TITLE

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

AUTHOR(S)
Kim, Sam Sun; Kim, Young Jae; Rhee, In-Koo
PUB. DATE
June 2001
SOURCE
Archives of Microbiology;Jun2001, Vol. 175 Issue 6, p458
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
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.
ACCESSION #
15731389

 

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