海藻糖微生物酶法合成机制的研究  

STUDY ON SYNTHESIS OF TREHALOSE BY A NOVEL MICROBIAL ENZYMATIC SYSTEM

作　　者：王绍校[1] 吴襟[2] 高春霄[2] 陈萌[2] 蔡同一[1] 张树政[2] 

机构地区：[1]中国农业大学食品学院,北京100094 [2]中国科学院微生物研究所,北京100080

出　　处：《微生物学通报》2003年第2期36-40,共5页Microbiology China

基　　金：国家"8 63"课题资助项目 (No 2 0 0 1AA2 1 4 1 4 1 )~~;微生物资源国家重点实验室课题资助项目 (No 0 2 1 0 2 4)

摘　　要：来源于嗜酸热古菌芝田硫化叶菌 (Sulfolobusshibatae)B1 2的麦芽寡糖基海藻糖合酶(MTSase)和麦芽寡糖基海藻糖海藻糖水解酶 (MTHase)基因在大肠杆菌中获得表达。将获得纯化的两个酶 ,分别以麦芽寡糖和淀粉为转化底物 ,在pH5 5 ,6 0℃条件下合成海藻糖。从反应产物分析结果可知 ,两个酶合成海藻糖时能利用的最小底物是麦芽四糖 ,海藻糖产率与麦芽寡糖链长正相关。同时还发现两个酶都具有轻微的α 1 ,4 葡萄糖苷酶活性 ,能在麦芽寡糖还原末端水解α 1 ,4糖苷键 ,生成葡萄糖分子 ,其反应最小底物分别是麦芽三糖和四糖。The genes of maltooligosyl trehalose synthase (MTSase) and maltooligosyl trehalose trehalohydrolase (MTHase) from Sulfolobus shibatae B12 were expressed in E coli Trehalose was synthesized from starch by purified MTSase and MTHase at pH 5 5 and 60℃ Based on a detailed analysis of the reaction products, it was verified that the minimal maltooligosaccharide as substrates for the enzymes was maltotetraose in the reaction The yield of trehalose increased with substrate length At the same time, low α 1,4 glycosidase activity were found in two enzymes, which hydrolyzed α 1,4 glycosidic linkage of the reducing end of maltooligosaccharide or starch Glucoses were produced as by products The minimal maltooligosaccharide as substrates for glycosidases were maltotriose and maltotetraose in the hydrolysis reaction, respectively It was presumed there were two different active centers in the MTSase

关 键 词：海藻糖 麦芽寡糖基海藻糖合酶 麦芽寡糖基海藻糖海藻基水解酶 淀粉 微生物酶法合成 二糖 

分 类 号：Q591[生物学—生物化学]