Abstract
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.
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Revisions requested 13 April 2005 and 26 May 2005; Revisions received 19 May 2005 and 30 August 2005
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Chen, Z., Cai, H., Lu, F. et al. High-level Expression of a Synthetic Gene Encoding a Sweet Protein, Monellin, in Escherichia coli. Biotechnol Lett 27, 1745–1749 (2005). https://doi.org/10.1007/s10529-005-3544-5
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DOI: https://doi.org/10.1007/s10529-005-3544-5