Compositions of detergents

FIELD: biotechnologies.

SUBSTANCE: detergent is described, which contains a tinting agent, a version of a parent lipase and auxiliary materials, where the parent lipase has an amino acid sequence SEQ ID NO: 2, given in the description. The method is proposed to clean and/or process the surface or fabric, including contact of the surface or fabric with the specified composition.

EFFECT: invention provides for better cleaning of a surface or a fabric as a result of the fact that combination of lipase with a tinting agent has synergetic effect.

5 cl, 5 tbl, 1 dwg, 16 ex

 

The technical field

This invention relates to compositions containing lipase and colouring agents for fabrics and methods of producing and using such products.

Prior art

The emergence of lipase enzymes suitable for use in detergents, developer creates new opportunities to improve removal of fat. These enzymes catalyze the hydrolysis of triglycerides, which constitute the major component of many widespread grease, such as the secretion of sebaceous glands, animal fats (e.g. lard, melted fat, oil) and vegetable oil (e.g. olive oil, sunflower oil, peanut oil). However, these enzymes typically have low efficiency in the first cycle of washing and typically lead to the formation of unpleasant odors arising are considered to be the result of hydrolysis of fats present in the stains from dairy products such as milk drinks, cream, butter and yogurt. Without limitation by theory, it is believed that these impurities have a tendency to the formation of induced lipase unpleasant smell, as they contain triglycerides, functionalityand short-chain (for example, C4) fatty acyl chains that after lipolysis release malodorous volatile fatty acids. Yes the e in case of improvement of the effectiveness of these enzymes issue odor remains. Thus, the use of this technology is severely limited.

We found that the combination of colouring agent for fabrics with certain variants of the lipase leads to improvement of the treatment efficiency at the same time minimizing unacceptable odor. Not wishing to be bound by theory, we can note that these beneficial effects are considered likely by the following mechanisms: selected options lipase increase the degree of fat removal that leads to improved access colouring agent to the tissue with the tissue surface and, due to this enhanced deposition. The resulting combination of improved removal of oily stains and deposits tinting dye improves the appearance of the fabric; even in case of insufficient removal of oil pollution, the hydrolysis of fats to more hydrophilic fatty acids, mono - and diglycerides leads to improved deposition tinting dye and, thus, the feeling of cleanliness; and the presence of dye molecules, postponed in oil pollution, which is on the fabric, can inhibit the activity of the enzyme, leading to the occurrence of an unpleasant smell.

The invention

The present invention relates to compositions containing a colouring agent for fabric and variant lipase with a reduced potential of education the project for a smell and a good relative efficiency, without attaching a C-terminal extension. A variant of the lipase produced by the introduction of mutations in one or more areas identified in the parent lipase. Option obtained in this way should have lipase activity, at least 80% of the activity of the parent lipase, which is expressed as the relative efficiency.

Brief description of figures

Figure 1 depicts the comparative analysis of the primary structure of lipases.

The sequence listing

SEQ ID NO: 1 depicts the DNA sequence encoding the lipase Thermomyces lanoginosus.

SEQ ID NO: 2 depicts the amino acid sequence of the lipase Thermomyces lanoginosus.

SEQ ID NO: 3 depicts the amino acid sequence of the lipase Absidia reflexa.

SEQ ID NO: 4 depicts the amino acid sequence of the lipase Absidia corymbifera.

SEQ ID NO: 5 depicts the amino acid sequence of the lipase Rhizomucor miehei.

SEQ ID NO: 6 depicts the amino acid sequence of the lipase Rhizopus oryzae.

SEQ ID NO: 7 depicts the amino acid sequence of the lipase of Aspergillus niger.

SEQ ID NO: 8 depicts the amino acid sequence of the lipase of Aspergillus tubingensis.

SEQ ID NO: 9 depicts the amino acid sequence of the lipase of Fusarium oxysporrum.

SEQ ID NO: 10 depicts the amino acid sequence of the lipase of Fusarium heterosporum.

SEQ ID NO: 11 depicts the amino acid sequence of the lipase Aspergilus oryzae.

SEQ ID NO: 12 depicts the amino acid sequence of the lipase Penicillium camemberti.

SEQ ID NO: 13 depicts the amino acid sequence of the lipase of Aspergillus foetidus.

SEQ ID NO: 14 depicts the amino acid sequence of the lipase of Aspergillus niger.

SEQ ID NO: 15 depicts the amino acid sequence of the lipase of Aspergillus oryzae.

SEQ ID NO: 16 depicts the amino acid sequence of the lipase Landerina penisapora.

A detailed description of the invention

Definition

Used here meaning the term "cleaning composition" includes, unless otherwise indicated, granular or powder-like universal or "heavy duty" cleaning agents, especially cleaning detergents for Laundry use; liquid, gel or paste-like universal cleaning agents, especially the so-called funds liquid type for heavy-duty, liquid detergent for delicate lung tissue; means for washing dishes manually or dishwasher tools for lightweight modes, especially silvopastures type; means for dishwashing machines, including the various tablet, granular, liquid types and means to reduce the amount remaining on ware drops for use in the home and in catering establishments; liquid cleaning and disinfecting agents, including antibacterial agents for hand washing, ku is the same washing means, liquid for rinsing the mouth, cleanser for the teeth and mouth, shampoos for washing machines and carpet cleaning products bathroom; shampoos and conditioners for the hair; shower gels and foam for the soul and the means for cleaning metals, as well as additives for detergents, such as bleach additives and "pencils for removing stains or tools for pre-processing.

Used here meaning the term "toning agent for fabric" means the dyes or pigments which, when incorporated in a detergent composition may be deposited on the fabric when the specified fabric is introduced into contact with the detergent solution containing the detergent composition, thereby changing the hue of the specified fabric. For the purposes of this application fluorescent optical brighteners are not considered colouring agents for fabrics.

Used here is the phrase "independently selected from the group consisting of..." means that the components or elements selected from the specified group Markush, may be the same, may be different or may be any mixture of elements.

Methods of testing disclosed in the section methods of testing this application should be used to determine the appropriate values of the parameters of the claimed inventions.

Unless otherwise indicated, all levels of the components is now or compositions include the active levels of a given component or composition, and do not take into account impurities, for example, residual solvents or by-products that may be present in commercially available sources.

All values are percentages and ratios are calculated by weight, unless otherwise indicated. All values are percentages and ratios are calculated with respect to the entire composition, unless otherwise indicated.

It should be understood that every maximum numerical limit specified in the present description includes every lower numerical limit, as if such lower numerical limits were explicitly listed here. Each minimum numerical limit specified in the present description, will enable each of the upper numerical limit, as if such upper numerical limit has been explicitly specified here. Each interval of numerical values given in this specification will include every narrower interval of numerical values within this broader interval of numerical values, as if such narrower intervals of numerical values were all explicitly specified here.

All cited documents in the relevant parts are included here as a reference; a reference to any document should not be construed as an admission that it is prior art with respect to the present invention.

Composition

Composers the AI of the present invention can contain from about 0,00003% to about 0.1%, from about 0,00008% to approximately 0.05%, or even from about 0,0001% to about 0.04 percent, colouring agent for fabric and from some of 0.0005% to about 0.1%, from about 0,001% to about 0.05 percent, or even from about 0.002% to about 0.03%, the lipase.

Such compositions can be of any shape, for example the form of washing compositions and/or compositions to be processed.

The rest of detergent compositions according to any one of the above aspects consists of one or more auxiliary materials.

Suitable variants of the lipase

Lipase compositions of the present invention is a variant lipase without C-terminal extension, but with mutations introduced in certain areas of the parent lipase, which reduces the tendency to the formation of odor.

The parent lipase

The parent lipase may be a fungal lipase with an amino acid sequence having at least 50% homology, as defined in section "Homology and comparative analysis of the primary structure, the sequence of the lipase T. lanuginosus shown in SEQ ID NO: 2.

In another preferred aspect, the parent lipase is a lipase Thermomyces.

In a more preferred aspect, the parent lipase is a lipase Thermomyces lanuginosus. In an even more preferred variant of embodiment Lipa parent is and is a lipase SEQ ID NO: 2.

The identification of areas and substitutions

The provisions stipulated in Region I - Region IV, below, represent the position of the amino acid residues in SEQ ID NO: 2. In order to find the appropriate (or homologous) positions in another lipase, use the procedure described in "Homology and comparative analysis of the primary structure.

Substitution in Region I

Region I consists of the amino acid residues surrounding the N-terminal residue of E1. In this area, preferably substituted amino acid of the parent lipase on a more positive amino acid. Region I comprises amino acid residues corresponding to the following provisions: 1-11 and 223-239. The following provisions are of particular interest: 1, 2, 4, 8, 11, 223, 227, 229, 231, 233, 234 and 236. In particular, we have identified the following substitution: X1N/*, X4V, X227G, X231R and X233R.

In a preferred variant embodiment of the parent lipase has at least 80%, such as 85% or 90%, for example at least 95%, or 96%, or 97%, or 98%, or 99%, identity with SEQ ID NO: 2. In a preferred variant embodiment of the parent lipase is identical to SEQ ID NO: 2.

Substitution in Region II

Region II consists of amino acid residues in contact with the substrate on one side acyl chains and one side alcohol part. In this area, preferably replaces the amino acid parent is coy lipase on a more positive amino acid or to a less hydrophobic amino acid. Region II encompasses amino acid residues corresponding to the following provisions: 202-211 and 249-269. The following provisions are of particular interest: 202, 210, 211, 253, 254, 255, 256, 259. In particular, we have identified the following substitution: X202G, X210K/W/A, X255Y/V/A, X256K/R and X259G/M/Q/V

In a preferred variant embodiment of the parent lipase has at least 80%, such as 85% or 90%, for example at least 95%, or 96%, or 97%, or 98%, or 99%, identity with SEQ ID NO: 2. In a preferred variant embodiment of the parent lipase is identical to SEQ ID NO: 2.

Substitution in Region III

Region III consists of amino acid residues that form a flexible structure and thereby allow the substrate to enter the active site. In this area, preferably substituted amino acid of the parent lipase on a more positive amino acid or to a less hydrophobic amino acid. Region III covers the amino acid residues corresponding to the following provisions: 82-102. The following provisions are of particular interest: 83, 86, 87, 90, 91, 95, 96, 99. In particular, we have identified the following substitution: HT, X86V and X90A/R.

