title: Characterization of an enzyme from Rhizoctonia praticola which polymerizes phenolic compounds.
abstract: 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.
mesh_terms: 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
chemical_list: D010636:Phenols; D003300:Copper; D004156:Catechol Oxidase