 4) and a lower pH soluble builder system in Detergent Formulation B shows an improvement in leachability on starch stains as compared to Detergent Formulation A with the same amylase.

Table 2: Washing results with statistical analysis on a Tukey 6-fold determination (starch or starchy stains)

 Difference and HSD (Tukey) Product A A @ pH ~ 10

 B @ pH - 8.5

 A vs B

 Diff. HSD

 CFT CS26 corn starch, dyed 1, 5 0.5

 CFT CS28 rice starch, dyed 0.8 0.4

 CFT CS44 chocolate drink 5.2 1, 1

 CFT CS29 tapioca starch 2.4 0.6

 EMPA 160 chocolate cream 1, 7 1, 3

 EMPA 162 corn starch, dyed 2.4 0.8

EMPA 163 oatmeal 3,3 1, 6

Table 3: Washing results with statistical analysis on a Tukey 6-fold determination (bleachable stains)

 Difference and HSD (Tukey) Product A A @ pH ~ 10

 B @ pH ~ 8.5

 A vs B

 Diff. HSD

 Equest AISE Coffee EQUEST Coffee 2.5 1.7

 (WE5ECWKC)

 Equest AISE Tea EQUEST Tea 8.7 3.2

 (WE5LTWKC)

 Equest redwine red wine 8.5 2.1

 CFT CS103 red wine, fresh 4.1 1.7

 CFTCS12 Black 2.0 1.9

 currant

 CFTCS15 blueberry juice 2.6 1.8

 CFT CS03 red wine, aged 5.7 1,9

 EMPA167 tea 1.5 0.9

 H-K-B Coffee 5,8 0,7

 H-T-B Tea 10.8 2.9

 WFK10BB blackberry juice 3.3 1.9

 WFK10JB Black Johannis 3,7 2,5

 beer juice

 WFK10WB Blueberry juice 4.2 2.2

Claims

Patent claims

1. Solid detergent or cleaning agent containing:

a) 5-70% by weight of surfactant;

b) at least one a-amylase, the a-amylase being characterized in that it comprises an amino acid sequence which is at least 89% identical to the amino acid sequence specified in SEQ ID NO:1 over its entire length and in the count according to SEQ ID NO: 1 has deletions at one or more of positions 180, 181, 182, 183 and 184;

c) at least one protease, the protease comprising an amino acid sequence which is at least 80% identical to that in SEQ ID NO:2 over its entire length; d) 10-50% by weight, preferably 10 to 25% by weight, of a water-soluble builder system, in particular an organic builder system;

wherein the washing or cleaning agent has a pH of 7.5 to 9.5, preferably 8.0 to 9.0, more preferably about 8.5.

2. Solid detergent or cleaning agent according to claim 1, characterized in that

(1) the at least one amylase comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO: 1 over its total length to at least 90%, 90.5%, 91%, 91.5%, 92%, 92.5% , 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99 %, 99.5% and up to 100% are identical;

(2) the at least one amylase deletions at at least two positions selected from positions 180+181, 181+182, 182+183 and 183+184 in the count according to SEQ ID NO: 1, and preferably at positions 183+184 in the count according to SEQ ID NO: 1, more preferably the deletions H 183 ^* + G184 ^* in the count according to SEQ ID NO: 1;

(3) the at least one amylase in the count according to SEQ ID NO: 1

Has amino acid substitutions at one or more of positions 405, 421, 422 and 428, preferably substitutions I405L; A421H, A422P and A428T; and or

(4) the at least one amylase has the amino acid sequence according to SEQ ID NO:3.

3. Solid detergent or cleaning agent according to claim 1 or 2, characterized in that

(1) the at least one protease comprises an amino acid sequence which corresponds to the amino acid sequence specified in SEQ ID NO:2 over its total length to at least 90%, 90.5%, 91%, 91.5%, 92%, 92.5% , 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99 %, 99.5% and up to 100% are identical; (2) the at least one protease has an amino acid substitution at at least one of positions 3, 4 and 199, preferably at two or all three positions, particularly preferably the amino acid threonine (T) at position 3 and the amino acid isoleucine (I) at position 4 ) and at position 199 the amino acid isoleucine (I);

(3) the at least one protease has the amino acid sequence according to SEQ ID NO:4.

4. Solid detergent or cleaning agent according to one of claims 1 to 3, characterized

characterized in that the concentration of the protease in the solid washing or

Cleaning agent 0.001-0.5% by weight, preferably 0.01 to 0.1% by weight, based on active protein and/or the concentration of amylase in the detergent or cleaning agent 0.0005-0.5% by weight. -%, preferably 0.001 to 0.2% by weight, based on active protein.

5. Solid detergent or cleaning agent according to one of claims 1 to 4, characterized

characterized in that the water-soluble organic builder system comprises at least one water-soluble organic builder, preferably citric acid and/or citrate, particularly particularly preferably in an amount of 5% by weight to 25% by weight, preferably 7.5 to 12.5% by weight. -% citric acid and/or 5% by weight to 25% by weight, preferably 7.5 to 12.5% by weight of citrate, preferably alkali metal citrate, more preferably sodium citrate.

6. Solid detergent or cleaning agent according to one of claims 1 to 5, characterized

characterized in that the water-soluble organic builder system contains, based on the total mass of the agent:

a) 5% by weight to 25% by weight, preferably 7.5 to 12.5% by weight, of citric acid;

b) 5% by weight to 25% by weight, preferably 7.5 to 12.5% by weight, of citrate, preferably alkali metal citrate;

c) 0 to 40% by weight, preferably 0 to 15% by weight, of alkali metal carbonate, which can also be at least partially replaced by alkali metal bicarbonate, in particular sodium carbonate;

d) 0 to 20% by weight, preferably 3 to 10% by weight, alkali metal silicate;

e) 0.005 to 10% by weight, preferably 0.02 to 2% by weight, of phosphonic acid and/or alkali metal phosphonate, in particular HEDP and/or DTPMP; and

f) 0 to 10% by weight, preferably 0.5 to 3% by weight, of polymeric polycarboxylate,

especially polyacrylate.

7. Solid detergent or cleaning agent according to one of claims 1 to 6, characterized

characterized in that the agent has 5-55% by weight, preferably 5-35% by weight, of surfactant, in particular anionic surfactants, nonionic surfactants and mixtures thereof.

8. Use of a solid detergent or cleaning agent according to one of claims 1-7 for washing textiles or cleaning hard surfaces, in particular for removing starch-containing soiling on textiles or hard surfaces.

9. A process for cleaning textiles or hard surfaces, characterized in that a solid detergent or cleaning agent according to one of claims 1-7 is used in at least one process step.