| Title | Multicatalytic Alkaline Serine Protease from the Psychrotrophic Bacillus amyloliquefaciens S94 |
|---|---|
| Author | Eui-Sun Son and Jong-Il Kim * |
| Address | Department of Food and Microbial Technology, Seoul Women's University 126 kongnung 2-dong, Nowon-Gu, Seoul 139-774, Korea (Received Jan 17, 2003/Accepted Feb 6, 2003) |
| Bibliography | Journal of Microbiology, 41(1),58-62, 2003, |
| DOI | |
| Key Words | Bacillus amyloliquefaciens, multifunctional endopeptidase, serine protease, cold active enzyme. |
| Abstract | An extracellular protease of Bacillus amyloliquefaciens S94 was purified to apparent homogeneity. The enzyme activity was strongly inhibited by general inhibitor for serine protease, PMSF, suggesting that the enzyme is a serine protease. The purified enzyme activity was inhibited by leucine peptidase inhibitor, bestatin, suggesting that the enzyme is a leucine endopeptidase. The maximum proteolytic activity against different protein substrates occurred at pH 10, 45℃ (protein substrate) and pH 8, 45℃ (synthetic substrate). The purified enzyme was specific in that it readily hydrolyzed substrates with Leu or Lys residues at P1 site. The protease had characteristics of a cold-adapted protein, which was more active for the hydrolysis of synthetic substrate in the range of 15℃ to 45℃, specially at low temperature. |
| Download PDF | 411-1007.pdf |