In a preferred variant embodiment of the parent lipase has at least 80%, such as 85% or 90%, for example at least 95%, or 96%, or 97%, or 98%, or 99%, identity with SEQ ID NO: 2. In the most preferred embodiment, is embodied what I parent lipase is identical to SEQ ID NO: 2.

Substitution in Region IV

Region IV consists of amino acid residues that are electrostatically bound to the surface. In this area, preferably substituted amino acid of the parent lipase on a more positive amino acid. Region IV comprises amino acid residues corresponding to the following provisions: 27 and 54-62. The following provisions are of particular interest: 27, 56, 57, 58, 60. In particular, we have identified the following substitution: X27R, X58N/AG/T/P and X60V/S/G/N/R/K/A/L.

In a preferred variant embodiment of the parent lipase has at least 80%, such as 85% or 90%, for example at least 95%, or 96%, or 97%, or 98%, or 99%, identity with SEQ ID NO: 2. In a preferred variant embodiment of the parent lipase is identical to SEQ ID NO: 2.

Amino acids in other positions

The parent lipase may optionally include substitution of other amino acids, especially less than 10 or less than 5 of such substitutions. Examples are the substitution corresponding to one or more of the provisions 24, 37, 38, 46, 74, 81, 83, 115, 127, 131, 137, 143, 147, 150, 199, 200, 203, 206, 211, 263, 264, 265, 267 and 269 of the parent lipase. In a particular variant embodiment has a substitution in at least one of the positions corresponding to the positions 81, 143, 147, 150 and 249. In a preferred variant embodiment, at least one substitution selected from the group consisting the th of X81Q/E, X143S/C/N/D/A, X147M/Y, X150G/K and X249R/I/L.

Option may include substitution outside of these Regions I-IV, and the number of substitutions outside of these Areas I-IV is preferably less than six or less than five, or less than four, or less than three, or less than two, for example five or four or three or two or one. Alternatively, the option does not include any substitutions outside of these Areas I-IV.

Other substitutions can be made in accordance with principles known in the art, for example the substitution described in WO 92/05249, WO 94/25577, WO 95/22615, WO 97/04079 and WO 97/07202.

The parent lipase variants

In one aspect of this option, compared with the specified parent, contains in total at least three substitutions, and these substitutions are selected from one or more of the following groups of substitutions:

a) at least two or at least three or at least four or at least five or at least six, for example two, three, four, five or six substitutions in Region I,

b) at least one, at least two or at least three or at least four or at least five or at least six, for example one, two, three, four, five or six substitutions in Region II,

c) at least one, at least TLD is, or at least three or at least four or at least five or at least six, for example one, two, three, four, five or six substitutions in Region III,

d) and/or at least one, at least two or at least three or at least four or at least five or at least six, for example one, two, three, four, five or six substitutions in Region IV.

Option may include substitution, compared with the parent option corresponding to the substitutions listed below in Table 1.

Table 1
Some specific options
Region IRegion IIRegion IIIRegion IVOutside areas
X4V+X227G+X231R+233RX210K+X256KHT+X86VHA+X60SX150G
X227G+X231R+X233RX256KX86VX58N+X60SX150G
X231R+X233R X255Y
X231R+X233RX202G
X227G+X231R+X233RX256KX86V
X4V+X231R+X233RX58N+X60S
X231R+X233RX90RX58N+X60S
X231R+X233RX255VHA
X227G+X231R+X233RX256KX86VX58N+X60SX150G
X231R+X233RX211LX58N+X60SGM
X231R+X233R X150K

The following specific variant embodiment of the parent lipase is identical to SEQ ID NO: 2 and variants from Table 1 will, therefore, provide:

Table 2
Some specific variants of SEQ ID NO: 2
Region IRegion IIRegion IIIRegion IVOutside areas
Q4V+L227G+T231R+N233RE210K+P256KS83T+I86VS58A+V60SA150G
L227G+T231R+N233RP256KI86VS58N+V60SA150G
T231R+N233RI255Y
T231R+N233RI202G
L227G+T231R+N233RP256K
Q4V+T231R+N233RS58N+V60S
T231R+N233RI90RS58N+V60S
T231R+N233RI255VI90A
L227G+T231R+N233RP256KI86VS58N+V60SA150G
T231R+N233RF211LS58N+V60SL147M
X231R+X233RX150K

The nomenclature of amino acid modifications

When describing variants of the lipase in accordance with the invention for the convenience of the instructions use the following nomenclature: the Original amino acid(s):position(s):substituted amino acid(s).

According to this nomenclature, for example, semadeni the glutamic acid for glycine in position 195 is described as G195E. Deletion of glycine in the same position described as G195*, and the insertion of an additional amino acid residue such as lysine, is described as G195GK. In cases where specific lipase contains a "deletion" in comparison with other lipases and runs the insertion in such a position, this is indicated as *36D for insertion aspartic acid in position 36. Multiple mutations are separated by pluses, i.e: R170Y+G195E indicates mutations in positions 170 and 195 with the substitution of tyrosine and glutamic acid for arginine and glycine, respectively.

H specifies the amino acid in the parent polypeptide corresponding to position 231, when the application of the described procedure of comparative analysis of the primary structure. X231R indicates that the amino acid is substituted for R. For SEQ ID NO: 2 X denotes T and X231R, thus, indicates the substitution of T at position 231 on R. In cases where the amino acid in position (e.g., 231) can be replaced by another amino acid selected from the group of amino acids, for example the group consisting of R, R and Y, it will be marked as X231R/P/Y.

In all cases, are adopted by the IUPAC one-letter or three-letter abbreviations of amino acids.

Division of amino acids into groups

In this specification, amino acids are classified as negatively charged, positively charged or electric is Eski neutral, according to their electric charge at pH 10. Thus, negatively charged amino acids are E, D, C (cysteine) and Y, especially E and D. Positively charged amino acids are R, K and N, especially R and Neutral amino acids are G, A, V, L, I, R, F, W, S, T, M, N, Q and S, when it forms part of a disulfide bridge. Substitution with another amino acid from the same group (negatively charged, positively charged or neutral) is called a conservative substitution.

Neutral amino acids can be divided into hydrophobic or non-polar (G, A, V, L, I, R, F, W and as part of a disulfide bridge) and hydrophilic or polar (S, T, M, N, Q). In this specification, amino acids are classified as negatively charged, positively charged or electrically neutral according to their electric charge at pH 10. Thus, negatively charged amino acids are E, D, C (cysteine) and Y, especially E and D. Positively charged amino acids are R, K and N, especially R and Neutral amino acids are G, A, V, L, I, R, F, W, S, T, M, N, Q and S, when it forms part of a disulfide bridge. Substitution with another amino acid from the same group (negatively charged, positively charged or neutral) is called a conservative substitution.

Neutral amino is islote can be divided into hydrophobic or non-polar (G, A, V, L, I, R, F, W and as part of a disulfide bridge) and hydrophilic or polar (S, T, M, N, Q).

Amino acid identity

The degree of affinity between two amino acid sequences or between two nucleotide sequences is described by the parameter "identity".

For the purposes of the present invention comparative analysis of the primary structure of the two amino acid sequences is performed using the Needle program from the EMBOSS package (http://emboss.org version 2.8.0. The Needle program implements the algorithm global comparison described Needleman, S.B. and Wunsch, C.D. (1970), J. Mol. Biol., 48, 443-453. Use the substitution matrix BLOSUM62, the penalty for the start of the gap is equal to 10 and the penalty for the continuation of the gap is equal to 0.5.

The degree of identity between the amino acid sequences of the present invention (sequence according to the invention; for example, amino acids 1-269 SEQ ID NO: 2) and a different amino acid sequence ("foreign sequence") is calculated as the number of exact matches in the comparative analysis of the primary structure of two sequences divided by the length of the sequences according to the invention or the length of the "foreign sequence", whichever, whichever is shorter. The results are expressed in percent identity.

An exact match occurs when the sequence according to the invention" and "alien sequence have identical amino acid residues in the same positions overlapping. The sequence length is equal to the number of amino acid residues in the sequence (for example, the length of SEQ ID NO: 2 is equal to 269).

The parent lipase has an amino acid identity of at least 50% with lipase T. lanuginosus (SEQ ID NO: 2), especially at least 55%, at least 60%, at least 75%, at least 85%, at least 90%, 95% or 98%. In a particular variant embodiment of the parent lipase is identical to the lipase T. lanuginosus (SEQ ID NO: 2).

The above procedure can be used to calculate the identity and homology and comparative analysis of the primary structure. In the context of the present invention homology and comparative analysis of the primary structure was calculated, as described below.

Homology and comparative analysis of the primary structure

For the purposes of this invention, the degree of homology may be conveniently determined by means of computer programs known in the art, such as GAP, part of the GCG software package (Program Manual for the Wisconsin Package, Version 8, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711) (Needleman, S.B. and Wunsch, C.D. (1970), Journal of Molecular Biology, 48, 443-45), using GAP with the following settings for comparison of polypeptide sequences: the penalty for creating a gap of 3.0 and a fine for a continuing gap of 0.1.

In the present invention is appropriate (or homologous) position is as sequences of lipases Absidia reflexa, Absidia corymbefera, Rhizmucor miehei, Rhizopus delemar, Aspergillus niger, Aspergillus tubigensis, Fusarium oxysporum, Fusarium heterosporum, Aspergillus oryzea, Penicilium camembertii, Aspergillus foetidus, Aspergillus niger, Thermomyces lanoginosus (synonym: Humicola lanuginose) and Landerina penisapora determined using the comparative analysis of the primary structure, shown in Figure 1.

In order to find the homologous position in the sequences of lipases, not shown in the comparative analysis of the primary structure, the sequence of interest, compared with the sequences depicted in Figure 1. A new sequence is correlated with the primary structure of the present invention in Figure 1, using a comparative analysis of the primary structure by the method of GAP for the most homologous sequence was found using the program GAP. GAP is included in the GCG software package (Program Manual for the Wisconsin Package, Version 8, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711) (Needleman, S.B. and Wunsch, C.D. (1970), Journal of Molecular Biology, 48, 443-45). For comparison of polypeptide sequences, use the following settings: the penalty for creating a gap of 3.0 and a fine for a continuing gap of 0.1.

