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 |
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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. |
Download PDF |
Kor_270405_348-356p.pdf |