[Overexpression of a sweet protein monellin in Escherichia coli].
According to the amino acid sequence of monellin, a single chain 294bp monellin gene was synthesized and inserted into vector pET-22b to yield the recombinant secretion plasmid pETMO. The single-chain monellin gene was designed based on the biased codons of E. coli so that its expression would be then optimized. Under the expressing conditions, monellin was produced accounting for 44.8% of total soluble proteins. The E. coli-expressed single-chain monellin is 3000 times sweeter than sucrose. The thermal-stability and acid-resistance of the protein are higher than the natural monellin.
Chen
Zhong-Jun
ZJ
Tan Key Lab of Industrial Microbiology, The College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300222, China.
Cai
Heng
H
Lu
Fu-Ping
FP
Du
Lian-Xiang
LX
D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D010940:Plant Proteins / Q000096:biosynthesis* / Q000235:genetics; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics
D010940:Plant Proteins; D011994:Recombinant Proteins; C002541:monellin protein, Dioscoreophyllum cumminsii