The parent lipase has a homology of at least 50% with lipase T. lanuginosus (SEQ ID NO: 2), especially at least 55%, at least 60%, at least 75%, at least 85%, at least 90%, 95% or 98%. In a specific embodiment, volodymyrvilensky lipase is identical to the lipase So lanuginosus (SEQ ID NO: 2).

Hybridization

The present invention also relates to isolated polypeptides having lipase activity, which is encoded by polynucleotide, hybridization under conditions of very low hardness, preferably low rigidity, it is preferable conditions of medium hardness, it is preferable conditions, medium-high stringency, more preferably under high stringency, and most preferably very high stringency, with (i) nucleotides 178-660 SEQ ID NO: 1, (ii) the cDNA sequence contained in nucleotides 178-660 SEQ ID NO: 1, (iii) a subsequence of (i) or (ii) or (iv) a complementary chain (i), (ii) or (iii) (J.Sambrook, E.F.Fritsch and T.Maniatus, 1989, Molecular Cloning, A Laboratory Manual, 2d edition, Cold Spring Harbor, New York). A subsequence of SEQ ID NO: 1 contains at least 100 contiguous nucleotides or preferably at least 200 contiguous nucleotides. Moreover, the subsequence may encode a polypeptide fragment having lipase activity.

For long probes of length at least 100 nucleotides conditions from very low to very high stringency is defined as prehybridization and hybridization at 42°C in 5×SSPE, 0.3% of SDS, 200 μg/ml degraded by hydrodynamic shear and denatured DNA salmon sperm and either 25% formamide for conditions of PTS is ery low and low stiffness, or 35% for middle and low hardness, or 50% formamide for high and very high stiffness optimally in accordance with standard procedures southern blotting for 12 to 24 hours.

For long probes of length at least 100 nucleotides material carrier at the end washed three times for 15 minutes using 2×SSC, and 0.2% SDS preferably at least at 45°C (very low stiffness), preferably at at least 50°C (low stiffness), preferably with at least 55°C (medium hardness), it is preferable if at least 60°C (low stiffness), more preferably at least 65°C (high rigidity), and most preferably at least 70°C (very high stiffness).

The DNA sequence, expression vector, a host cell, the production of lipase

The invention provides a DNA sequence encoding the lipase according to the invention, the expression vector comprising the DNA sequence, and transformed cell host containing a DNA sequence or expression vector. They can be obtained using methods known in the art. The invention also provides a method of production of lipase by cultivating the transformed host cell under conditions conducive to the production of limes is SHL, and allocation of lipase obtained from the environment. The method can be carried out in accordance with principles known in the art.

Lipase activity

- Lipase activity tributyrin at neutral pH (LU)

The substrate for the lipase is prepared by emulsification of tributyrin (glyceryltrinitrate) using gum Arabic as emulsifier. Hydrolysis of tributyrin at 30°C and pH 7 or 9 track with the title of the experiment at pH Artic. Unit of lipase activity (1 LU) equals the amount of enzyme able to release 1 μmol butyric acid per minute at pH 7.

- Benefit-Risk

The ratio of Benefit-Risk, describing the efficiency compared to a reduced risk of smell, is defined as: BR=RPavg/R. lipase Variants described in the present invention, can have a BRs is greater than 1, greater than 1.1 or even from greater than 1 to about 1000.

- The average relative efficiency

The procedure of calculating the average relative performance (RPavg) given in example 5 of the present description. Options lipases described in this invention can have (RPavg) at least 0.8, at least 1,1, at least 1.5, or even at least 2 to about 1000.

Suitable colouring agents for fabric

Fluorescent optical Brightener emit at least some visible what about the light. In contrast, colouring agents for fabrics can change the shade of the surface due to the absorption of at least part of the spectrum of visible light. Suitable colouring agents for fabrics include dyes, conjugates dye-clay and pigments that meet the requirements of test Method 1 in section test Methods of the present description. Suitable dyes include the dyes with small molecules and polymeric dyes. Suitable dyes with small molecules include dyes with small molecules selected from the group consisting of:

(1) Tris-azo direct blue dyes of the formula

where at least two of naftalina rings, and substituted sulphonate group, the ring may be substituted in position 5 by a group NH2or NHPh, X denotes benzyl or naphtalene ring, substituted up to 2 sulphonate groups and may be substituted in position 2 by a group of IT and can also be substituted by a group NH2or NHPh.

(2) Bis-azo direct violet dyes of the formula:

where Z denotes H or phenyl ring And is preferably a substituted methyl and methoxy group in the positions indicated by the arrows, ring And can also be nafcillin ring, the group Y is benzyl or naphtalene ring, substituted by sulfate groups,and may be mono - or disubstituted by methyl groups.

(3) Blue or red acid dyes of the formula

where at least one of X and Y must be an aromatic group. In one aspect both aromatic groups can be substituted benzyl or naftilos group which may be substituted is not solubilities in water groups such as alkyl, or alkyloxy-, or alloctype, X and Y cannot be substituted solubilities in water groups, such as sulfonates or carboxylates. In another aspect X is nitrosamino benzyl group, and Y denotes a benzyl group.

(4) Red acid dyes patterns

or

where is naftilos or benzyl group which may be substituted is not solubilities in water groups such as alkyl, or alkyloxy-, or alloctype, cannot be substituted solubilities in water groups, such as sulfonates or carboxylates.

(5) Dis-azo dyes of the structure

or

where X and Y independently of one another, represent each hydrogen, C1-C4-alkyl or C1-C4-alkoxy, Rα denotes hydrogen or aryl, Z represents C1-C4-alkyl, C1-C4-alkoxy; Galaga is; hydroxyl or carboxyl, n is 1 or 2 and m is 0, 1 or 2, and their respective salts and mixtures thereof.

(6) Triphenylmethane dyes of the following structures

,

,

,

,

and/or

and mixtures thereof. In another aspect suitable dyes with small molecules include dyes with small molecules selected from the group consisting of dyes with numbers in Colour Index (Society of Dyers and Colourists, Bradford, UK) direct violet 9, direct violet 35, direct violet 48, direct violet 51, direct violet 66, direct blue 1, direct blue 71, direct blue 80, direct blue 279, acid red 17, acid red 88, acid red 150, acid violet 15, acid violet 17, acid violet 24, acid violet 49, acid blue 15, acid blue 17, acid blue 29, acid blue 40, acid blue 75, acid blue 80, acid blue 83, acid blue 90 and acid blue 113, basic violet 1, basic violet 3, basic violet 4, basic violet 10, basic violet 35, basic blue 3, basic blue 16, basic blue 22, basic blue 47, the basis of the nogo blue 66, basic blue 75, basic blue 159, and mixtures thereof.

Suitable polymeric dyes include polymeric dyes selected from the group consisting of polymers containing conjugated Chromogens (conjugates of the dye-polymer), and polymers with Chromogens, copolymerizable in the main chain of the polymer, and mixtures thereof.

In another aspect, suitable polymeric dyes include polymeric dyes selected from the group consisting of substantive dyes for fabrics sold under the name Liquitint® (Milliken, Spartanburg, South Carolina, USA), the conjugates of the dye-polymer formed from at least one reactive dye and a polymer selected from the group consisting of polymers comprising a fragment selected from the group consisting of hydroxyl groups, primary amino groups, secondary amino groups, Tilney groups and mixtures thereof. In yet another aspect, suitable polymeric dyes include polymeric dyes selected from the group consisting of Liquitint® (Milliken, Spartanburg, South Carolina, USA), violet CT, carboxymethylcellulose (CMC), conjugated with reactive blue, reactive violet or reactive red dye, such as CMC, conjugated with CL reactive blue 19, which is sold by the company Megazyme, Wicklow, Ireland, under the trademark AZO-CM-CELLULOSE, product code S-ACMC, and mixtures thereof.

Suitable conjuga the s dye-clay include conjugates dye-clay, selected from the group comprising at least one cationic/basic dye and smectite clay and mixtures thereof. In another aspect suitable conjugates dye-clay include conjugates dye-clay selected from the group consisting of one cationic/basic dye selected from the group consisting of basic yellow C.I. 1-108, basic orange C.I. 1-69, basic red C.I. 1-118, basic violet C.I. 1-51, basic blue C.I. 1-164, basic green C.I. 1-14, basic brown C.I. 1-23, basic black C.I. 1-11, and clay selected from the group consisting of montmorillonite clay, hectorite clay, aponitolau clay and mixtures thereof. In another aspect suitable conjugates dye-clay include conjugates dye-clay selected from the group consisting of a conjugate of montmorillonite and the main blue V7 C.I. 42595, conjugate, montmorillonite and basic blue B9 C.I. 52015, conjugate, montmorillonite and basic violet V3 C.I. 42555, conjugate, montmorillonite and the main green G1 C.I. 42040, conjugate, montmorillonite and the main red R1 C.I. 45160, conjugate, montmorillonite and C.I. basic black 2, the conjugate of hectorite and basic blue V7 C.I. 42595, conjugate of hectorite and basic blue B9 C.I. 52015, conjugate of hectorite and basic violet V3 C.I. 42555 the conjugate of hectorite and the main green G1 C.I. 42040, conjugate of hectorite the main red R1 C.I. 45160, conjugate of hectorite and C.I. basic black 2, the conjugate of saponite and basic blue V7 C.I. 42595, conjugate of saponite and basic blue B9 C.I. 52015, conjugate of saponite and basic violet V3 C.I. 42555, conjugate of saponite and the main green G1 C.I. 42040, conjugate of saponite and primary red R1 C.I. 45160, conjugate of saponite and C.I. basic black 2, and mixtures thereof.

