Department of Chemistry, D.D.U. Gorakhpur University, Gorakhpur, 273009, India.
Biochemistry (Mosc). 2009 Oct;74(10):1125-31. doi: 10.1134/s0006297909100083.
Lignin peroxidase from the liquid culture filtrate of Gloeophyllum sepiarium MTCC-1170 has been purified to homogeneity. The molecular weight of the purified enzyme was 42 kDa as determined by SDS-PAGE. The K(m) values were 54 and 76 microM for veratryl alcohol and H2O2, respectively. The pH and temperature optima were 2.5 and 25 degrees C, respectively. Depolymerization of coal by the fungal strain has been demonstrated using humic acid as a model of coal. Depolymerization of humic acid by the purified lignin peroxidase has been shown by the decrease in absorbance at 450 nm and increase in absorbance at 360 nm in presence of H2O2. Depolymerization of humic acid by the purified enzyme has also been demonstrated by the decrease in the viscosity with time of the reaction solution containing humic acid, H2O2, and the purified lignin peroxidase. The influence of NaCl and NaN3 and inhibitory effects of various metal chelating agents on the lignin peroxidase activity were studied.
从木层孔菌（Gloeophyllum sepiarium）MTCC-1170 的液体培养滤液中纯化出木质素过氧化物酶，达到了均一性。SDS-PAGE 测定该酶的分子量为 42 kDa。酶对藜芦醇和 H2O2 的 K(m)值分别为 54 和 76 μM。最适 pH 和温度分别为 2.5 和 25°C。用腐殖酸作为煤的模型，已经证明了真菌菌株对煤的解聚作用。在 H2O2 存在下，通过在 450nm 处吸光度降低和在 360nm 处吸光度增加，表明纯化的木质素过氧化物酶对腐殖酸进行了解聚。通过腐殖酸、H2O2 和纯化的木质素过氧化物酶反应溶液的粘度随时间的降低，也证明了腐殖酸的解聚。研究了 NaCl 和 NaN3 的影响以及各种金属螯合剂对木质素过氧化物酶活性的抑制作用。
