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- Purification and Characterization of Caseinolytic Extracellular protease from Bacillus amyloliquefaciens S94
- Eui-Sun Son , Jong-Il Kim
- J. Microbiol. 2002;40(1):26-32.
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Abstract
- From the culture supernatant of the psychrotrophic strain of Bacillus amyloliquefaciens an extracellular serine protease was purified to apparent homogeneity by successive purification steps using QAE-Sephadex, SP-Sephadex and Sephacryl S-100 column chromatography. The protease is monomeric, with a relative molecular mass of 23,000. It is inhibited by the serine protease inhibitor phenylmethylsulfonyl fluoride, but not by EDTA. The enzyme is most active at pH 9-10, and at 45 C, although it is unstable at 60 C.
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