Suitable pigments include pigments selected from the group consisting of flavanone, indanthrene, chlorinated indanthrene containing from 1 to 4 chlorine atoms, piraterna, dichloropentane, monobromobimane, dibromodichloromethane, tetrabromoethane, diimide perylene-3,4,9,10-tetracarbonyl acid, where kidnie groups can be unsubstituted or substituted C1-C3-alkyl, or phenyl, or heterocyclic radical, and where the phenyl and heterocyclic radicals may optionally carry substituents which do not impart solubility in water, amides intraperitoneally acid, violation, isofilename, dioxazine pigments, copper phthalocyanine, which may contain up to 2 chlorine atoms in the molecule, polihlorbifenilov copper or polybromodiphenyl copper containing up to 14 atoms of bromine in the molecule, and mixtures thereof. In another aspect suitable pigments include pigments selected from the group consisting of ultramarine, the first blue (C.I. pigment blue 29), ultramarine violet (C.I. pigment violet 15), and mixtures thereof.

The above colouring agents for fabrics can be used in combination (can be used any mixture of colouring agents for fabric). Suitable colouring agents for fabrics can be purchased from Aldrich, Milwaukee, Wisconsin, USA; Ciba Specialty Chemicals, Basel, Switzerland; BASF, Ludwigshafen, Germany; Dayglo Color Corporation, Mumbai, India; Organic Dyestuffs Corp., East Providence, Rhode Island, USA; Dystar, Frankfurt, Germany; Lanxess, Leverkusen, Germany; Megazyme, Wicklow, Ireland; Clariant, Muttenz, Switzerland; Avecia, Manchester, UK, and/or manufactured in accordance with the examples in the present invention.

Auxiliary materials

Although it is not essential for the purposes of the present invention, non-limiting list of excipients described here and further is suitable for use in the compositions of the present invention and may be desirable for inclusion in some of the variants of embodiment of the invention, for example, to ensure or enhance the treatment efficiency of the processing of the substrate in need of cleaning, or for modification of the aesthetic characteristics of the detergent, as in the case of perfumes, pigments, dyes, etc. as to the Exact nature of these additional components, and levels of their content will depend on the physical form of the composition and nature of the cleanup operation, which is th they should be used. Suitable support materials include, without limitation, surfactants, core components, chelating agents, agents inhibiting the transfer of dyes, dispersants, additional enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, pre-prepared percolate, polymeric dispersants, agents to remove dirt particles and prevent them from re-deposition, brighteners, pinagsama additives, dyes, odorants, sastifactory patterns, fabric softeners, carriers, girotropnye substances, processing AIDS, solvents and/or pigments. In addition to the below description, are suitable examples of such other auxiliary substances and the levels of their use are shown in U.S. patent No. 5576282, 6306812 B1 and 6326348 B1, which are incorporated here as reference.

As mentioned, the auxiliary ingredients are not essential to the inventive compositions. Thus, in certain variations of embodiments of the inventive compositions do not contain one or more of the following materials, auxiliary chemicals: surfactants, core components, chelating agents, agents inhibiting the transfer of dyes, dispersants, additional enzymes, and stabilizer the Torah enzymes catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, pre-prepared percolate, polymeric dispersants, agents to remove dirt particles and prevent them from re-deposition, brighteners, pinagsama additives, dyes, odorants, sastifactory patterns, fabric softeners, carriers, girotropnye substances, processing AIDS, solvents and/or pigments. However, in the presence of one or more excipients that may be present, such one or more of the excipients listed below.

Bleaching agents. Detergent compositions of the present invention can include one or more bleaching agents. Suitable bleaching agents other than the bleach catalysts include fotoatelier, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, pre-prepared percolate and mixtures thereof. In General, in the case of a bleaching agent composition of the present invention may include from about 0.1% to about 50% or even from about 0.1% to about 25% of the whitening agent to the weight of this detergent composition. Examples of suitable bleaching agents include:

(1) fotoatelier, for example sulphonated phthalocyanine zinc;

(2) the prior is about prepared percolate: suitable pre-prepared percolate include, without limitation, compounds selected from the group consisting of percarbonic acids and salts, peroralnyh acids and salts, perekidnyh acids and salts, peroxymonosulfuric acids and salts, for example Oxzone®, and mixtures thereof. Suitable percarbonate acid include hydrophobic and hydrophilic percolate having the formula R-(C=O)O-O-M, where R denotes an alkyl group, optionally branched, containing, in cases where percolate is hydrophobic, from 6 to 14 carbon atoms or from 8 to 12 carbon atoms and, in those cases where percolate is hydrophilic, less than 6 carbon atoms or even less than 4 carbon atoms; and M represents a counterion, such as sodium, potassium or hydrogen;

(3) sources of hydrogen peroxide, for example inorganic perpetrate salts, including alkali metal salts such as sodium salt of perborate (usually mono - or tetrahydrate), percarbonate, persulfate, perphosphate, perserikatan salts and mixtures thereof. In one aspect of the invention inorganic perpetrate salt selected from the group consisting of sodium salts of perborate, percarbonate, and mixtures thereof. In the case of using inorganic perpetrate salt is typically present in an amount of from 0.05 to 40 wt.%. or from 1 to 30% wt. from the total amount of the composition and is typically included in such compositions in the form of a crystalline solid ve is esta, which can be the floor. Suitable coatings include inorganic salts such as silicate, carbonate or borate salts of alkali metals or mixtures thereof, or organic materials such as water-soluble or dispergirujutsja polymers, waxes, oils or fatty soap; and

(4) the bleaching activators having the formula R-(C=O)-L, where R denotes an alkyl group, optionally branched, containing, in those cases, when the bleach activator is hydrophobic, from 6 to 14 carbon atoms or from 8 to 12 carbon atoms and, in those cases, when the bleach activator is hydrophilic, less than 6 carbon atoms or even less than 4 carbon atoms; and L denotes outgoing group. Examples of suitable waste groups are benzoic acid and its derivatives, and especially bansilalpet. Suitable bleach activators include dodecanesulfonate, technologiessalon, technologiesin acid or its salts, 3,5,5-trimethylcyclohexylisocyanate, tetraacetylethylenediamine (TAED) and nonanoyloxybenzenesulfonate (NOBS). Suitable bleach activators are also disclosed in WO 98/17767. Although it may be used any suitable bleach activator, in one aspect of the invention which is the subject of the invention of the washing composition may include NOBS, TAED or mixtures thereof.

In the case of the AE's presence percolate and/or bleach activator is typically present in the composition in an amount of from about 0.1 to about 60 wt.%, from about 0.5 to about 40 wt.%. or even from about 0.6 to about 10% wt. from the composition. One or more hydrophobic perkiset or its precursors may be used in combination with one or more hydrophilic percolate or its precursor.

Number source of hydrogen peroxide and percolate or bleach activator may be selected so that the molar ratio of available oxygen (from the source of peroxide) to percolate is from 1:1 to 35:1 or even 2:1 to 10:1.

Surfactants. Detergent compositions in accordance with the present invention may include a surfactant or surfactant, where the surfactant may be selected from nonionic surfactants, anionic surfactants, cationic surfactants, ampholytic surfactants, zwitterionic surfactants, polupryamykh nonionic surfactants and mixtures thereof. In the presence of surfactant is typically present in an amount of from about 0.1% to about 60%, from about 1% to about 50% or even from about 5% to about 40% wt. from being the subject of the invention composition.

The main components. Detergent composition for infusion is to him the invention may include one or more of the main components of the detergent or system main component. In the case of a main component which is the subject of the invention, the composition will typically include at least about 1%, from about 5% to about 60%, or even from about 10% to about 40% of the main component of the weight of the subject invention compositions. The main components include, without limitation, polyphosphate salts of alkali metals, ammonium and alkanolamine, silicates of alkali metals, carbonates of alkaline earth and alkali metal aluminosilicate core components and polycarboxylate compounds, ethers of hydroxypolycarboxylic, copolymers of maleic anhydride with ethylene or vinylmation ether, 1,3,5-trihydroxybenzene-2,4,6-trisulfonic acid and carboxymethylcysteine acid, various salts of alkali metals, ammonium and substituted ammonium polixeni acids, such as ethylenediaminetetraacetic acid, nitrilotriacetic acid, and polycarboxylate, such as malletova acid, succinic acid, citric acid, accidentally acid, primulina acid, benzene-1,3,5-tricarboxylic acid, carboxymethylcysteine acid and its soluble salts.

Chelating agents. Detergent compositions of the present invention may contain a chelating agent. Suitable chelating agents include chelating agents is s copper iron and/or manganese, and mixtures thereof. In case of using a chelating agent which is the subject of the invention, the composition may include from about 0,005% to about 15% or even from about 3.0% to about 10% chelating agent by weight of the subject invention compositions.

Agents that inhibit the migration of the dye. Detergent compositions of the present invention can also include one or more agents, inhibiting the migration of the dye. Suitable polymeric agents, inhibiting the transfer of dyes include, without limitation, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polivinilatsetatny and polyvinylimidazole or mixtures thereof. In the case of the presence in the subject invention compositions of agents that inhibit the transfer of dye can be present in an amount of from about 0,0001% to about 10%, from about 0.01% to about 5% or even from about 0.1% to about 3% by weight of the composition.

The clarifiers. Detergent compositions of the present invention may also contain additional components that may tint articles being washed, such as fluorescent brighteners. Suitable levels of fluorescent brighteners include low levels of from about 0.01 to, from approximately 0.05, from about 0.1 or daget approximately 0.2 wt.%, to the upper levels of 0.5 or even to 0.75 wt.%.

Dispersants. The compositions of the present invention can also contain dispersants. Suitable water-soluble organic materials include Homo - or copolymer acids or their salts in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by no more than two carbon atoms.

Additional enzymes. Detergent compositions can include one or more enzymes which provide cleaning performance and/or fabric care. Examples of suitable enzymes include, without limitation, hemicellulase, peroxidase, protease, cellulase, xylanase, lipase, phospholipase, esterase, cutinase, pectinase, mannanase, pectolyase, keratinase, reductase, oxidase, phenoloxidase, lipoxidase, ligninase, pullulanase, tannaz, pentosanase, Malagasy, β-glucanase, arabinosidases, hyaluronidase, chondroitinase, laccase, and amylases, or mixtures thereof. A typical combination is an enzyme cocktail, which may contain, for example, protease and lipase in combination with amylase. In the case of presence in the detergent composition of the above-mentioned additional enzymes may be present in amount from about 0.00001% to about 2%, from about 0,0001% to about 1% or even from about 0,001% to about 0.5% of enzyme Bel is and the weight of the composition.

