Abstract: New PB92 or Subtilisin 309 mutant serine proteases are provided having specific mutations, resulting in an surprisingly better wash performance or in an improved storage stability with at similar or even better wash performance. These PB92 or Subtilisin 309 mutants include mutations at positions 60, 87, 97, 99, 102, 116, 117, 126, 127, 128, 130, 133, 134, 154, 156, 158, 159, 160, 164, 169, 175, 180, 182, 193, 197, 198, 203, 211, and 216. The new proteases, therefore, are very suitable for use in various types of detergents, whether or not in conjunction with other enzymes, for example amylases, cellulases and lipases. Preferred embodiments are the PB92 and Subtilisin 309 mutants having a mutation at position 102 and in particular those having at least one further mutation.

Abstract: New proteolytic enzymes are provided exhibiting improved properties for application in detergents, especially laundry detergents. These enzymes are obtained by expression of a gene encoding a proteolytic enzyme having an amino acid sequence which differs at least in one amino acid from the wild type enzyme. Preferred enzymes are certain mutants derived from the serine protease of Bacillus nov. spec. PB92.

Abstract: New mutant .beta.-lactam acylases are provided exhibiting altered substrate specificities. These .beta.-lactam acylases are obtained by expression of a gene encoding said .beta.-lactam acylase and having an amino acid sequence which differs at least in one amino acid from the wild-type .beta.-lactam acylase.

Abstract: New mutant .beta.-lactam acylases are provided exhibiting altered substrate specificities. These .beta.-lactam acylases are obtained by expression of a gene encoding said .beta.-lactam acylase and having an amino acid sequence which differs at least in one amino acid from the wild-type .beta.-lactam acylase.

Abstract: A method for selecting amino acid residues is disclosed which upon replacement will give rise to an enzyme with an altered pH optimum. The method is specific for metalloenzymes which are inactivated at low pH due to the dissociation of the metal ions. The method is based on altering the pK.sub.a of the metal coordinating ligands or altering the K.sub.ass for the metal binding. New glucose isomerases with an altered pH optimum are provided according to this method. These altered properties enable starch degradation to be performed at lower pH values.

Abstract: A method for selecting amino acid residues is disclosed which upon replacement will give rise to an enzyme with an altered pH optimum. The method is specific for metalloenzymes which are inactivated at low pH due to the dissociation of the metal ions. The method is based on altering the pK.sub.a of the metal coordinating ligands or altering the K.sub.ass for the metal binding. New glucose isomerases with an altered pH optimum are provided according to this method. These altered properties enable starch degradation to be performed at lower pH values.

Abstract: New proteolytic enzymes are provided exhibiting improved properties for application in detergents, especially laundry detergents. These enzymes are obtained by expression of a gene encoding a proteolytic enzyme having an amino acid sequence which differs at least in one amino acid from the wild type enzyme. Preferred enzymes are certain mutants derived from the serine protease of Bacillus nov. spec. PB92.

Abstract: New proteolytic enzymes are provided exhibiting improved properties for application in detergents, especially laundry detergents. These enzymes are obtained by expression of a gene encoding a proteolytic enzyme having an amino acid sequence which differs at least in one amino acid from the wild type enzyme. Preferred enzymes are certain mutants derived from the serine protease of Bacillus nov. spec. PB92.