Increased 2,3-butanediol production by changing codon usages in Escherichia coli
- Authors
- Park, Seo-Young; Kim, Borim; Lee, Soojin; Oh, Minkyu; Won, Jong-In; Lee, Jinwon
- Issue Date
- 9월-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
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
- Volume
- 61
- Number
- 5
- Start Page
- 535
- End Page
- 540
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/97520
- 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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Collections - College of Engineering > Department of Chemical and Biological Engineering > 1. Journal Articles
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