Enhanced production of epsilon-caprolactone by overexpression of NADPH-regenerating glucose 6-phosphate dehydrogenase in recombinant Escherichia coli harboring cyclohexanone monooxygenase gene
- Authors
- Lee, Won-Heong; Park, Jin-Byung; Park, Kyungmoon; Kim, Myoung-Dong; Seo, Jin-Ho
- Issue Date
- Aug-2007
- Publisher
- SPRINGER
- Keywords
- cyclohexanone monooxygenase; Escherichia coli; glucose 6-phosphate dehydrogenase; fed-batch; substrate/product inhibition; NADPH
- Citation
- APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, v.76, no.2, pp.329 - 338
- Journal Title
- APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 76
- Number
- 2
- Start Page
- 329
- End Page
- 338
- URI
- https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/23559
- DOI
- 10.1007/s00253-007-1016-7
- ISSN
- 0175-7598
- Abstract
- Whole-cell conversion of cyclohexanone to epsilon- was attempted by recombinant Escherichia coli BL21(DE3) expressing cyclohexanone monooxygenase (CHMO) of Acinetobacter calcoaceticus NCIMB 9871. High concentrations of cyclohexanone and epsilon-caprolactone reduced CHMO-mediated bioconversion of cyclohexanone to epsilon-caprolactone in the resting recombinant E. coli cells. Metabolically active cells were employed by adopting a fed-batch culture to improve the production of epsilon-caprolactone from cyclohexanone. A glucose-limited fed-batch Baeyer-Villiger oxidation where a cyclohexanone level was maintained less than 6 g/l resulted in a maximum epsilon-caprolactone concentration of 11.0 g/l. The maximum epsilon-caprolactone concentration was improved further to 15.3 g/l by coexpression of glucose-6-phosphate dehydrogenase, an NADPH-generating enzyme encoded by the zwf gene which corresponded to a 39% enhancement in epsilon-caprolactone concentration compared with the control experiment performed under the same conditions.
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