Abstract
A serine alkaline protease (SapSh) from a psychrophilic bacterium Shewanella sp. strain Ac10 is a cold-active subtilase with low thermostability [Appl. Environ. Microbiol. 65 (1999) 611–617]. By means of homology modeling with other subtilase structures, we have constructed a mutant SapSh containing an extra salt bridge on its surface that exhibits higher thermostability and even higher V max/ K m, app value than those of the wild-type SapSh.
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