Journal of Microbiology

The Microbiological Society of Korea (한국미생물학회)
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Purification and Characterization of Caseinolytic Extracellular pretense from Bacillus amyloliquefaciens S94

  • Son, Eui-Sun (Department of Food and Microbial Technology, Seoul Women's University) ;
  • Kim, Jong-Il (Department of Food and Microbial Technology, Seoul Women's University)
  • Published : 2002.03.01
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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 pretense 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 $45^{\circ}C$, although it is unstable at $60^{\circ}C$.

Keywords

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