Abstract: The present invention provides a subtilisin variant that is particularly well suited to cleaning applications. In particular, the present invention provides a Bacillus sp. subtilisin variant and cleaning compositions comprising this variant.

Abstract: Described are variants (mutants) of a parent alpha-amylase having alpha-amylase activity and exhibiting altered properties relative to the parent alpha-amylase, and methods of use, thereof.

Abstract: Disclosed are compositions comprising variants of alpha-amylase that have alpha-amylase activity and which exhibit altered properties relative to a parent AmyS-like alpha-amylase from which they are derived. The compositions comprise an additional enzyme such as a phytase. Also disclosed are methods of using the compositions, and kits related thereto.

Abstract: Novel enzyme variants including protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease, Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue correspond to positions 27, 45, 170, 181, 251 and 271 of Bacillus amyloliquefaciens subtilisin. Additional variants comprising at least one additional substitution at a position selected from 1, 14, 49, 61, 87, 100, 102, 118, 128, 204 and 258 of Bacillus amyloliquefaciens subtilisin are also described.

Abstract: Novel enzyme variants including protease variants derived from the DNA sequences of naturally-occurring or re-combinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue correspond to positions 27, 45, 170, 181, 251 and 271 of Bacillus amyloliquefaciens subtilisin. Additional variants comprising at least one additional substitution at a position selected from 1, 14, 49, 61, 87, 100, 102, 118, 128, 204 and 258 of Bacillus amyloliquefaciens subtilisin are also described.

Abstract: Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Protease variants are provided that contain substitutions of the amino acids at one or more residue positions so that the substitution alters the charge at that position to make the charge more negative or less positive compared to a precursor protease and thus the protease variant is more effective in a low detergent concentration system than a precursor protease.

Abstract: A microtiter method for assaying the wash performance of new enzymes and/or new detergent formulations is described.

Abstract: A polyesterase enzyme which produces a positive result in an UV and/or MB assay is used to treat polyester to modify polyester properties such as pilling, pilling prevention, weight, feel, appearance and luster.

Abstract: Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue correspond to positions 62, 212, 230, 232, 252 and 257 of Bacillus amyloliquefaciens subtilisin.

Abstract: The present invention relates to cleaning compositions comprising a protease variant.

Abstract: The present invention relates to bleaching compositions comprising a protease variant.

Abstract: Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance.

Abstract: Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Protease variants are provided that contain substitutions of the amino acids at one or more residue positions so that the substitution alters the charge at that position to make the charge more negative or less positive compared to a precursor protease and thus the protease variant is more effective in a low detergent concentration system than a precursor protease.

Abstract: The present invention relates to cleaning compositions comprising a protease variant.

Abstract: Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue correspond to positions 62, 212, 230, 232, 252 and 257 of Bacillus amyloliquefaciens subtilisin.

Abstract: The present invention relates to cleaning compositions comprising a protease variant.

Abstract: Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance.

Abstract: A method is provided for improving the uptake of a cationic compound onto a polyester article starting material, comprising the steps of: (a) obtaining a polyesterase enzyme; (b) contacting said polyesterase enzyme with said polyester article starting material under conditions and for a time suitable for said polyesterase to produce surface modification of said polyester article starting material and produce a surface modified polyester; (c) contacting said modified polyester article, subsequently or simultaneously with said step (b) with a cationic compound whereby adherence of said cationic compound to said modified polyester is increased compared to said polyester starting material. Also disclosed is a method for increasing the hydrophilicity of a polyester to improve fabric characteristics such as stain resistance, wettability and/or dyeability.