食品与发酵工业2016，Vol.42Issue(5)：97-101,5.DOI:10.13995/j.cnki.11-1802/ts.201605017
琥珀酸半醛脱氢酶GabD4的表达、纯化及酶学性质分析
Heterologous expression, purification and enzymatic characterization of succinate-semialdehyde dehydrogenase GabD4
摘要
Abstract
The synthesis of succinate-semialdehyde dehydrogenase GabD4 gene,its expression in Escherichia coli and purification were described herein.The enzymatic characterization was analyzed.The study showed that the optimal reaction temperature of GabD4 was 37 ℃.The optimal reaction pH was pH 7.5 in phosphate buffer or pH 9.0 in glycine-NaOH buffer.Among several divalent metal ions,Cu2+ had stimulative effect on enzyme activity.Furthermore,GabD4 preferred to catalyze aldehyde substrates containing 3 ～5 carbon,and it had a Michaelis constant (Km) of 6.86 mmol/L and Vmax of 20.6 μmol/(min · mg protein) with acetaldehyde as substrate.These results could provide more information for research on enzymatic properties of GabD4.关键词
醛脱氢酶/重组表达/分离纯化/酶学性质Key words
aldehyde dehydrogenase/recombinant expression/protein purification/enzymatic properties引用本文复制引用
贾东旭,刘东,郑裕国..琥珀酸半醛脱氢酶GabD4的表达、纯化及酶学性质分析[J].食品与发酵工业,2016,42(5):97-101,5.基金项目
国家自然科学基金(21306173) （21306173）
浙江省自然科学基金青年基金(LQ15C010001) （LQ15C010001）
