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.
李敏 堵国成. 聚乙烯醇脱氢酶的分离纯化及其酶学性质[J]. , 2014, 14(6): 1015-1019.
LI Min DU GUo-cheng;. Purification and Enzymatic Properties of Polyvinyl Alcohol Dehydrogenase. , 2014, 14(6): 1015-1019.
2014, Vol. 14 
