Yarrowia lipolytica TH65가 생산하는 Alkaline Proteinase의 정제 및 특성

  • 유춘발 (대구대학교 공과대학 식품공학과) ;
  • 김창화 (대구대학교 공과대학 식품공학과) ;
  • 진영호 (대구대학교 공과대학 식품공학과) ;
  • 진익렬 (경북대학교 자연과학대학 미생물학과)
  • Published : 1996.06.01

Abstract

An alkaline proteinase produced by Yarrowia lipolytica TH65 was purified by 40-65% ammonium sulfate fractionation, DEAE-cellulose chromatography, and gel filtration with Sephadex G-100 and Sephadex G-75. The purified enzyme was shown as a single band on SDS-PAGE, and its molecular weight 31,500. Optimum temperature and pH were 40$\circ$C and 8.5-9.0, respectively, and the enzyme was stable below 40$\circ$C and in the pH range of 6-8. The enzyme was strongly inhibited by divalent ions, completely by PMSF, and partially by EDTA, EGTA, and phenanthroline. But the inhibitory effect in the presence of EDTA, EGTA and phenanthroline could be reversed by addition of Ca$^{2+}$. Thus, these results indicated that the purified enzyme was an alkaline serine proteinase (E.C. 3.4.21.14).

Keywords

References

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