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Increased 2,3-butanediol production by changing codon usages in Escherichia coli

Authors
Park, Seo-YoungKim, BorimLee, SoojinOh, MinkyuWon, Jong-InLee, Jinwon
Issue Date
Sep-2014
Publisher
WILEY-BLACKWELL
Keywords
Escherichia coli; codon optimization; ribosome-binding site; 2; 3-butanediol; acetolactate decarboxylase; acetoin reductase
Citation
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY, v.61, no.5, pp.535 - 540
Journal Title
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
Volume
61
Number
5
Start Page
535
End Page
540
URI
https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/16610
DOI
10.1002/bab.1216
ISSN
0885-4513
Abstract
The natural microorganism Escherichia coli without modification is not suitable for the efficient production of 2,3-butanediol (2,3-BD) on an industrial scale because of its poor metabolic performance. Metabolic capacities of E. coli have been improved to produce 2,3-BD efficiently, the performance of which is possible for producing such a product. Codon optimization with the ribosome-binding site for the efficient production of target genes (budA and budC) was achieved by molecular engineering, which allowed the metabolic engineering to proceed to the next level. As a result, comparing the productivity in 26H, where the amount of p18COR was 1.04g/L and that of p18WTR was 0.41g/L, represents an approximate 60.6% increase in the productivity of the p18WTR with codon optimization. In other words, p18COR was 2.54-fold greater than p18WTR in the production of 2,3-BD. (C) 2014 International Union of Biochemistry and Molecular Biology, Inc.
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