蜡状芽孢杆菌几丁质脱乙酰基酶克隆和表达  

Cloning and Recombinant Expression of Chitin Deacetylase from Bacillus cereus

作　　者：孙玉英[1,2] 张继泉[2] 王淑军[1] 严翠 

机构地区：[1]淮海工学院海洋学院,江苏连云港222005 [2]中国科学院海洋研究所实验海洋生物学重点实验室,山东青岛266071

出　　处：《食品研究与开发》2016年第21期151-155,共5页Food Research and Development

基　　金：碳谷-江苏海资院海洋先进材料联合研究中心项目(TG-201402);连云港市第五期"521工程"科研项目

摘　　要：从产几丁质脱乙酰基酶的蜡状芽孢杆菌(Bacillus cereus M1)中获得了几丁质脱乙酰基酶BcCDA基因序列,并在大肠杆菌中实现了其高效分泌表达以及一步亲和法纯化重组几丁质脱乙酰基酶BcCDA,经SDS-PAGE检测该酶为单一条带,其分子量约为23 kD,所得重组BcCDA的具有脱乙酰基酶活性,其比活力为11 608.31U/mg。该研究为BcCDA作用机制的进一步研究和BcCDA的利用鉴定基础。A gene encoding chitin deacetylase from Bacillus cereus M1 （BcCDA） was obtained. BcCDA was recombinant expressed in Escherichia coli at the secretion form and purified by affinity chromotagraphy.The purity of the purified BcCDA was tested by SDS-PAGE, which molecular weight was approximately 23 kD.The recombinant BcCDA had deacetylase activity, which specific activity was 11 608.31 U/mg. The research would provide a basis for studying the action mechnism and harness of BcCDA.

关 键 词：几丁质脱乙酰基酶 蜡状芽孢杆菌 分泌表达 纯化 

分 类 号：Q936[生物学—微生物学] Q78