首页 | 本学科首页   官方微博 | 高级检索  
     

人工合成的单链甜蛋白monellin基因在大肠杆菌中的高效表达
引用本文:陈忠军,路福平,蔡恒,杜连祥.人工合成的单链甜蛋白monellin基因在大肠杆菌中的高效表达[J].食品与发酵工业,2005,31(9):18-20.
作者姓名:陈忠军  路福平  蔡恒  杜连祥
作者单位: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,天津,300222
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。

关 键 词:甜蛋白monellin  细菌优化密码子  重组PCR  诱导表达
收稿时间:03 23 2005 12:00AM
修稿时间:07 4 2005 12:00AM

High-level Expression of A Sweet Protein, Single-chain Monellin, in E. coli
Chen Zhongjun,Lu Fuping,Cai Heng,Du Lianxiang.High-level Expression of A Sweet Protein, Single-chain Monellin, in E. coli[J].Food and Fermentation Industries,2005,31(9):18-20.
Authors:Chen Zhongjun  Lu Fuping  Cai Heng  Du Lianxiang
Abstract: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.
Keywords:monellin  bacteria preferred condon  recombination PCR  inducing expression
本文献已被 CNKI 维普 万方数据 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号