期刊
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
卷 76, 期 2, 页码 329-338出版社
SPRINGER
DOI: 10.1007/s00253-007-1016-7
关键词
cyclohexanone monooxygenase; Escherichia coli; glucose 6-phosphate dehydrogenase; fed-batch; substrate/product inhibition; NADPH
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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