聚乙烯醇脱氢酶的分离纯化及其酶学性质  

Purification and Enzymatic Properties of Polyvinyl Alcohol Dehydrogenase

作　　者：李敏[1] 堵国成[2] 

机构地区：[1]内蒙古师范大学生命科学与技术学院,内蒙古呼和浩特010022 [2]江南大学生物工程学院工业生物技术教育部重点实验室,江苏无锡214122

出　　处：《过程工程学报》2014年第6期1015-1019,共5页The Chinese Journal of Process Engineering

基　　金：教育部新世纪优秀人才支持计划资助项目(编号:NCET050488;NCET070378);国家重点基础研究发展计划(973)基金资助项目(编号:2007CB714036);国家杰出青年基金资助项目(编号:20625619);教育部长江学者和创新团队计划资助项目(编号:IRT0532)

摘　　要：采用(NH4)2SO4分级沉淀及Q-Sepharose HP柱层析两步纯化,首次从可高效降解聚乙烯醇(PVA)的混合菌系发酵产物中分离纯化获得了纯蛋白聚乙烯醇脱氢酶(PVADH),并对其酶学性质进行了研究.结果表明,PVADH分子量为134.3 k Da,最适作用温度为35℃,最适作用p H值为7.5;PVADH以仲醇为底物时酶活性普遍高于以其他醇类为底物时,PVADH与PVA反应产物中检测到羰基化合物,证实PVADH对PVA有降解作用.The polyvinyl alcohol（PVA） dehydrogenase（PVADH） was purified using ammonium sulfate precipitation and ion exchange chromatography of Q-Sepharose HP,and its enzymatic properties were studied.The results showed that the molecular weight of this enzyme was estimated to be 134.3 k Da,its optimal reaction temperature was 35 ℃,and the optimum p H value 7.5.Its activity was generally higher when the substrate was secondary alcohols.The carbonyl compounds were detected from the reaction products of PVADH and PVA,which confirmed the degradation effect of PVADH on PVA.

关 键 词：聚乙烯醇脱氢酶 纯化 酶学性质 沉淀 层析 

分 类 号：Q815[生物学—生物工程]