Overexpression of a sweet protein monellin in Escherichia coli / 生物工程学报
Chinese Journal of Biotechnology
; (12): 568-572, 2005.
Article
in Zh
| WPRIM
| ID: wpr-305201
Responsible library:
WPRO
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.
Full text:
1
Index:
WPRIM
Main subject:
Plant Proteins
/
Recombinant Proteins
/
Protein Engineering
/
Escherichia coli
/
Genetics
/
Metabolism
/
Methods
Language:
Zh
Journal:
Chinese journal of biotechnology
Year:
2005
Type:
Article