Simultaneous biocatalyst production and Baeyer-Villiger oxidation for bioconversion of cyclohexanone by recombinant Escherichia coli expressing cyclohexanone monooxygenase
- Authors
- Lee, W.-H.; Park, Y.-C.; Lee, D.-H.; Park, K.; Seo, J.-H.
- Issue Date
- 2005
- Publisher
- Humana Press
- Keywords
- Cyclohexanone monooxygenase; Escherichia coli; Fed-batch process; Simultaneous biocatalyst production and Baeyer-Villiger oxidation; ε-caprolactone
- Citation
- Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology, v.123, no.1-3, pp.827 - 836
- Journal Title
- Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
- Volume
- 123
- Number
- 1-3
- Start Page
- 827
- End Page
- 836
- URI
- https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/25642
- DOI
- 10.1007/978-1-59259-991-2_70
- ISSN
- 0273-2289
- Abstract
- Cyclohexanone monooxygenase (CHMO) catalyzing Baeyer-Villiger oxidation converts cyclic ketones into optically pure lactones, which have been used as building blocks in organic synthesis. A recombinant Escherichia coli BL21(DE3)/pMM4 expressing CHMO originated from Acinetobacter sp. NCIB 9871 was used to produce ε-caprolactone through a simultaneous biocatalyst production and Baeyer-Villiger oxidation (SPO) process. Afed-batch process was designed to obtain high cell density for improving production of ε-caprolactone. The red-batch SPO process gave the best results, 10.2 g/L of ε-caprolactone and 0.34 g/(L · h) of productivity corresponding to a 10.5- and 3.4-fold enhancement compared with those of the batch SPO, respectively. Copyright © 2005 by Humana Press Inc. All rights of any nature whatsoever reserved.
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Collections - College of Science and Technology > Department of Biological and Chemical Engineering > 1. Journal Articles
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