Purification and Enzymology Characteristics of Laccase Derived from Ganoderma lucidum Karst Mutant G1502

Abstract

Abstract: The laccase derived from Ganoderma lucidum Karst mutant G1502 was purified and characterized in enzymology.The result of polypropylene amine gelatin electrophoresis(PAGE) analysis indicated that this strain in the fermentation medium only produces single laccase.Its cultured liquid with laccase was condensed by dialyzing,and purified by DEAE-cellulose ion exchange chromatography.The enzymic purity increases 24.28 fold,and the recovery ratio of enzyme reaches 18.66%.The Km and Vmax for oxidizing guaiacol,the kinetic parameters of enzyme,are 1.94×10-4 mol/L and 2.28×10-6 mol/L·min,respectively.The activities are inhibited by Fe2+,Co2+,Ca2+,Na+ and Ba2+ and induced by K+ and Cu2+,but Cu2+ is weak inducer.

Key words: Ganoderma lucidum Karst, laccase, purification, enzymology charatferisties

WANG Sui-Lou, WANG Qiong-Bo. Purification and Enzymology Characteristics of Laccase Derived from Ganoderma lucidum Karst Mutant G1502[J]. FOOD SCIENCE, 2008, 29(5): 287-291.

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Purification and Enzymology Characteristics of Laccase Derived from Ganoderma lucidum Karst Mutant G1502

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