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Efficient kinetic bioresolution of 2-nitrocyclohexanol |
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| Authors: | Sinead E. Milner Maude Brossat Thomas S. Moody Curtis J. Elcoate Simon E. Lawrence Anita R. Maguire |
| Affiliation: | 1. Department of Chemistry, Analytical and Biological Chemistry Research Facility, University College Cork, Cork, Ireland;2. Biocatalysis Group, Almac Sciences, David Keir Building, Stranmillis Road, Belfast, BT9 5AG, United Kingdom;3. Department of Chemistry & School of Pharmacy, Analytical and Biological Chemistry Research Facility, University College Cork, Cork, Ireland |
| Abstract: | The kinetic bioresolution of 2-nitrocyclohexanol 1 was investigated by screening a range of hydrolases both for enantioselective transesterification and for enantioselective hydrolysis of the corresponding acetate. By appropriate choice of biocatalyst and conditions, both enantiomers of cis and trans 2-nitrocyclohexanol 1 can be accessed in enantiopure form. |
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