Cognis Corporation

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Henkel Kommanditgesellschaft Auf Aktien

Henkel Research Corporation

Henkel Konnarditgesellshaft Auf Aktien

Robert B Reynolds

Christian G Paech

Charles R Wilson

Teresa M Christianson

Dean W Goddette

Shiow-Shong Yang

Beth Frances Ladin

Maria R Lau

Joachim Schindler

Rolf Schmid

Michael Bahn

Dieter Hansen

Nicholas C Kennedy

Sherman S Hom

Jonathan R Mielenz

Beth F Ladin

Martina Markgraf

Karlheinz Maurer

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

A proteolytic enzyme for use in detergent formulations having increased pH and oxidative stability under typical laundering conditions in aqueous solutions is produced by fermenting Bacillus licheniformis host strain transformed by a multicopy plasmid comprised of DNA sequences which code for the desired proteolytic enzyme.

Alkaline proteolytic enzyme and method of production

Bacillus lentus alkaline protease variants with increased stability

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Santa Rosa, CA, United States of America

Robert B Reynolds