Title Pleurotus ostreatus에서 분비되는 peroxidase의 특성
Author 배성호 · 신광수 · 강사욱 · 하영칠 · 최선진 * · 김규중 ** · 최형태 ***
Address 서울대학교 자연과학대학 미생물학과; * 서울대학교 치과대학 미생물학교실; ** 강릉대학교 생물학과; *** 강원대학교 자연과학대학 미생물학과
Bibliography Korean Journal of Microbiology, 27(4),348-356, 1989
DOI
Key Words Pleurotus ostreatus, extracellular peroxidase, iron protoporphyrin IX
Abstract An extracellular peroxidase found in culture broth of Pleurotus ostreatus was induced by syringic acid. This enzyme was fractionated by DEAE Sephadex A-50 ion exchange chromatography and gel filtration chromatogrphy on Sephadex G-150. The enzyme is a glycoprotein containing 35.7% carbohydrate. The results of SDS-linear polyacrylamide gradient gel electrophoresis and gel filtration indicate that the enzyme is a dimer consisted of identical subunits (Mr=72,400). The absorption spectrum of the enzyme indicates the presence of one mole of iron protoporphyrin IX per one mole of subunit. Isoelectric point of the enzyme is 4.26 and K_m values for H_2O_2 is 7.2uM. The enzyme showed its optimal activity at pH 3.5-4.0 and at 40℃. The Km values of this enzyme for ferulic acid and sinapic acid are 2.4 and 12.3 times higher than those of horseradish peroxidase, respectively.
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