Overexpression of a sweet protein monellin in Escherichia coli.
- Author:
Zhong-Jun CHEN
1
;
Heng CAI
;
Fu-Ping LU
;
Lian-Xiang DU
Author Information
1. Tan Key Lab of Industrial Microbiology, The College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300222, China.
- Publication Type:Journal Article
- MeSH:
Escherichia coli;
genetics;
metabolism;
Plant Proteins;
biosynthesis;
genetics;
Protein Engineering;
methods;
Recombinant Proteins;
biosynthesis;
genetics
- From:Chinese Journal of Biotechnology
2005;21(4):568-572
- CountryChina
- Language:Chinese
-
Abstract:
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.
