Title |
Pleurotus ostreatus의 Laccase 작용특성 |
Author |
김규중 * · 신광수 · 맹진수 · 강사욱 · 하영칠 · 홍순우 |
Address |
* 강를대학 생물학과; 서울대학교 자연과학대학 미생물학과 |
Bibliography |
Korean Journal of Microbiology, 25(2),148-156, 1987 |
DOI |
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Key Words |
Pleurotus ostreatus, laccase |
Abstract |
Extracellular laccase (E.C. 1.10.3.2) from the culture filtrate of Pleurotus ostreatus was purified by ammonium sulfate precipctation, protamine sulfate precipitation, DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel permeation chromatography. The molecular weight of the enzyme was estimated by SDS-polyacrylamide gel electrophoresis to be 58,000 and the isoelectric point was 3.75. The optimum temperature for the enzyme was about 45℃ and the optimum pH was 6.5. The enzyme was found to be stable at temperature below 35℃ and rapidly inactivated at higher temperatures. Km values for ferulic acid, vanillic acid, dihydroxyphenylalanine (DOPA) were 48.6uM, 0.52mM, and 2.73mM, respectively, which indicates that the enzyme has much higher affinity towards ferulic acid. The reaction products of the enzyme were separated by TLC and HPLC. |
Download PDF |
Kor_250210_148-156p.pdf |