Abstract: We disclose a PS4 variant polypeptide derivable from a parent polypeptide, the parent polypeptide having non-maltogenic exoamylase activity, which PS4 variant polypeptide comprises one or more of the following substitutions: G69P, A141P, G223A, A268P, G313P, S399P and G400P, with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. Such PS4 variant polypeptides may be used as exo-amylases, particularly as non-maltogenic exoamylases. Combinations of such PS4 variant polypeptides together with Novamyl are disclosed.

Abstract: We disclose a PS4 variant polypeptide derivable from a parent polypeptide, the parent polypeptide having non-maltogenic exoamylase activity, which PS4 variant polypeptide comprises one or more of the following substitutions: G69P, A141P, G223A, A268P, G313P, S399P and G400P, with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. Such PS4 variant polypeptides may be used as exo-amylases, particularly as non-maltogenic exoamylases. Combinations of such PS4 variant polypeptides together with Novamyl are disclosed.

Abstract: We disclose a PS4 variant polypeptide derivable from a parent polypeptide, the parent polypeptide having non-maltogenic exoamylase activity, which PS4 variant polypeptide comprises one or more of the following substitutions: G69P, A141P, G223A, A268P, G313P, S399P and G400P, with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. Such PS4 variant polypeptides may be used as exo-amylases, particularly as non-maltogenic exoamylases. Combinations of such PS4 variant polypeptides together with Novamyl are disclosed.

Abstract: The present invention involves a method of coupling disulfide bridge containing proteins to a carrier by inducing the formation of thiol groups on a protein with irradiation, and coupling the protein to the carrier. The formation of thiol group(s) in the protein is a consequence of the disruption of disulfide bridges following electronic excitation of aromatic amino acid residues located in close spacial proximity to the disulfide bridge. The light-induced coupling method facilitates the orientated immobilization of a protein on a carrier.

Abstract: The present invention relates to mutations of a subtilisin gene which result in changes in the chemical characteristics of subtilisin enzymes. Mutations at specific nucleic acids of the subtilisin gene result in amino acid substitutions and consequently, altered enzyme function. Some of these mutant enzymes exhibit physical properties advantageous to industrial applications, particularly in the detergent industry, providing subtilisin which is more stable to oxidation, possesses greater protease activity, and exhibits improved washability.