Bollag J M, Sjoblad R D, Liu S Y
Can J Microbiol. 1979 Feb;25(2):229-33. doi: 10.1139/m79-035.
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.
从真菌立枯丝核菌中分离并鉴定出一种能使多种外源酚类物质聚合的细胞外酚氧化酶。该酶通过DEAE -纤维素和葡聚糖G - 200柱层析，随后进行制备型聚丙烯酰胺凝胶电泳进行纯化。原子吸收光谱和电子顺磁共振光谱表明该酶含有铜，SDS凝胶电泳显示其分子量为78,000。以2,6 -二甲氧基苯酚为底物时，该酶的最适pH为6.7 - 6.9，最适温度为40℃。根据这些以及其他特性，该酶似乎属于漆酶类。
