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Enhanced production of ε-caprolactone by overexpression of NADPH-regenerating glucose 6-phosphate dehydrogenase in recombinant Escherichia coli harboring cyclohexanone monooxygenase gene

Title
Enhanced production of ε-caprolactone by overexpression of NADPH-regenerating glucose 6-phosphate dehydrogenase in recombinant Escherichia coli harboring cyclohexanone monooxygenase gene
Authors
Lee W.-H.Park J.-B.Park K.Kim M.-D.Seo J.-H.
Ewha Authors
박진병
SCOPUS Author ID
박진병scopus
Issue Date
2007
Journal Title
Applied Microbiology and Biotechnology
ISSN
0175-7598JCR Link
Citation
vol. 76, no. 2, pp. 329 - 338
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Whole-cell conversion of cyclohexanone to ε-caprolactone was attempted by recombinant Escherichia coli BL21(DE3) expressing cyclohexanone monooxygenase (CHMO) of Acinetobacter calcoaceticus NCIMB 9871. High concentrations of cyclohexanone and ε-caprolactone reduced CHMO-mediated bioconversion of cyclohexanone to ε-caprolactone in the resting recombinant E. coli cells. Metabolically active cells were employed by adopting a fed-batch culture to improve the production of ε-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 ε-caprolactone concentration of 11.0 g/l. The maximum ε-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 ε-caprolactone concentration compared with the control experiment performed under the same conditions. © 2007 Springer-Verlag.
DOI
10.1007/s00253-007-1016-7
Appears in Collections:
엘텍공과대학 > 식품공학전공 > Journal papers
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