【摘要】 根据西非植物Ｄｉｏｓｃｏｒｅｏｐｈｙｌｌｕｍ　ｃｕｍｍｉｎｉｓｉｉ果实中分离到的ｍｏｎｅｌｌｉｎ甜蛋白的氨基酸序列，首次按照细菌优化密码子，人工合成了全长２９４ｂｐ的ｍｏｎｅｌｌｉｎ甜蛋白基因。克隆后序列分析表明，所获得基因与设计相符。构建了该基因的表达载体ｐＧＥＳＰ９。经４２℃诱导表达，发现所合成甜蛋白基因可在大肠杆菌ＢＬ２１中高效表达，表达量占菌体可溶性蛋白的２２．８％。分离纯化ｍｏｎｅｌｌｉｎ，经测定其甜度是相同重量蔗糖的１１００倍，且甜味纯正持久。更多还原

【Abstract】 According to the amino acid sequence of monellin isolated from the fruit of Western African plant Dioscoreophyllum Cumminisii., a single chain 294bp monellin sweet protein gene was synthesized using E. colt biased codons. After sequencing, an expression vector pGESP9 harboring the gene was constructed and was transferred into E. coli BL21. Heat inducing expression showed that the sweet protein could be produced at a high level: 22. 8% of the E. coli soluble protein. The flavorful monellin was 1100 times sweeter than sucrose on a same weight basis.更多还原