Stabilizers enzymes. Enzymes for use in detergents can be stabilized in different ways. The enzymes used in the present invention can be stabilized by the presence in the finished compositions of water-soluble sources of calcium ions and/or magnesium, which ensure the delivery of such ions to the enzymes. In the case of aqueous compositions, containing a protease, for additional stability can be added reversible protease inhibitor, such as a boron compound.

The catalytic metal complexes. The claimed detergent composition can include catalytic metal complexes. One type of metal-containing bleaching catalyst system is a catalyst comprising a transition metal cation with a specific catalytic activity whitening, such as the cations of copper, iron, titanium, ruthenium, tungsten, molybdenum or manganese, an auxiliary metal cation having little or no catalytic activity whitening, such as the cations of zinc or aluminum, and prescribe, having defined stability constants with the catalytic and auxiliary metal cations, particularly ethylenediaminetetraacetic acid, ethylenediaminetetra (methylenephosphonate acid) and their soluble salts. Such was pushing the congestion disclosed in US 4430243.

Optionally, the compositions of the present invention can be catalyzed by manganese compounds. Such compounds and levels of use are well known in the art and include, for example, catalysts based on manganese disclosed in US 5576282.

Cobalt catalysts whitening suitable for use in this invention are known and described, for example, in US 5597936; US 5595967. Such cobalt catalysts easily get known methods, such as described, for example, in US 5597936 and US 5595967.

The compositions of the present invention is also suitable to include the complex of the transition metal with ligands, such as bispinosa (WO 05/042532 A1) and/or hard macropolicies ligands - abbreviated marked "MRLs". In practice, and without limitation, the compositions and methods of the present invention can be adjusted in order to provide at least one part per hundred million of the active particles MRL in the aqueous washing medium, and will typically provide from about 0,005 million-1to about 25 million-1from approximately 0.05 million-1up to about 10 million-1or even from about 0.1 million-1to about 5 million-1MRL in the washing solution.

Suitable transition metals in the bleaching catalyst based on transition metal of the present invention include, for example the EP, manganese, iron and chromium. Suitable MRLs include 5,12-diethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane.

Suitable MRLs on the basis of transition metals easily get known methods, such as described, for example, in WO 00/32601 and US 6225464.

The solvents. Suitable solvents include water and other solvents, such as lipophilic fluid. Examples of suitable lipophilic liquid media include siloxanes, other silicones, hydrocarbons, simple glycol ethers, derivatives of glycerol, such as ethers, glycerin, perfluorinated amines, perfluorinated and hydrotherapie solvents, low-volatile non-fluorinated organic solvents, diol solvents, other environmentally safe solvents and mixtures thereof.

Methods of obtaining compositions

The compositions of the present invention can be prepared in any suitable form and produced by any method chosen by the originator, non-limiting examples of which are described in the examples of the application and in the US 4990280; US 20030087791 A1; US 20030087790 A1; US 20050003983 A1; US 20040048764 A1; US 4762636; US 6291412; US 20050227891 A1; EP 1070115 A2; US 5879584; US 5691297; US 5574005; US 5569645; US 5565422; US 5516448; US 5489392; US 5486303, which are all included in the present invention as references.

Method of use

The present invention includes a method of cleaning and/or processing site, including the surface or fabric. This JV is the property includes the introduction phase in contact variant embodiment of the inventive cleaning compositions undiluted or diluted in the washing solution, with at least part of a surface or fabric, and then, optionally, rinsing the surface or fabric. Surface or the fabric may be subjected to a stage of washing before the above-mentioned stage rinse. For the purposes of the present invention washable includes, without limitation, washing and mechanical stirring. As will be clear to experts in this field, the detergent compositions of the present invention are ideal for use when washing. Accordingly, the present invention includes a method of washing fabric. The method includes the introduction phase in contact with the fabric to be washed, with the specified detergent to the washing solution containing at least one variant embodiment of the inventive detergent compositions, detergent additive, or a mixture. The fabric can include almost any fabric, suitable for washing in normal conditions of use. The solution preferably has a pH from about 8 to about 10.5V. The composition can be used in concentrations of from about 500 million-1to about 15000 million-1in the solution. Water temperature typically ranges from about 5°to about 90°C. the Ratio of water:fabric typically is from about 1:1 to about 30:1.

TEST METHOD 1

Below is the Protocol for determining whether a cu is Khabibullina or pigment material colouring agent for fabric for purposes of this invention.

1) Fill two targetmetadata vessel of 800 ml of water from the municipal water supply Newcastle upon Tyne, UK (total hardness approx 12 Grand on the American gallon is supplied Northumbrian Water, Pity Me, Durham, Co. Durham, UK).

2) Install the vessels in ergotimer at a given water temperature 30°C and the stirring speed is 40 rpm throughout the experiment.

3) is Added to each vessel 4.8 g of detergent IEC-B (IEC 60456 Reference basic detergent for washing machines type b) was delivered wfk, the municipalities of brüggen-Bracht, Germany.

4) After two minutes add in the first vessel 2.0 mg active coloring tools.

5) After one minute, add in each vessel 50 g of tissue from non-compacted cotton for jackets (supplied by Warwick Equest, Consett, County Durham, UK), cut into samples of 5 cm × 5 cm

6) After 10 minutes, pour the liquid from the vessel and again fill with cold water from the municipal water supply Newcastle upon Tyne (16°C).

7) After 2 minutes, rinse out the cloth.

8) Repeat stages 3-7 three more times using the same procedure.

9) Collect and dry on the rope fabric in the room for 12 hours.

10) Analyze the samples using a spectrometer Hunter Miniscan with light source D65 and UVA cut-off filter, to obtain the value of a Hunter (the axis of the red-green) and Hunter b (axis yellow-green).

11) Average values of Hunter and Hunter b DL is each set of tissues. If the fabric treated with the tested dye, show the average difference of hue more than 0.2 units of a-axis or b axis, it is considered toning agent for fabric purposes of the present invention.

EXAMPLES

Examples of lipases

Chemicals used as buffers and substrates, are commercial products, at least chemically pure.

Environment and solutions: LAS (Surfac PS™) and zeolite A (Wessalith P™). Other ingredients used are standard laboratory reagents.

- Materials: EMRE from EMPA St. Gallon, Lerchfeldstrasse 5, CH-9014 St. Gallon, Switzerland.

Example 1: Production of enzyme

A plasmid containing the gene encoding the lipase, design and transform in a suitable cell host, using standard methods known to experts.

Fermentation is carried out as batch fermentation with water using a constant temperature environment equal to 34°C, and the initial volume of 1.2 liters. The initial pH of the medium set equal to 6.5. After the pH will increase to 7.0, it is support by adding 10% H3PO4. The level of dissolved oxygen in the medium is controlled by varying the speed mixing using a constant speed aeration, equal to 1.0 liter of air per liter of medium per minute. The feed rate support the claim constant throughout the periodic phase fermentation with water.

Uterine environment contains maltose syrup as a carbon source, urea and yeast extract as nitrogen source and a mixture of trace metals and salts. The raw material is added continuously during the periodic phase fermentation with water, contains maltose syrup as a carbon source, while yeast extract and urea added to provide sufficient amount of nitrogen.

Purification of lipase can be carried out using standard methods known in the art, for example by filtering a fermentation supernatant and subsequent hydrophobic chromatography and anion exchange, for example as described in EP 0851913, Example 3.

Example 2: AMSA - Automated analysis with a mechanical load to calculate the relative performance (RP)

Test variants of enzymes by the application using automated analysis with manual load (AMSA). Using test AMSA can be analyzed washing ability of a large number of small volumes of solutions of enzyme-detergent. Plate AMSA has a number of slots to test solutions and cover tightly presses designed for washing textile sample to all the openings of the slots. During washing the plate, test solutions, those who style and cover vigorously shaken for to bring the test solution in contact with the textile and applying mechanical stress. A more detailed description is given in WO 02/42740, especially the paragraph "Special variants of embodiment of the method" on pages 23-24. Containers containing test solutions of detergent, are cylindrical holes (diameter 6 mm, depth 10 mm) in the metal plate. The soiled fabric (test material) is placed on the metal plate and used as covers and seals for containers. Another metal plate is placed on the soiled fabric to prevent leakage from each container. Two metal plates together with the contaminated cloth fluctuate up and down with a frequency of 30 Hz, with an amplitude of 2 mm

The analysis is performed in the experiment shown below.

Table 3
The tested solution0.5 g/l LAS
0.52 g/l Na2CO3
1.07 g/l zeolite And
0.52 g/l triacrylate
The volume of the test solution160 ál
pHAs eating is (≈9,9)
The wash20 minutes
Temperature30°C
Water hardness15°dH
The ratio of Ca2+/Mg2+/NaHCO3: 4:1:7,5
The concentration of enzyme in the tested solution0,125, 0,25, 0,50, 1.0 mg of enzyme protein per liter (mg PH.B./l)
DryingEfficiency: after washing the pieces of textile, wash immediately with tap water and dried in air at 85°C for 5 minutes
Smell: after washing the pieces of textile, wash immediately with tap water and dried at room temperature (20°C) for 2 hours
The tested materialSample cream-turmeric, as described below (as cotton textiles used EMRA)

Samples of the cream-turmeric is prepared by mixing 5 g turmeric (Santa Maria, Denmark) with 100 g of cream (38% fat, Aria, Denmark) at 50°C, the mixture is left at this temperature for about 20 minutes and filtered (50°C) to remove undissolved particles. The mixture is cooled to 20°C, samples of cotton fabric EMRA p is Gruaud in a mixture of cream-turmeric and then leave to dry at room temperature overnight and frozen until use. Sample preparation cream-turmeric disclosed in the patent application RA 200500775, filed may 27, 2005.

The efficiency of the variant enzyme is measured as the brightness of colouring textile samples, washed with this particular variant of the enzyme. The brightness can also be expressed as the intensity of the light reflected from the textile sample when illuminated with white light. When the textile is dirty, the reflected light intensity lower than that of pure textiles. Thus, the intensity of the reflected light can be used to measure detergency variant of the enzyme.

Color measurement is performed with the help of a professional flatbed scanner (PFU DL2400pro), which is used to obtain images of the washed textile samples. The scans do with the resolution of 200 dpi and 24-bit color depth. For accurate results, the scanner often calibrated using reflective Etalon Kodak IT8.

