The extracellular enzyme with oxidase function was extracted from the Neonothopanus nambi luminescent fungus by using mild processing of mycelium with β-glucosidase and then isolated by gel-filtration chromatography. The extracted enzyme is found to be a FAD-containing protein, catalyzing phenol co-oxidation with 4-aminoantipyrine without addition of H₂O₂, which distinguishes it from peroxidases. This fact allowed us to assume that this enzyme may be a mixed-function oxidase. According to gel-filtration chromatography and SDS-PAGE, the oxidase has molecular weight of 60 kDa. The enzyme exhibits maximum activity at 55–70 °C and pH 5.0. Kinetic parameters K_m and V_max of the oxidase for phenol were 0.21 mM and 0.40 µM min⁻¹. We suggest that the extracted enzyme can be useful to develop a simplified biosensor for colorimetric detection of phenol in aqueous media, which does not require using hydrogen peroxide.

用β-葡萄糖苷酶对菌丝体进行温和处理，从Neonothopanus nambi发光真菌中提取具有氧化酶功能的胞外酶，然后通过凝胶过滤层析分离。发现提取的酶是一种含有 FAD 的蛋白质，在不添加 H ₂ O _{2 的}情况下催化苯酚与 4-氨基安替比林的共氧化，这将其与过氧化物酶区分开来。这一事实使我们能够假设这种酶可能是一种混合功能的氧化酶。根据凝胶过滤层析和 SDS-PAGE，氧化酶的分子量为 60 kDa。该酶在 55–70 °C 和 pH 5.0 时表现出最大活性。动力学参数 K _m和 V _max苯酚氧化酶的浓度为 0.21 mM 和 0.40 μM min ^-1。我们建议提取的酶可用于开发一种简化的生物传感器，用于水介质中苯酚的比色检测，不需要使用过氧化氢。