A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: purification and characterization

Biosci Biotechnol Biochem. 2006 Jun;70(6):1395-401. doi: 10.1271/bbb.50658.

Abstract

A halophilic bacterium was isolated from fish sauce, classified, and named Halobacillus sp. SR5-3. A purified 43-kDa proteinase produced by this bacterium showed optimal activity at 50 degrees C and pH 9-10 in 20% NaCl. The activity of the enzyme was enhanced about 2.5-fold by the addition of 20-35% NaCl, and the enzyme was highly stabilized by NaCl. It was found to be a serine proteinase related to either chymotrypsin or subtilisin. It absolutely preferred Ile at the P(2) position of substrates. Thus, the enzyme was found to be a halophilic serine proteinase with unique substrate specificity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillaceae / classification
  • Bacillaceae / enzymology*
  • Enzyme Inhibitors / pharmacology
  • Enzyme Stability / drug effects
  • Fish Products / microbiology*
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / classification
  • Serine Endopeptidases / isolation & purification*
  • Serine Endopeptidases / metabolism*
  • Sodium Chloride / pharmacology
  • Substrate Specificity
  • Thailand

Substances

  • Enzyme Inhibitors
  • Sodium Chloride
  • Serine Endopeptidases