To get the value of the light intensity for scanned images using a specially designed software program (Novozymes Color Vector Analyzer). The program samples the 24-bit pixel values from the image and converts them into values of red, green and blue (RGB). The intensity value (Int) is calculated by vector addition of the RGB values and then define the length of the floor is the observation vector:

.

Washing capacity (P) of the options is calculated by the formula:

R=Int(v)-Int(r), where

Int(v) denotes the intensity value of light to the surface of textiles, washed with the test enzyme, and Int(r) denotes the intensity value of light to the surface of textiles, washed without the tested enzyme.

Point estimation of the relative efficiency is defined as the result of washing AMSA in accordance with the following definition: point relative performance (RP) represents the ratio of the sum of the efficacies (R) of the tested variants of the enzymes to the reference enzyme: RP=P(test enzyme)/R(reference enzyme). RPavgindicates the average relative efficiency compared to the reference enzyme at all four concentrations of the enzyme (0,125, 0,25, 0,5, 1.0 mg PH.B./l)

RPavg=avg(RP(0,125), RP(0,25), RP(0,5), RP(1,0))

It is believed that the variant has improved washing ability, if its higher than those of the benchmark. In the context of the present invention the reference enzyme is a lipase SEQ ID NO: 2 by substitution T231R+N233R.

Example 3: GC - Gas chromatograph - to calculate the risk factor

The allocation of butyric acid from the sample, washed with a lipase, measured by gas chromatography with solid-phase microextraction (SPME-GC) using the following methodology. Four pieces of textiles (5 mm in diameter), washed in solution indicated in Table 3, containing 1 mg/l lipase, transferred into a vial for gas chromatograph (GC). Samples will be analyzed by the instrument Varian 3800 GC equipped with a Stabilwax-DA column Integra-Guard (30 m, 0.32 mm ID (inner diameter) and 0.25 µm df) and fiber Carboxen PDMS SPME (75 microns). Each sample is pre-incubated for 10 min at 40°C and then 20 min sampling using SPME fiber space over pieces of textile. The sample is then injected into the column (injector temperature = 250°C). Consumption, column = 2 ml helium/min Temperature gradient of the furnace column: 0 min = 40°C, 2 min = 40°C, 22 min = 240°C, 32 min = 240°C. Butyric acid is detected using a flame ionization detector (FID), and the amount of butyric acid is calculated using the standard curve for butyric acid.

The risk factor of smell R variant lipase represents the ratio between the amount of released butyric acid from a sample, which is washed with a variant of the lipase, and the amount of released butyric acid from a sample, which is washed with a lipase SEQ ID NO: 2 by substitution T231R+N233R (reference enzyme), after amending both values on the amount of butyric acid released from a sample, which washed without lipase. Risk (R) for options calculated in accordance with the following the formula:

Smell = measured in microgram quantity of butyric acid released during 1 mg enzyme protein/l adjusted for idle experience

αthe tested enzyme= smellthe tested enzymeFree - running experience

αthe reference enzyme= smellthe reference enzymeFree - running experience

R=αthe tested enzymethe reference enzyme

It is considered that option has reduced odor compared to the benchmark, if the ratio R is less than 1.

Example 4: the Ratio of activity (LU) to the optical density at 280 nm

The ratio of activity to the optical density at 280 nm is determined using the following analysis.

LU/A280:

The lipase activity is determined as described above in section Lipase activity. Measure the optical density of the lipase at 280 nm (A) and calculate the ratio LU/A280. Relative LU/A280 is calculated as LU/A280 option divided by LU/A280 of the reference enzyme. In the context of the present invention the reference enzyme is a lipase SEQ ID NO: 2 by substitution T231R+N233R.

Example 5: BR - Benefit-Risk

The ratio of Benefit-Risk, describing the relation of efficiency and reduced risk of smell, is defined as follows: BR=RPavg/R.

It is believed that the variant has improved washing ability and reduced odor, if the ratio of BR is greater than 1.

Using the methods described above the following results were obtained.

Reference lipase and options 7 and 8 in Table 4 are described in WO 2000/060063.

Example 6

BR - Benefit-Risk

Measure the ratio of Risk-Benefit for the cases listed in Table 5. The ratio of Benefit-Risk is measured in the same manner as described in example 5, and the obtained values were above 1 for all listed options.

Reference lipase described in WO 2000/060063.

EXAMPLES of COMPOSITIONS

Unless otherwise specified, the materials can be obtained from Aldrich, P.O. Box 2060, Milwaukee, WI 53201, USA.

Examples 1-6

Granular detergent compositions for washing, intended for hand washing or washing machines top loading

1 (% wt.)2 (% wt.)3 (% wt.)4 (% wt.)5 (% wt.)6 (% wt.)
Line Las2022201520 20
With12-14-dimethylsiloxy-ethylammonium chloride0,7110,60,00,7
AE3S0,90,00,90,00,00,9
AE0,00,50,0131
Sodium tripolyphosphate233023171223
Zeolite And0,00,00,00,0100,0
1.6 has been released silicate (ratio of SiO2:Na2O=1,6:1)777 777
Sodium carbonate151415181515
Polyacrylate MW 450010,0111,51
Carboxymethylcellulose111111
Savinase® 32,89 mg/g0,10,070,10,10,10,1
Natalase® 8,65 mg/g0,10,10,10,00,10,1
Lipase18 mg/g0,030,070,3 0,10,070,4
Fluorescent Brightener 10,060,00,060,180,060,06
Fluorescent Brightener 20,10,060,10,00,10,1
Diethylenetriaminepenta-acetic acid0,60,30,60,250,60,6
MgSO41110,511
Percarbonate sodium0,05,20,10,00,00,0
Perborate sodium monohydrate4,4 0,03,852,090,783,63
NOBS1,90,01,66-0,330,75
TAED0,581,20,51-0,0150,28
Sulfonated phthalocyanine zinc0,0030-0,00120,00300,0021-
S-ACMC0,10,06---
Direct violet 9--0,00030,00050,0003-
Ultramarine blue- ----0,2
Sulfate/moistureUp to 100%Up to 100%Up to 100%Up to 100%Up to 100%Up to 100%

Any of the above compositions are used for washing fabrics at a concentration of 600-10000 million-1in water at typical median conditions 2500 million-1, 25°C and the ratio of water : fabric 25:1.

Examples 7-10

Granular detergent compositions for washing, intended for automatic washing machines front load

7 (% wt.)8 (% wt.)9 (% wt.)10 (% wt.)
Line Las87,176,5
AE3S04,805,2
Alkylsulfate 1010
AE2,203,20
C10-12-dimethylhydroxylamine chloride0,750,940,980,98
Crystalline layered silicate (δ-Na2Si2O5)4,104,80
Zeolite And200170
Citric acid3534
Sodium carbonate15201420
Silicate 2R (SiO2:Na2O in the ratio 2:1)0,0800,110
Dirt repellent agent0,750,720,710,72
Copolymer of acrylic acid/maleic acid1,13,71,03,7
Carboxymethylcellulose0,151,40,21,4
Protease (56,00 mg active substance/g)0,370,40,40,4
Termamyl® (21,55 mg active substance/g)0,30,30,30,3
Lipase(18,00 mg active substance/g)0,050,150,10,5
Natalase® (8,65 mg active substance/g)0,10,140,140,3
TAED3,64,03,64,0
Percarbonate1313,21313,2
Na-salt Ethylenediamine-N,N'-dinternal acid, (S,S)isomer (EDDS)0,20,20,20,2
Hydroxyethylphosphonate (HEDP)0,20,20,20,2
MgSO40,420,420,420,42
Flavor0,50,60,50,6
The agglomerate of antifoam0,050,10,050,1
Soap0,450,450,450,45
The sodium sulfate22332430
Sulfonated phthalocyanine zinc (active)0,00070,00120,0007-
S-ACMC0,010,01-0,01
Direct violet 9 (active)--0,00010,0001
Water and differentUp to 100%Up to 100%Up to 100%Up to 100%

Any of the above compositions are used for washing fabrics at a concentration of 10000 million-1in water, 20-90°C, with a ratio of water : fabric 25:1. The typical pH of approximately 10.

Examples 11-16

Liquid detergent composition for washing heavily soiled items

11 (% wt.)12 (% wt.)13 (% wt) 14 (% wt.)15 (% wt.)16 (% wt.)
AES C12-15-alkylators(1.8)sulfate111046,326,08,2
Line Las4083,34,03,0
HSAS05,13020
Formate sodium1,60,091,20,041,61,2
Sodium hydroxide2,3the 3.81,71,92,31,7
Monoethanolamine1,4 1,4901,00,71,351,0
Diethylene glycol5,50,04,10,05,5004,1
Non-ionic0,40,60,30,320,3
The chelator0,150,150,110,070,150,11
Citric acid2,53,961,881,982,51,88
C12-14-dimethylaminomethyl0,30,730,230,370,30,225
C12-18fatty acid 0,81,90,60,990,80,6
Borax1,431,51,10,751,431,07
Ethanol1,541,771,150,891,541,15
Ethoxylated (EO15) Tetraethylenepentamine10,30,330,230,170,00,0
Ethoxylated hexamethylenediamine were20,80,810,60,40,00,0
1,2-Propandiol0,06,60,03,30,00,0
Protease*36,436,427,318,236,427,3
Mannaway®*1,11,10,80,61,10,8
Natalase®*7,37,35,53,77,35,5
Lipase*103,20,53,22,43,2
Liquitint® violet CT (active)0,0060,002---0,002
S-ACMC--0,010,050,010,02
Water, flavouring, dyes and other componentsRestRestRestRestRestRest

