Abstract:
The present invention provides variant subtilisins and compositions comprising at least one variant subtilisin set forth herein, as well as methods for using these variants and compositions. In some embodiments, the present invention provides variant subtilisins suitable for laundry cleaning applications.
Abstract:
This invention relates to fabric and home care products comprising one or more cold water proteases and processes for making and using such products. Such compositions provide improved cleaning and freshness. Such cold water proteases may be derived from parent enzymes, including BPN′ subtilisin and subtilisin derived from Bacillus lentus, by substitution, insertion and/or deletion of one or more of the parent enzymes' amino acids.
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:
The present invention provides engineered protease variants. In particular, the protease variants comprise combinable mutations at selected surface positions that affect the charge and/or hydrophobicity of the enzyme to enhance at least one desired property of the resulting variant enzyme in a chosen application. Compositions comprising the protease variants, and methods for using the same are also provided.
Abstract:
The present invention provides methods and compositions comprising at least one isoprene synthase enzyme with improved catalytic activity and/or solubility. In particular, the present invention provides variant plant isoprene synthases for increased isoprene production in microbial host cells. Biosynthetically produced isoprene of the present invention finds use in the manufacture of rubber and elastomers.
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:
The present invention provides efficient methods for obtaining a protein with one or more beneficial attributes in industrial, consumer or pharmaceutical applications. In some preferred embodiments, the present invention provides methods for producing superior enzymes for a given application through screening an abbreviated set of candidate enzymes.
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.