| Title | Purification and Characterization of Caseinolytic Extracellular protease from Bacillus amyloliquefaciens S94 |
|---|---|
| Author | Eui-Sun Son and Jong-Il Kim * |
| Address | Department of Food and Microbial Technology, Seoul Women's University |
| Bibliography | Journal of Microbiology, 40(1),26-32, 2002, |
| DOI | |
| Key Words | extracelluar protease, alkaline protease, psychrotrophic Bacillus |
| 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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