期刊
ORGANIC & BIOMOLECULAR CHEMISTRY
卷 13, 期 6, 页码 1897-1903出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4ob01441c
关键词
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资金
- Biotechnology and Biosciences Research Council
- Dr Reddy's [BB/H01618X/1]
- Biotechnology and Biological Sciences Research Council [1359511] Funding Source: researchfish
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 degrees 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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