Abstract: Biomolecular conjugates are provided which comprise the conjugation product of a repeat sequence protein polymer and at least one active agent. Additional aspects provide methods for their manufacture and various industrial and consumer applications.

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: 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: Improved methods of treating cellulose containing fabrics with cellulase comprising contacting the cellulose fabrics with truncated cellulase enzyme. Treatment of cellulose containing fabrics with cellulase core domains of the invention are disclosed as offering specific advantages of reduced redeposition of dye and increased abrasion.

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: Textile fibers are treated with enzymes in the absence of surfactants, with the effect of increasing the wettability and absorbency of the fibers. The enzymes are pectinases, cellulases, proteases, lipases or combinations thereof. The wetting properties of cotton fibers are found to be most substantially improved by treatment with a mixture of cellulase and pectinase. The effects of five hydrolyzing enzymes on improving the hydrophilicity of several polyester fabrics have been studied. Four out of the five lipases studied improve the water wetting and absorbent properties of the regular polyester fabrics more than alkaline hydrolysis under optimal conditions (3N NaOH at 55° C. for 2 hours). Compared to aqueous hydrolysis, the enzyme reactions have shown to be effective under more moderate conditions, including a relatively low concentration (0.01 g/L), a shorter reaction time (10 minutes), at an ambient temperature (25° C.).

Abstract: The use is provided of a composition as a feed additive which comprises one or more endoglucanases, and 0-20% by weight, based upon the content of cellulase proteins in the composition, of a cellobiohydrolase. The endoglycanases may be one or more of EGI, EGII EGIII and any functionally active derivative of any thereof. Such endoglucanases may be obtained from a genetically modified strain of the fungus Trichoderma. Also provided is an enzyme-based feed additive which comprises EGI and/or EGII which lack the cellulose binding domain, and 0-20% by weight, based upon the content of cellulase proteins in the additive, of a cellobiohydrolase. A further enzyme-based feed additive is provided which comprises a cereal-based carrier, one or more endoglucanases, and 0-20% by weight, based upon the content of cellulase proteins in the additive, of a cellobiohydrolase. Such enzyme-based feed additives can be incorporated into a cereal-based feed which includes one or more of barley, wheat, tricale, rye and maize.

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: 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: Improved methods of treating cellulose containing fabrics with cellulase comprising contacting the cellulose fabrics with truncated cellulase enzyme. Treatment of cellulose containing fabrics with cellulase core domains of the invention are disclosed as offering specific advantages of reduced redeposition of dye and increased abrasion.

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

Abstract: Textile fibers are treated with enzymes in the absence of surfactants, with the effect of increasing the wettability and absorbency of the fibers. The enzymes are pectinases, cellulases, proteases, lipases or combinations thereof. The wetting properties of cotton fibers are found to be most substantially improved by treatment with a mixture of cellulase and pectinase. The effects of five hydrolyzing enzymes on improving the hydrophilicity of several polyester fabrics have been studied. Four out of the five lipases studied improve the water wetting and absorbent properties of the regular polyester fabrics more than alkaline hydrolysis under optimal conditions (3N NaOH at 55° C. for 2 hours). Compared to aqueous hydrolysis, the enzyme reactions have shown to be effective under more moderate conditions, including a relatively low concentration (0.01 g/L), a shorter reaction time (10 minutes), at an ambient temperature (25° C.).

Abstract: Textile fibers are treated with enzymes in the absence of surfactants, with the effect of increasing the wettability and absorbency of the fibers. The enzymes are pectinases, cellulases, proteases, lipases or combinations thereof. The wetting properties of cotton fibers are found to be most substantially improved by treatment with a mixture of cellulase and pectinase. The effects of five hydrolyzing enzymes on improving the hydrophilicity of several polyester fabrics have been studied. Four out of the five lipases studied improve the water wetting and absorbent properties of the regular polyester fabrics more than alkaline hydrolysis under optimal conditions (3N NaOH at 55° C. for 2 hours). Compared to aqueous hydrolysis, the enzyme reactions have shown to be effective under more moderate conditions, including a relatively low concentration (0.01 g/L), a shorter reaction time (10 minutes), at an ambient temperature (25° C.).

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: Improved methods of treating cellulose containing fabrics with cellulase comprising contacting the cellulose fabrics with truncated cellulase enzyme. Treatment of cellulose containing fabrics with cellulase core domains of the invention are disclosed as offering specific advantages of reduced redeposition of dye and increased abrasion.

Abstract: Textile fibers are treated with enzymes in the absence of surfactants, with the effect of increasing the wettability and absorbency of the fibers. The enzymes are pectinases, cellulases, proteases, lipases or combinations thereof. The wetting properties of cotton fibers are found to be most substantially improved by treatment with a mixture of cellulase and pectinase. The effects of five hydrolyzing enzymes on improving the hydrophilicity of several polyester fabrics have been studied. Four out of the five lipases studied improve the water wetting and absorbent properties of the regular polyester fabrics more than alkaline hydrolysis under optimal conditions (3N NaOH at 55.degree. C. for 2 hours). Compared to aqueous hydrolysis, the enzyme reactions have shown to be effective under more moderate conditions, including a relatively low concentration (0.01 g/L), a shorter reaction time (10 minutes), at an ambient temperature (25.degree. C.).