Author:
Bollag Jean-Marc,Sjoblad Roy D.,Liu Shu-Yen
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 °C. According to these and additional characteristics it appears that the enzyme belongs to the class of laccases.
Publisher
Canadian Science Publishing
Subject
Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology
Cited by
61 articles.
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