High-level expression of a synthetic gene encoding a sweet protein, monellin, in Escherichia coli.
The expression of a synthetic gene encoding monellin, a sweet protein, in E. coli under the control of T7 promoter from phage is described. The single-chain monellin gene was designed based on the biased codons of E. coli so as to optimize its expression. Monellin was produced and accounted for 45% of total soluble proteins. It was purified to yield 43 mg protein per g dry cell wt. The purity of the recombinant protein was confirmed by SDS-PAGE.
Chen
Zhongjun
Z
Tianjin Key Lab of Industrial Microbiology, College of Biotechnology, Tianjin University of Science and Technology, 300222, Tianjin, P. R. China.
Cai
Heng
H
Lu
Fuping
F
Du
Lianxiang
L
D017123:Bacteriophage T7 / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D010940:Plant Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D013549:Sweetening Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D014162:Transfection / Q000379:methods
D010940:Plant Proteins; D011994:Recombinant Proteins; D013549:Sweetening Agents; C002541:monellin protein, Dioscoreophyllum cumminsii