Characterization of an enzyme from Rhizoctonia praticola which polymerizes phenolic compounds.
An extracellular phenol oxidase from the fungus Rhizoctonia praticola which polymerizes various xenobiotic phenols was isolated and characterized. The enzyme was purified by DEAE-cellulose and Sephadex G-200 chromatography followed by preparative polyacrylamide gel electrophoresis. Atomic absorption and EPR spectroscopy indicated the presence of copper, and SDS gel electrophoresis revealed a molecular weight of 78,000. With 2,6-dimethoxyphenol as substrate, the enzyme showed a pH optimum of 6.7--6.9, and a temperature optimum of 40 degrees C. According to these and additional characteristics it appears that the enzyme belongs to the class of laccases.
D004156:Catechol Oxidase / Q000032:analysis / Q000037:antagonists & inhibitors / Q000378:metabolism*; D003300:Copper / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D010636:Phenols / Q000378:metabolism*; D012232:Rhizoctonia / Q000201:enzymology*; D012988:Soil Microbiology; D013379:Substrate Specificity; D013696:Temperature
D010636:Phenols; D003300:Copper; D004156:Catechol Oxidase