Abstract

Using the original technique of treating biomass with β-glucosidase, a pool of extracellular fungal enzymes was obtained for the first time from the mycelium of basidiomycete Neonothopanus nambi. Two protein fractions containing enzymes with oxidase activity were isolated from the extract by gel-filtration chromatography and conventionally called F1 and F2. Enzyme F1 has a native molecular weight of 80–85 kDa and does not contain chromophore components; however, it catalyzes the oxidation of veratryl alcohol with K_m = 0.52 mM. Probably, this enzyme is an alcohol oxidase. Enzyme F2 with a native molecular weight of approximately 60 kDa is a FAD-containing protein. It catalyzes the cooxidation of phenol with 4-aminoantipyrine without the addition of exogenous hydrogen peroxide, which distinguishes it from the known peroxidases. It was assumed that this enzyme may be a mixed-function oxidase. F2 oxidase has K_m value 0.27 mM for phenol. The temperature optimums for oxidases F1 and F2 are 22–35 and 55–70°C, and pH optimums are 6 and 5, respectively.

中文翻译：

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担子菌新拟南芥的胞外氧化酶：分离和一些性质。

摘要

使用原始的用β-葡萄糖苷酶处理生物质的技术，第一次从担子菌Neonothopanus nambi的菌丝体中获得了池外真菌酶。通过凝胶过滤色谱法从提取物中分离出两个含有氧化酶活性酶的蛋白质级分，通常称为F1和F2。酶F1的天然分子量为80-85 kDa，不含发色团成分。但是，它会催化K _m氧化藜芦醇= 0.52毫米。该酶可能是醇氧化酶。天然分子量约为60 kDa的酶F2是一种含FAD的蛋白质。它催化苯酚与4-氨基安替比林的共氧化而无需添加外源过氧化氢，这使其与已知的过氧化物酶有所区别。假定该酶可以是混合功能氧化酶。F2氧化酶的苯酚K _m值为0.27 mM。氧化酶F1和F2的最适温度分别为22–35和55–70°C，最适pH分别为6和5。