한국미생물·생명공학회지 (Microbiology and Biotechnology Letters)

  • 제23권1호
  • /
  • Pages.53-59
  • /
  • 1995
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  • 1598-642X(pISSN)
  • /
  • 2234-7305(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
권호 표지

Bacillus sp. KUN-17 균주가 생산하는 균체외 Serine Protease의 정제 및 특성

Purification and characterization of An Extracellular Serine Protease from Bacillus sp. strain KUN-17

  • 황세영 (고려대학교 자연과학대학 생물공학과)
  • 발행 : 1995.02.01
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초록

A protease isolated and purified 51 fold from the culture filtrate of a soil bacterium, Bacillus sp. KUN-17, which was appeared to be a monomeric protein with molecular weight of 38, 000 daltons, was suggested to be involved in the serine (-alkaline) protease (E.C 3.4.21.14) since its activity was selectively inhibited by phenylmethylsulfonyl fluoride (PMSF) and required 40$\circ$C and pH 10.5 for optimal condition. The half-life of the enzyme activity was 1 hr at 55$\circ$C, and the activity was maintained even under high concentrations of SDS or urea. The enzyme was indicated to perform random proteolysis from the fact that most of the chromogenic substrates employed were hydrolyzed by the enzyme. The affinity of the enzyme for natural proteins was approximately 10-times higher than ester compounds, and both substrates showed mutual inhibitory effect competitively for the enzyme activity.

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