An alkaline proteinase produced by Yarrowia lipolytica 504D

Yarrowia lipolytica 504D의 Alkaline Proteinase 특성

  • Kim, Chang-Hwa (Department of Microbiology, Kyungpook National University) ;
  • Jin, Ingnyol (Department of Microbiology, Kyungpook National University) ;
  • Yu, Choon-Bal (Department of Food Science and Technology, Taegu University)
  • 김창화 (경북대학교 미생물학과) ;
  • 진익렬 (경북대학교 미생물학과) ;
  • 유춘발 (대구대학교 식품공학과)
  • Received : 1998.05.20
  • Accepted : 1998.08.21
  • Published : 1998.09.01


An alkaline proteinase secreted from Yarrowia lipolytica 504D was purified by salting-out and column chromatography. The molecular weight of the purified enzyme was about 32,000 Da estimated by SDS-PAGE. The optimal condition for the activity of the enzyme was at pH 9.5 and $42^{\circ}C$ The enzyme was stable up to $45^{\circ}C$ and at the range of pH 4-10. Because the enzyme was inhibited by PMSF as well as EDTA, EGTA, and phenan-throlin, it is uncertain whether the enzyme is serine proteinase or metalloproteinase. However, almost all metal salts tested did not increase the enzyme activity, and Ca salt restored the activity of the enzyme inactivated by EDTA. Therefore, the purified enzyme seems to be an serine proteinase (E.C.


alkaline protease;yeast;yarrowia lipolytica