We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Purification and characterization of a novel extracellular protease from Bacillus cereus KCTC 3674.
- Authors
Kim, Sam Sun; Kim, Young Jae; Rhee, In-Koo
- Abstract
Bacillus cereus KCTC 3674 excretes several kinds of extracellular proteases into the growth medium. Two proteases with molecular masses of approximately 36-kDa and 38-kDa, as shown by SDS-PAGE, were purified from the culture broth. The 38-kDa protease was purified from B. cereus cultivated at 37 °C, and the 36-kDa protease was obtained from the B. cereus cultivated at 20 °C. The 38-kDa protease was identified as an extracellular neutral (metallo-) protease and was further characterized. The 36-kDa protease was shown to be a novel enzyme based on its N-terminal amino acid sequence, its identification as a metallo-enzyme that was strongly inhibited by EDTA and o-phenanthroline, its hemolysis properties, and its optimal pH and temperature for activity of 8.0 and 70 °C, respectively.
- Subjects
BACILLUS cereus; BACILLUS (Bacteria); BACILLACEAE; GRAM-positive bacteria; PROTEOLYTIC enzymes; HYDROLASES
- Publication
Archives of Microbiology, 2001, Vol 175, Issue 6, p458
- ISSN
0302-8933
- Publication type
Article
- DOI
10.1007/s002030100282