Raw materials and notes examples of compositions 1-16
Line Las with an average length of the aliphatic carbon chain C11-C12was delivered Stepan, Northfield, Illinois, USA
C12-14-dimethylhydroxylamine chloride was delivered Clariant GmbH, Sulzbach, Germany
AE3S is a12-15-alkylators(3)sulfate was supplied Stepan, Northfield, Illinois, USA
AE7 is an ethoxylate C12-15-alcohol with an average degree of amoxilonline 7 was delivered Huntsman, Salt Lake City, Utah, USA
Sodium tripolyphosphate was delivered Rhodia, Paris, France
Zeolite - supplied Industrial Zeolite (UK Ltd, Grays, Essex, UK
1.6 has been released Silicate was delivered Koma, Nestemica, Czech Republic
Sodium carbonate was delivered Solvay, Houston, Texas, USA
Polyacrylate MW 4500 - was supplied by BASF, Ludwigshafen, Germany
CMC Finnfix® BDA was delivered CPKelco, Arnhem, Netherlands
Savinase®, Natalase®, Termamyl®, Mannaway® was delivered Novozymes, Bagsvaerd, Denmark
Options lipase 1-5 described in example 5, table 4, and combinations thereof.
Fluorescent Brightener 1 is Tinopal® AMS, fluorescent Brightener 2 is a Tinopal® CBS-X
Sulfonated phthalocyanine zinc and direct violet 9, representing Pergasol® Violet BN-Z, was delivered Ciba Specialty Chemicals, Basel, Switzerland
Diethylenetriaminepentaacetic acid was supplied by Dow Chemical, Midland, Michigan, USA
Percarbonate sodium was delivered Solvay, Houston, Texas, USA
Perborate of sodium was supplied by Degussa, Hanau, Germany
NOBS is a sodium nonanoyloxybenzenesulfonate was delivered Eastman, Batesville, Arkansas, USA
TAED is tetraacetylethylenediamine were supplied under the trademark Peractive® by the company Clariant GmbH, Sulzbach, Germany
S-ACMC is a carboxymethyl cellulose, conjugate with jet blue C.I. 19, sold by the company Megazyme, Wicklow, Ireland under the trademark AZO-CM-CELLULOSE, product code S-ACMC
Ultramarine blue was delivered Holliday Pigments, Kingston upon Hull, UK
Dirt repellent agent is Repel-o-tex® PF - supplied Rhodia, Paris, France
Copolymer of acrylic acid/maleic acid with a molecular weight of 70,000 and a ratio of acrylate/maleate 70:30 was supplied by BASF, Ludwigshafen, Germany
Protease FN3 was delivered Genencor International, Palo Alto, California, USA
Na-salt Ethylenediamine-N,N'-dinternal acid, (S,S)isomer (EDDS) - set is alas Octel, Ellesmere Port, UK
Hydroxyethylphosphonate (HEDP) was supplied by Dow Chemical, Midland, Michigan, USA
The agglomerate of antifoam was delivered Dow Corning, Midland, Michigan, USA
HSAS is a branched alkylsulfate with an average chain length, as disclosed in US 6020303 and US 6060443
C12-14-dimethylamine was delivered Procter & Gamble Chemicals, Cincinnati, Ohio, USA
Non-ionic, preferably represents C12-C13-ethoxylate, preferably with an average degree of amoxilonline 9
The protease was delivered Genencor International, Palo Alto, California, USA
Liquitint® Violet CT was delivered Milliken, Spartanburg, South Carolina, USA
* The values are expressed in mg enzyme/100 g
1as described in US 4597898
2available under the trademark LUTENSIT® BASF and such as described in WO 01/05874
Lipase described in the description of the present invention

Although there have been illustrated and described specific ways embodiment of the present invention, specialists in the art it will be obvious that various other changes and modifications can be made without violating the essence and scope of the invention. Therefore, it is assumed that the appended claims cover all such changes and modifications are included in the scope of the present invention.

1. The detergent composition containing a colouring agent for fabric, a variant of a parent lipase, which is a lipase with the amino acid sequence SEQ ID NO: 2, and auxiliary materials, and the option compared with the specified parent contains one of the following groups of substitutions:
I202G+T231R+N233R;
I86V+L227G+T231R+N233R+P256K;
Q4V+S58N+V60S+T231R+N233R;
S58N+V60S+I90R+T231R+N233R;
I255Y+T231R+N233R;
I90A+T231R+N233R+I255V;
L97V+T231R+N233R;
A150G+T231R+N233R;
I90R+T231R+N233R;
I202V+T231R+N233R;
L227G+T231R+N233R+P256K;
I90A+T231R+N233R;
T231R+N233R+I255P;
I90V+I255V+T231R+N233R;
F211L+L227G+T231R+N233R+I255L+P256K;
S58N+V60S+T231R+N233R+Q249L;
S58N+V60S+T231R+N233R+Q249I;
A150G+L227G+T231R+N233R+P256K;
K46L+S58N+V60S+T231R+N233R+Q249L+D254I;
Q4L+E43T+K461+S58N+V60S+T231R+N233R+Q249L+D254I;
Q4L+S58N+V60S+T231R+N233R+Q249L+D254I;
K461+S58N+V60S+T231R+N233R+Q249L+D254L;
K46L+S58N+V60S+K223I+T231R+N233R+D254I;
E43T+K461+S58N+V60S+T231R+N233R+Q249L+D254I;
S58N+V60S+I6V+A150G+L227G+T231R+N233R+P256K;
K24R+K46R+K74R+I86V+K98R+K127R+D137K+A150G+K223R+T231R+N233R;
S58A+V60A+I86V+T231R+N233R;
K24R+K46R+S58N+V60S+K74R+I86V+K98R+K127R+D137K+K223R+T231R+N233R;
S58A+V60A+I86V+A150G+T231R+N233R;
S58N+V60V+D62G+T231R+N233R;
Q4V+S58N+V60S+I86V+T231R+N233R+Q249L;
Q4V+S58N+V60S+I86V+A150G+T231R+N233R+I255V;
Q4V+S58N+V60S+I90A+A150G+T231R+N233R+I255V;
Y53A+S58N+V60S+T231R+N233R+P256L;
I202L+T231R+N233R+I255A;
S58A+V60S+I86V+A150G+L227G+T231R+N233R+P256K;
D27R+S58N+V60S+I86V+A150G+L227G+T231R+N233R+P256K;
V60K+I86V+Al50G+L227G+T231R+N233R+P256K;
Q4V+S58A+V60S+S83T+I86V+A150G+E210K+L227G+T231R+N233R+P256K;
Q4V+V60K+S83T+I86V+Al50G+L227G+T231R+N233R+P256K;
D27R+V60K+I86V+A150G+L227G+T231R+N233R+P256K;
Q4N+L6S+S58N+V60S+I86V+A150G+L227G+T231R+N233R+P256K;
E1N+V60K+I86V+A150G+L227G+T231R+N233R+P256K;
V60K+I86V+A150G+K223N+G225S+T231R+N233R+P256K;
E210V+T231R+N233R+Q249R;
S58N+V60S+E210V+T231R+N233R+Q249R;
Q4V+V60K+I90R+T231R+N233R+I255V;
Q4V+V60K+A150G+T231R+N233R;
V60K+S83T+T231R+N233R;
V60K+A150G+T231R+N233R+I255V;
T231R+N233G+D234G;
S58N+V60S+I86V+A150G+E210K+L227G+T231R+N233R+Q249R+P256K;
S58N+V60S+I86V+A150G+E210K+L227G+T231R+N233R+I255A+P256K;
S58N+V60S+I86V+A150G+G156R+E210K+L227G+T231R+N233R+I255A+RC;
S58T+V60K+I86V+N94K+A150G+E210V+L227G+T231R+N233R+P256K;
S58T+V60K+I86V+D102A+A150G+L227G+T231R+N233R+P256K;
S58T+V60K+I86V+D102A+A150G+E210V+L227G+T231R+N233R+P256K;
S58T+V60K+S83T+I86V+N94K+A150G+E210V+L227G+T231R+N233R+P256K;
S58A+V60S+I86V+T143S+A150G+L227G+T231R+N233R+P256K;
G91S+D96V+D254R;
V60L+G91M+T231W+Q249L;
T37A+D96A+T231R+N233R+Q249G;
E56G+E87D+T231R+N233R+D254A;
E210K+T231R+N233R;
D27H+E87Q+D96N+T231R+N233R+D254V;
F181L+E210V+T231R+N233R;
D27N+D96G+T231R+N233R;
D96N+T231R+N233R;
T231R+N233I+D234G;
S58K+V60L+E210V+Q249R;
S58H+V60L+E210V+Q249R;
Q4V+F55V+I86V+T231R+N233R+I255V;
Q4V+S58T+V60K+T199L+N200A+E210K+T231R+N233R+I255A+P256K;
Q4V+D27N+V60K+T231R+N233R;
I90F+I202P+T231R+N233R+I255L;
S58N+V60S+D158N+T231R+N233R;
S58N+V60S+S115K+T231R+N233R;
S58N+V60S+L147M+A150G+F211L+T231R+N233R;
V60K+A150G+T231R+N233R;
I90V+L227G+T231R+N233R+P256K;
T231R+N233R+I255S;
I86G+T231R+N23R;
V60K+I202V+E210K+T231R+N233R+I255A+P256K;
I90G+I202L+T231R+N233R+I255S;
S58G+V60G+T231R+N233R.

2. The detergent composition according to claim 1, characterized in that the variant lipase characterized by the fact that the ratio of Benefit-Risk, measured as indicated in the description, has a value greater than 1.

3. The composition according to claim 1, characterized in that it comprises from 0.1% to 40% anionic surfactant.

4. The composition according to claim 3, characterized in that it is a composition for cleaning and/or surface treatment or tissue.

5. The method of cleaning and/or treatment of a surface or fabric comprising a stage on which is introduced into the contact specified surface or fabric with a composition according to claim 1, and then, optionally, washing and/or rinsing the specified surface or fabric.



 

Same patents:

FIELD: chemistry.

SUBSTANCE: present invention relates to a laundry detergent composition containing: (a) glycosyl hydrolase having enzyme activity with respect to both xyloglucan and amorphous cellulose substrates, where the glycosyl hydrolase is selected from GH 5, 12, 44 or 74 families; and (b) a fabric dyeing agent selected from a group consisting of dyes, dye-clay conjugates and mixtures thereof; and (c) a synthetic detergent.

EFFECT: bio-polishing of fabric surface so as to improve deposition and operational characteristics of dyeing agents.

10 cl, 28 ex

FIELD: chemistry.

