人工合成的单链甜蛋白monellin基因在大肠杆菌中的高效表达  

High-level Expression of A Sweet Protein, Single-chain Monellin, in E.coli

作　　者：陈忠军[1] 路福平[1] 蔡恒[1] 杜连祥[1] 

机构地区：[1]天津市工业微生物重点实验室天津科技大学生物工程学院

出　　处：《食品与发酵工业》2005年第9期18-20,共3页Food and Fermentation Industries

摘　　要：根据已报道的单链monellin甜蛋白的氨基酸序列,采用细菌偏爱密码子,人工合成了全长294bp的monellin基因。插入到大肠杆菌表达载体pET22b中,构建重组分泌型表达载体pETMO。经IPTG诱导pETMO所含有的甜蛋白基因可在大肠杆菌BL21(DE3)中高效表达,表达量占菌体可溶性蛋白的44.8%。且经纯化后测定其甜度是蔗糖的3000倍。According to the amino acid sequence of monellin, a single chain 294bp monellin gene was synthesized based on E. coli biased codons. The fragment was inserted into vector pET-22b to construct the recombinant secretary plasmid pETMO. Induced by IPTG, monellin could be produced at a high level in E. coli BL21 （DE3）, accounts for 44.8 % of the soluble protein. The E. coli expressed single-chain monellin was 3000 times sweeter than sucrose.

关 键 词：甜蛋白MONELLIN 细菌优化密码子 重组PCR 诱导表达 甜蛋白基因 大肠杆菌 高效表达 人工合成 N基因 单链 

分 类 号：Q786[生物学—分子生物学]