Cleaning compositions for solid surfaces – auxiliary compositions – Cleaning compositions or processes of preparing – Enzyme component of specific activity or source
Reexamination Certificate
1999-06-07
2001-09-18
Fries, Kery (Department: 1751)
Cleaning compositions for solid surfaces, auxiliary compositions
Cleaning compositions or processes of preparing
Enzyme component of specific activity or source
C510S292000, C510S300000, C510S320000, C510S360000, C510S499000, C510S475000, C510S466000, C510S530000
Reexamination Certificate
active
06291414
ABSTRACT:
FIELD OF THE INVENTION
The present invention relates to substantially bleach free detergent compositions comprising variants of the high alkaline protease having high homology with the amino acid sequence of
Bacillus lentus
protease. Said variants having at least one mutation in each of the regions 96-110 and 123-135 (BPN′-numbering), i.e. at least one mutation in both sites of the so-called “S1-S4 substrate binding pockets” (Int. symposium on subtilisin enzymes, Hamburg, Germany Sep. 24-25, 1992; R. J. Siezen).
More in particular, the present invention relates to detergent compositions comprising said mutated protease and in addition a polymeric dye transfer inhibiting agent to be used for treatment of fabrics, more specifically washing of colored fabrics and demonstrating high care on wool and/or silk fabrics.
BACKGROUND OF THE INVENTION
Enzymes make up a very important class of naturally occuring proteins. Each class of enzyme catalyzes a different kind of chemical reaction. One class of enzymes, known as proteases, are known for their ability to hydrolyze (break down a compound into two or more smaller compounds with the uptake of the H and OH parts of a water molecule on either side of the chemical bond cleaved) other proteins. This ability to hydrolyze proteins has been taken advantage of by incorporating naturally occurring and protein engineered proteases as an additive to laundry detergent preparations. Many stains and soils on clothes are proteinaceous and water-insoluble. Wide-specificity proteases can substantially improve removal of such stains by hydrolyzing the water-insoluble proteins into smaller water-soluble fragments.
Unfortunately, the efficacy level of these proteins in their natural environment, frequently does not translate when applied into the relatively unnatural wash environment. Specifically, protease characteristics such as thermal stability, pH stability, oxidative stability and substrate specificity are not necessarily optimized for utilization outside the natural environment of the enzyme. Moreover cleaning/stain removal performance and fabric care, more specifically wool/silk compatibility are not necessarily optimized.
Considering a specific type of protease (e.g.
subtilisins
of
B.amyloliquefaciens, B.lentus, B.licheniformis
etc.), the amino acid sequence of the protease enzyme determines the characteristics of the protease. Changing the amino acid sequence of the protease may alter the properties of the enzyme to varying degrees, or may even inactivate the enzyme, depending upon the location, nature and/or magnitude of the change in the amino acid sequence. Several approaches have been taken to alter the amino acid sequence of proteases in an attempt to improve their properties, with the goal of increasing the efficacy of the protease for cleaning uses such as in the wash environment. These approaches include altering the amino acid sequence to enhance thermal stability, proteolytic activity, oxidation stability, etc. under quite diverse conditions.
Despite the variety of approaches described in the art, there is a continuing need for new effective variants of proteases useful for cleaning a variety of fabrics without damaging the textile properties. It is therefore an object of the present invention to provide detergent compositions substantially free of bleach containing high alkaline protease enzymes combining excellent cleaning/stain removal performance to good wool and/or silk compatibility.
DETAILED DESCRIPTION OF THE INVENTION
High alkaline proteases suitable for detergent compositions have high homology (at least 70%) with the amino acid sequence shown in FIG. 1. This sequence is identical to
Bacillus lentus subtilisin
(BPN′ numbering). Some commercially available high alkaline proteases such as Savinase, Durazym, Maxacal, Maxapem, Opticlean etc. have either the same amino acid sequence or hardly differ from it (up to 2 amino acids). However, when used in substantially bleach free detergent compositions they all lack the necessary wool/silk compatibility in that they show high damage on such fabrics.
It has now surprisingly been found that specific variants of such high alkaline proteases having the amino acid sequence according to FIG. 1 (BPN′ numbering) with at least one mutation in each of the regions 96-110 and 123-135 demonstrate a good wool fabric compatibility and maintain an excellent washing performance. Accordingly, the present invention provides detergent compositions substantially free of bleach comprising a high alkaline protease with the amino acid sequence according to FIG. 1 (BPN′ numbering) having at least one mutation in each of the regions 96-110 and 123-135. The proteases are obtainable by methods known and described in the literature, e.g. by cultivation of a protease producing strain (for instance Bacillus lentus) in a suitable nutrient medium, containing carbon and nitrogen sources and inorganic salts, followed by the recovery of the enzyme desired, or may e.g. be produced by employing recombinant DNA technology.
A preferred protease according to the invention to be used in the substantially bleach free detergent composition and showing an excellent compatibility for wool and/or silk fabrics is the protease with a mutation at position V104, preferably from Valine into Isoleucine (V104I) or into tyrosine (V104Y) and a mutation at position N123, preferably from Asparagine into Serine (N123S).
In addition, mutations in and/or outside the regions mentioned, e.g. at positions 76, 99, 101, 103, 222 and mixtures thereof result in improved stability and/or activity of the proteases according to the invention without hampering the fabric compatibility. Non-limiting examples of mutations are N76D, S99D, S101R, S103A, M222S, M222A and M222C.
In addition the detergent compositons having above protease contain a polymeric dye transfer inhibiting agent selected from polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidones, polyvinyloxazolidones, polyvinylimidazoles or mixtures thereof. The density of the compositions herein ranges from 550 to 950 g/liter, preferably 600 to 900 g/liter of composition measured at 20° C.
The “compact” form of the compositions herein is best reflected, in terms of composition, by the amount of inorganic filler salt; inorganic filler salts are conventional ingredients of detergent compositions in powder form; in conventional detergent compositions, the filler salts are present in substantial amounts, typically 17-35% by weight of the total composition.
In the compact compositions, the filler salt is present in amounts not exceeding 15% of the total composition, preferably not exceeding 10%, most preferably not exceeding 5% by weight of the composition.
Inorganic filler salts, such as meant in the present compositions are selected from the alkali and alkaline-earth-metal salts of sulphates and chlorides.
A preferred filler salt is sodium sulphate.
Protease
Suitable high alkaline proteases are variants of proteases known in the literature as
B.lentus subtilisin,
subtilisin 309,
B.alkalophilus subtilisin,
PB 92 subtilisin or have an amino acid sequence with at least 70% homology. Other suitable proteases are variants of proteases which show a positive immunological cross-reaction with the antibody of the proteases as described hereinabove.
The proteases according to the present invention are present in an amount from 0.001% to 2%, preferably from 0.001% to 1%, more preferably from 0.002% to 0.5% of active enzyme by weight of the detergent composition.
In the context of this invention a subtilisin is defined as a serine protease produced by gram-positive bacteria or fungi. According to another definition, a subtilisin is a serine protease, wherein the relative order of the amino acid residues in the catalytic triad is Asp-His-Ser (positions 32, 64 and 221, BPN′ numbering).
Amino Acids
As abbreviations for amino acids the following symbols are used:
A=Ala=Alanine
C=Cys=Cysteine
D&equa
Baeck Andre Cesar
Busch Alfred
Verschuere Ann Katrien Marie
Cook C. Brant
Fries Kery
Miller Steven W.
The Procter & Gamble & Company
Zerby Kim W.
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