食品工业科技2018，Vol.39Issue(10)：100-104,5.DOI:10.13386/j.issn1002-0306.2018.10.019
醋酸菌中乙醛脱氢酶的分离纯化及酶学性质
Isolation, purification and enzymatic properties of aldehyde dehydrogenase from Acetobacter pomorum
摘要
Abstract
Acetaldehyde dehydrogenase (ALDH)was isolated and purified by the Acetobacter pomorum obtained from the self-screening of the laboratory,cell disruption,ammonium sulfate fractionation,DEAE-Sepharose fast flow chromatography and Superdex G-75 prep grade chromatography separation and purification of enzyme liquid aldehyde dehydrogenase,and its enzymatic properties was studied.The molecular weight of the enzyme was 221.60 kDa,in which the subunit molecular mass was 54.41 kDa,respectively.The crude enzyme was purified 10.16 times with 20.25 U/mg of enzyme activity and the recovery rate of ALDH was 6.53％.The enzyme properties showed that its optimal reaction temperature was 50 ℃,and the enzyme had a good stability between 40 ℃℃ and 50 ℃;The optimal reaction pH of ALDH was 7.0,and there was a good stability between pH5.5 and pH7.5.The effects of different metal ions on enzyme activity showed that the enzyme was strongly inhibited by Na +,K+,Zn2+,Ba2+,however,Mg2+ 、Ca2+ 、Al3+ 、Li + 、Cu2+ activated the enzyme activity.The substrate specificity of ALDH showed that the enzyme had higher enzyme activity on acetaldehyde,which was on straight aldehydes.ALDH had high enzyme activity,which provided a foundation for further investigation of biological function.关键词
醋酸菌/乙醛脱氢酶/分离纯化/酶学性质Key words
Acetobacter pomorum/aldehyde dehydrogenase/isolation and purification/enzyme properties分类
轻工纺织引用本文复制引用
张鸣明,宋勇强,李素岳,胡先望,梁宁,张春园..醋酸菌中乙醛脱氢酶的分离纯化及酶学性质[J].食品工业科技,2018,39(10):100-104,5.基金项目
甘肃省创新团队建设计划(1207TFCA011) （1207TFCA011）
甘肃-青海食品研究开发与检测联合实验室建设(1606RTSA337) （1606RTSA337）
食品酶制剂共性关键技术研究创新团队(098TTCA013) （098TTCA013）
兰州科技计划项目(2015-4-6). （2015-4-6）
