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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.

Authors
  • Summers, Benjamin D
  • Omar, Muhiadin
  • Ronson, Thomas O
  • Cartwright, Jared
  • Lloyd, Michael
  • Grogan, Gideon
Type
Published Article
Journal
Organic & Biomolecular Chemistry
Publisher
The Royal Society of Chemistry
Publication Date
Feb 14, 2015
Volume
13
Issue
6
Pages
1897–1903
Identifiers
DOI: 10.1039/c4ob01441c
PMID: 25501564
Source
Medline
License
Unknown

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.

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