Title Pleurotus ostreatus에서 분리한 아스콜빈산 산화효소의 특성
Author 황윤엽 · 김연란 · 강사욱
Address 서울대학교 자연과학대학 미생물학과
Bibliography Korean Journal of Microbiology, 26(4),324-331, 1988
DOI
Key Words Pleurotus ostreatus, ascorbate oxidizing enzyme
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 2.2uM, which indicates that the enzyme has the same affinity towards both substrates.
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