Improvement of thermostability of cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella sp. strain Ac10 by rational mutagenesis

Ljudmila Kulakova, Andrey Galkin, Toru Nakayama, Tokuzo Nishino, Nobuyoshi Esaki

Research output: Contribution to journalArticle

10 Citations (Scopus)

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 Vmax/Km,app value than those of the wild-type SapSh.

Original languageEnglish
Pages (from-to)113-117
Number of pages5
JournalJournal of Molecular Catalysis B: Enzymatic
Volume22
Issue number1-2
DOIs
Publication statusPublished - 2003 Apr 1

Keywords

  • Cold-active enzymes
  • Cold-adapted enzymes
  • Homology modeling
  • Protease
  • Psychrophile
  • Thermostability

ASJC Scopus subject areas

  • Catalysis
  • Bioengineering
  • Biochemistry
  • Process Chemistry and Technology

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