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Issue 6, 2015

E. coli cells expressing the Baeyer–Villiger monooxygenase ‘MO14’ (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor

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Abstract

The Baeyer–Villiger monooxygenase (BVMO) ‘MO14’ from Rhodococcus jostii RHA1, is an enantioselective BVMO that catalyses the resolution of the model ketone substrate bicyclo[3.2.0]hept-2-en-6-one to the (1S,5R)-2-oxa lactone and the residual (1S,5R)-substrate enantiomer. This regio-plus enantioselective behaviour is highly unusual for BVMOs, which often perform enantiodivergent biotransformations of this substrate. The scaleability of the transformation was investigated using fermentor-based experiments, in which variables including gene codon optimisation, temperature and substrate concentration were investigated. E. coli cells expressing MO14 catalysed the resolution of bicyclo[3.2.0]hept-2-en-6-one to yield (1S,5R)-2-oxa lactone of >99% ee and (1S,5R)-ketone of 96% ee after 14 h at a temperature of 16 °C and a substrate concentration of 0.5 g L−1 (4.5 mM). MO14 is thus a promising biocatalyst for the production of enantio-enriched ketones and lactones derived from the [3.2.0] platform.

Graphical abstract: E. coli cells expressing the Baeyer–Villiger monooxygenase ‘MO14’ (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor

Supplementary files

Article information


Submitted
09 Jul 2014
Accepted
05 Dec 2014
First published
05 Dec 2014

Org. Biomol. Chem., 2015,13, 1897-1903
Article type
Paper
Author version available

E. coli cells expressing the Baeyer–Villiger monooxygenase ‘MO14’ (ro03437) from Rhodococcus jostii RHA1 catalyse the gram-scale resolution of a bicyclic ketone in a fermentor

B. D. Summers, M. Omar, T. O. Ronson, J. Cartwright, M. Lloyd and G. Grogan, Org. Biomol. Chem., 2015, 13, 1897 DOI: 10.1039/C4OB01441C

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