粗毛栓菌胞外锰过氧化物酶的纯化及性质(英文)  

Purification and Characterization of an Extracellular Manganese Peroxidase from Trametes gallica

作　　者：孙迅[1] 朱陶[1] 张义正[2] 

机构地区：[1]菏泽学院生命科学系,山东菏泽274015 [2]四川大学生命科学学院,四川成都610064

出　　处：《微生物学杂志》2012年第5期40-45,共6页Journal of Microbiology

摘　　要：培养于麦草粉上的白腐担子菌粗毛栓菌分泌胞外木质纤维素降解酶(纤维素酶、木聚糖酶、漆酶、锰过氧化物酶和木质素过氧化物酶)。经过超滤、盐析、离子交换层析、凝胶过滤和活性聚丙烯酰胺凝胶电泳等步骤,获得了初步纯化的锰过氧化物酶组分。利用变性聚丙烯酰胺凝胶电泳和等电点聚焦技术所测定的锰过氧化物酶的相对分子质量和等电点分别为35.7 ku和pI 2.8。研究结果表明,所纯化的锰过氧化物酶在407nm处具有最大光吸收峰,该酶最适作用pH值和温度分别为pH 5.3和35℃。When cultured on wheat straw powder,the white-rot basidiomycete Trametes gallica secreted extracellular lignocellulolytic enzymes including cellulase,xylanase,laccase,manganese-dependent peroxidase（MnP） and lignin peroxidase（LiP）.By using membrane ultra-filtration,salting-out,ion-exchange chromatography,gel filtration and native-polyacrylamide gel electrophoresis（PAGE）,a preliminarily purified MnP was obtained.SDS-PAGE and isoelectric focusing（IEF） were used to evaluate the molecular weight and isoelectric point（pI） of the enzyme,respectively.The purified MnP had a molecular weight of 35.7 ku and a pI of 2.8.The result showed that the MnP had a maximum absorbance at 407 nm,an optimal pH of 5.3 and an optimal reaction temperature of 35 ℃.

关 键 词：粗毛栓菌 木质纤维素降解酶 锰过氧化物酶 纯化 性质分析 

分 类 号：Q936[生物学—微生物学]