Department of Chemistry, DDU Gorakhpur University, Gorakhpur 273009, India.
Environ Technol. 2011 Aug-Sep;32(11-12):1287-94. doi: 10.1080/09593330.2010.535177.
Lignin peroxidase has been purified to homogeneity using a process of concentration by ultrafiltration and anion exchange chromatography on diethylaminoethyl (DEAE) cellulose from the liquid culture filtrate of the brown rot fungi Gleophyllum striatum MTCC-1117. The molecular mass of the purified enzyme is 43 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The K(m) values for the enzyme using veratryl alcohol, hydrogen peroxide and n-propanol were 66 microM, 82 microM and 476 microM, respectively. The pH and temperature optima of the enzyme were 2.8 and 25 degrees C, respectively. The enzyme is completely inhibited by 20% of the water miscible organic solvents acetone dioxane, diethylether, acetonitrile and dimethylformamide. The lignin peroxidase oxidizes polycyclic aromatic hydrocarbons pyrene, acenaphthene, anthracene, dibenothiophene and 9-methyl anthracene.
木聚糖酶已通过超滤浓缩和二乙氨基乙基（DEAE）纤维素阴离子交换层析从褐腐真菌密粘褶菌 MTCC-1117 的液体培养滤液中纯化到均一性。通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）分析，确定纯化酶的分子量为 43 kDa。该酶使用藜芦醇、过氧化氢和正丙醇的 K(m) 值分别为 66 μM、82 μM 和 476 μM。酶的最适 pH 值和温度分别为 2.8 和 25°C。该酶完全被 20%的水溶性有机溶剂丙酮、二恶烷、二乙醚、乙腈和二甲基甲酰胺抑制。木聚糖酶氧化多环芳烃芘、苊、蒽、二苯并噻吩和 9-甲基蒽。
