CORC  > 厦门大学  > 化学化工-已发表论文
The improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions
Wang, Shizhen ; Wang, Jing ; Zhou, Xiaofen ; Guo, Yingxia ; Fang, Baishan ; Wang SZ(王世珍) ; Fang BS(方柏山)
刊名http://dx.doi.org/10.1007/s12257-013-0125-7
2013
英文摘要Natural Science Foundation of Fujian Province of China [2012J01049]; Chinese National Natural Science Foundation [41176111]; Fundamental Research Funds for the Central Universities [2013121029]; The substitution of the catalytic zinc ion of glycerol dehydrogenase (GDH) from Klebsiella pneumonia sp. by divalent metal ions, Mn2+ and Mg2+, enabled improvements of activity, substrate promiscuity and stability. The activity of Mn-GDH and Mg-GDH improved several folds in comparison to the native GDH. The activity of substituted GDH towards non-natural substrates, 4-chloroacetoacetate, 3-chloroacetylpyridine, p-chloroacetophenone, and acetophenone was 30 folds higher than native GDH. Manganese substitution increased the half-life of GDH by 6 folds at 60 and 70A degrees C. The two-fraction first order inactivation models fitted the nonlinear thermal inactivation curves well. Combined with the kinetic and thermodynamic analysis, further mechanistic insights to the metal ion roles in thermostability enhancements were studied. The thermodynamic parameters of inactivation, enthalpy, entropy and the Gibbs free energy indicated that Mn-GDH was stabilized entropically and elucidated the mechanisms of enzyme inactivation.
语种英语
出版者KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
内容类型期刊论文
源URL[http://dspace.xmu.edu.cn/handle/2288/88984]  
专题化学化工-已发表论文
推荐引用方式
GB/T 7714
Wang, Shizhen,Wang, Jing,Zhou, Xiaofen,et al. The improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions[J]. http://dx.doi.org/10.1007/s12257-013-0125-7,2013.
APA Wang, Shizhen.,Wang, Jing.,Zhou, Xiaofen.,Guo, Yingxia.,Fang, Baishan.,...&方柏山.(2013).The improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions.http://dx.doi.org/10.1007/s12257-013-0125-7.
MLA Wang, Shizhen,et al."The improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions".http://dx.doi.org/10.1007/s12257-013-0125-7 (2013).
个性服务
查看访问统计
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。


©版权所有 ©2017 CSpace - Powered by CSpace