Purification and characterization of a novel extracellular protease from Bacillus cereus KCTC 3674

Kim, Sam Sun; Kim, Young Jae; Rhee, In-Koo
June 2001
Archives of Microbiology;Jun2001, Vol. 175 Issue 6, p458
Academic Journal
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.


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