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›› 2014, Vol. 14 ›› Issue (6): 1015-1019.

• 生化工程专栏 • 上一篇    下一篇

聚乙烯醇脱氢酶的分离纯化及其酶学性质

李敏2 堵国成   

  1. 内蒙古师范大学生命科学与技术学院 江南大学工业生物技术教育部重点实验室
  • 收稿日期:2014-01-10 修回日期:2014-05-27 出版日期:2014-12-20 发布日期:2014-12-20
  • 通讯作者: 李敏2

Purification and Enzymatic Properties of Polyvinyl Alcohol Dehydrogenase

LI Min DU GUo-cheng,   

  1. Inner Mongolia Normal University Lab of Environmental Biotechnology, School of biotechnology Southern Yangtze University
  • Received:2014-01-10 Revised:2014-05-27 Online:2014-12-20 Published:2014-12-20
  • Contact: LI Min

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被引次数

1

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 kDa，最适作用温度为35℃，最适作用pH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.

关键词: 聚乙烯醇脱氢酶, 纯化, 酶学性质, 沉淀, 层析

Abstract: 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 kDa, its optimal reaction temperature was 35℃, and the optimum pH 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.

Key words: polyvinyl alcohol dehydrogenase, purification, enzymatic property, precipitation, chromatography

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