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A new detergent protease from a novel alkaliphilic Bacillus sp: enzymatic properties and sequence

 

Katsuhisa Saeki and Susumu Ito

Tochigi Research Laboratories of Kao Corporation, 2606 Akabane, Ichikai, Haga, Tochigi 321-3497, Japan

 

The gene for a subtilisin-like serine protease from a novel sp. of alkaliphilic Bacillus exhibiting resistance to oxidative inactivation were cloned and sequenced. The enzyme was composed of 639 amino acids, including a possible 〜200-amino acid prepro-peptide and a unique C-terminal stretch of 〜160 amino acids. Phylogenetic analysis indicated that this enzyme is far removed from other known subtilisins in the line of molecular evolution. We propose that this novel protease be categorized as a new subfamily in family A subtilisins. This enzyme is promising for use in detergent formulations.

 

 

 

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