Properties of Ascorbate-Oxidizing Enzyme Purified from Pleurotus ostreatus

Pleurotus ostreatus에서 분리한 아스콜빈산 산화효소의 특성

  • 황윤엽 (서울대학교 자연과학대학 미생물학과) ;
  • 김연란 (서울대학교 자연과학대학 미생물학과) ;
  • 강사욱 (서울대학교 자연과학대학 미생물학과)
  • Published : 1988.12.01

Abstract

Ascorbate oxidizing enzyme from the crude extract of Pleurotus ostreatus was purified by ammonium sulfate precipitation, preparative polyacrylamide gel electrophoresis, DEAE Sepharose CL-6B ion exchange chromatography and Sephadex G-150 gel filtration chromatography. The molecular weight of the enzyme estimated by Sephadex G-150 gel filtration chromatography was 140,000 and that of its subunit by SDS-polyacrylamide gel electrophoresis 66,000. The optimum pH for the maximum activity of the enzyme was 5.2 and the isoelectric point of the enzyme was 6.0 Km values for L-ascorbic acid and D-isoascorbic acid were both 2.2.$\mu$M, which indicates that the enzyme has the asme affinity towards both substrates.

Keywords

Pleurotus ostreatus;ascorbate oxldiding enzyme