Bleaching and dyeing; fluid treatment and chemical modification – Cleaning or laundering – Removing formation impurities from artifical fiber
Patent
1996-12-06
1999-07-13
Fries, Kery
Bleaching and dyeing; fluid treatment and chemical modification
Cleaning or laundering
Removing formation impurities from artifical fiber
510292, 510300, 510320, 510350, 510360, 510392, 510466, 510474, 510475, 510499, 510530, C11D 3386, C11D 337, C11D 183, D06B 100
Patent
active
059220821
DESCRIPTION:
BRIEF SUMMARY
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 compatibilit
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Baeck Andre Cesar
Busch Alfred
Verschuere Ann Katrien Marie Agnes
Cook C. Brant
Fries Kery
Procter & Gamble Company
Rasser Jacobus C.
Zerby Kim W.
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