SUBSTANCE: present invention relates to a laundry detergent composition containing glycosyl hydrolase, having enzyme activity with respect to both xyloglucan and amorphous cellulose substrates, where the glycosyl hydrolase is selected from GH 5, 12, 44 or 74 families; (ii) 0.05-10 wt % amphiphilic alkoxylated fat-removing polymer; and (iii) 2-50 wt % synthetic detergent. The present invention also relates to a laundry detergent composition containing: (i) glycosyl hydrolase, having enzyme activity with respect to both xyloglucan and amorphous cellulose substrates, where the glycolsyl hydrolase is selected from GH 5, 12, 44 or 74 families; (ii) a random graft polymer containing: (a) a hydrophilic backbone chain containing monomers selected from a group consisting of: alcohols, alkoxyl links and maleic anhydride; and (b) hydrophobic side chain(s) selected from a group consisting of: vinyl ester of saturated C1-C6 monocarboxylic acid, C1-C6 alkyl ester of acrylic or methacrylic acid; and (iii) 2-50 wt % synthetic detergent. The present invention also relates to a method of washing fabrics.

EFFECT: improved dirt-removing profile and whiteness retention profile with low content of surfactants.

20 cl, 28 ex

FIELD: chemistry.

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4 cl, 10 dwg, 3 ex

FIELD: chemistry.

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EFFECT: invention provides cellulase, having low activity with respect to restaining, and can be used to treat cellulose material; disclosed fused proteins and enzyme preparations based thereon can be used to prepare detergent compositions or for improving quality of animal feed.

26 cl, 8 dwg, 10 tbl, 10 ex

FIELD: chemistry.

SUBSTANCE: present invention relates to a detergent composition which contains glycosyl hydrolase selected from GH 5, 12, 44 or 74 families, and carrier particles which contains an agent having a positive effect. The invention also relates to a method of processing and/or cleaning affected places with the detergent composition.

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15 cl, 28 ex

FIELD: chemistry.

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15 cl, 8 tbl, 9 ex, 3 dwg

FIELD: chemistry.

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7 cl, 5 ex, 5 dwg

FIELD: chemistry.

SUBSTANCE: composition contains more than 5% anionic surfactant, less than 25% nonionic surfactant, a light-sensitive ingredient and an inorganic mother-of-pearl agent. The light-sensitive ingredient is selected from a group comprising enzymes, dyes, vitamins, aromatising agents and mixtures thereof.

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20 cl, 14 ex

FIELD: chemistry.

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18 cl, 16 ex

FIELD: chemistry.

SUBSTANCE: cleaning compositions contain organic catalysts having improved enzyme compatibility and having the following formulae: where each R1 independently denotes a branched alkyl group selected from a group comprising 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, isodecyl, isotridecyl and isopentadecyl, or a linear alkyl group containing 11-18 carbon atoms. The composition also contains one or more auxiliary ingredients.

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15 cl, 16 ex

FIELD: gene and protein engineering, in particular substances for detergents and cleaning compositions.

SUBSTANCE: invention relates to mutant forms of subtilisin Bacillus, obtained by certain combination of replacement in origin native enzyme amino acid sequence. Such mutant forms are differ from precursor subtilisin by increased cleaning effect. According to present invention all subtilisin variants are characterized either by residue substitution in position accepted to 232 position of Bacillus amyloliquifaciens amino acid sequence with valine, or by residue substitution in position accepted to 212 position of said subtilisin natural form with proline. To produce disclosed new form of enzyme respective mutant DNA sequences have been expressed in host cells, preferably in strain Bacillus cells with decreased level of proteases activity. Subtilisin variants of present invention are useful as components of any cleaning composition allowing for protease including.

EFFECT: new materials for detergents and cleaning compositions of improved effect.

6 cl, 5 dwg, 6 tbl, 3 ex

FIELD: enzymology, protein engineering, in particular enzyme with proteolysis activity.

SUBSTANCE: invention relates to new subtilisin variants obtained by substitution in amino acid sequence of wild-type enzyme following by certain charge alteration in corresponding site, namely negative charge increasing (positive charge decreasing) or vice versa. Subtilisin variants with the first-type substitutions have higher cleaning activities mainly in systems with law detergent concentrations. Subtilisin variants with the second-type substitutions have higher cleaning activities mainly in systems with high detergent concentrations. Variants being effective both in systems with low and high detergent concentration also are disclosed. New subtilisin variants are obtained by expression of DNA mutant sequence in cells of strain Bacillus. Subtilisin muteins of present invention are useful in cleaning compositions and composition for cloth treatment, as well as in animal feed additives.

EFFECT: enzyme of improved effectiveness.

18 cl, 4 dwg, 14 tbl, 2 ex

FIELD: chemistry.

SUBSTANCE: invention pertains to compositions of granulated synthetic detergents, meant for manual and machine washing (in any type of machine) and soaking all types of textiles, including coloured and other household needs. The detergent contains the following components in the given % mass: anionic surface active agent sodium alkylbenzenesulfonate 9-12; non-ionic surfactant 2-5; sodium tripolyphosphate 15-30; dispergator 0.3-1.2; carboxymethyl cellulose 0.3-0.7; sodium silicate 3-6; modified polyalkylene glycol 0.2-0.6; enzyme 0.3-0.8; sodium carbonate 6-12; photo-bleaching agent 0.003-0.020; optical brightener 0.05-0.20; fragrance component 0.1-0.3; sodium sulphate and water up to 100. The non-ionic surfactant preferably contains oxyethylated monoalkylphenols based on propylene trimers or oxyethylated fatty alcohols. The dispergator used is sodium polyacrylate or sodium salt of a copolymer of maleic or acrylic acid or a sodium salt of a copolymer of acrylic, methacrylic and maleic acid. Alternatives of the synthetic detergent are also described.

EFFECT: increased effectiveness of the detergent, bleaching effect after washing, wider assortment of high quality granulated synthetic detergents.

7 cl, 1 tbl

FIELD: chemistry.

SUBSTANCE: invention is meant for soaking, washing and bleaching all types of textile articles, except articles from natural silk and wool, in any kind of machine, and also hand wash. Substance contains in % mass: an anionic surfactant 7-15, nonionic surfactant oxyethylated fatty alcohol 2-5, sodium tripolyphosphate 15-25, sodium ethylene-diaminotetraacetate (versene) 0.3-1, polycarboxylate, containing monomers of acrylic acid 0.2-0.6, carboxymethyl cellulose (CMC) (in terms of 100% of the share of the main substance) 0.4-0.6, sodium silicate (in terms of SiO2) - 2-5, sodium perborate or sodium percarbonate (in terms of activated oxygen) 1.5-4, tetraacetylethylenediamine (TAED) 0.5-3, enzymes 0.4-1, caustic ash 5-15, mixture of sodium carbonate and amorphous sodium silicate 2-5, optical brightener 0.05-0.4, perfume 0.1-0.3, sodium sulphate and water till 100.

EFFECT: increase in the effectiveness of the detergent with a whitening effect, removal of all kinds of dirt while adding extra softness without an irritating effect on the skin during hand washing, reducing the temperature regimes of washing, reduction in the harmful effect to the metallic part of the washing machine.

9 cl, 2 tbl

FIELD: chemistry.

SUBSTANCE: detergent contains the components as follows, wt %: anionic surface active agent (SAG) - alkylbenzol sodium sulphonate 10-16; nonionic SAG - oxyethylated fatty alcohols or oxyethylated alkylphenol 2-5; sodium tripolyphosphate 15-25; organophosphonate compound - sodium salt 1-hydroxyethylidene of phosphonic acid or sodium diethylentriaminopentaxys-(methylene phosphonate) 0.2-0.6; polycarboxylate 0.5-1.5; carboxymethyl cellulose 0.3-0.6; modified polyalkylene glycol 0.2-0.6; optical bleaching agent 0.05-0.3; soda ash 3-6; liquid glass 3.5-6.0; enzyme 0.4-0.7; defoaming agent 0.05-1.5; aromatiser 0.15-0.3; sodium sulphate and water to 100.

EFFECT: higher efficiency of bleaching detergent, all type decontamination with additional softening of fabric and without irritation of hand skin during manual washing, lower temperature modes of washing, reduced damage effect on metal parts of washing machines.

10 cl, 2 tbl, 5 ex

FIELD: chemistry.

SUBSTANCE: present invention relates to compositions which contain certain versions of lipase and a toned agent for fabric, and includes use of such compositions for cleaning and/or treating surface areas or fabric.

EFFECT: improved deposition of temporary colourant, reduced activity of the enzyme which leads to bad smell, and improved perception of cleanness.

17 cl, 3 tbl, 16 ex

FIELD: chemistry.

SUBSTANCE: compositions contain certain versions of lipase and a photo-bleaching agent based on xanthene dye, a photoinitiator and their mixtures.

EFFECT: more efficient cleaning, leading to minimal undesirable bad smells.

11 cl, 3 tbl, 16 ex

FIELD: chemistry.

SUBSTANCE: detergent composition contains a polymer combined with a surfactant or an inorganic detergent component and auxiliary ingredients. The fat purification efficiency index of the detergent composition is at least equal to 10. The polymer is a random grafted copolymer which has a hydrophilic skeleton and hydrophobic side chains, obtained by grafting (a) polyethylene oxide; (b) vinyl ester of acetic and/or propionic acid; and/or C1-4alkyl ester of acrylic or methacrylic acid; and (c) modifying monomers. The detergent compositions preferably additionally contain lipase enzyme.

EFFECT: improved removal of fat contaminants and stains with reduced amounts of conventional surfactants or inorganic detergent components.

22 cl, 6 ex

FIELD: chemistry.

SUBSTANCE: present invention relates to a composition which contains lipase, and a bleaching catalyst which can accept an oxygen atom from a peroxy acid and transfer the oxygen atom to an oxidisable substrate.

EFFECT: less bad smell which arises when using lipase enzymes in detergents.

13 cl, 4 tbl, 3 ex

FIELD: chemistry.

SUBSTANCE: cleaning compositions contain organic catalysts having improved enzyme compatibility and having the following formulae: where each R1 independently denotes a branched alkyl group selected from a group comprising 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, isodecyl, isotridecyl and isopentadecyl, or a linear alkyl group containing 11-18 carbon atoms. The composition also contains one or more auxiliary ingredients.

EFFECT: cleaning compositions with efficient bleaching at low water temperature.

15 cl, 16 ex

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