• Korean Journal of Microbiology
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• v.25 no.2
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• pp.148-156
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• 1987

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 $45^{\circ}C$ and the optimum pH was 6.5. The enzyme was found to be stable at temperature below $35^{\circ}C$ and rapidly inactivated at higher temperatures. Km values for ferulic acid, vanillic acid, dihydroxyphenylalanine (DOPA) were 48.6.$\mu$M, 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.