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Henkel Kommanditgesellschaft Auf Aktien

Henkel Konnarditgesellshaft Auf Aktien

Beth Frances Ladin

Christian G Paech

Charles R Wilson

Teresa M Christianson

Dean W Goddette

Robert B Reynolds

Shiow-Shong Yang

Maria R Lau

Mutant DSM 5483 proteases are derived by the replacement of at least one amino acid residue of the mature form of the DSM 5483 alkaline protease. The mutant proteases are expressed by genes which are mutated by site-specific mutagenesis. The amino acid sites selected for replacement are identified by means of a computer based method which compares the three dimensional structure of the wild-type protease and a reference protease.

Mutant proteolytic enzymes and method of production

Mutant B. lentus DSM 5483 proteases are derived by the replacement of at least one amino acid residue of the mature form of the B. lentus DSM 5483 alkaline protease. The mutant proteases are expressed by genes which are mutated by site-specific mutagenesis. The amino acid sites selected for replacement are identified by means of a computer based method which compares the three dimensional structure of the wild-type protease and a reference protease.

Bacillus lentus alkaline protease varints with enhanced stability

Bacillus lentus alkaline protease variants with increased stability

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Beth Frances Ladin