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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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