Journal
CHEMCATCHEM
Volume 5, Issue 12, Pages 3875-3881Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.201300409
Keywords
alcohols; cofactors; enzymes; deracemization; oxidation
Categories
Funding
- BIOTRAINS Marie-Curie Initial Training Network
- European Union [238531]
- Ministerio de Ciencia e Innovacion (MICINN) (Spain) [MICINN-12-CTQ2011-24237]
- MICINN under the Ramon y Cajal Program
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The nicotinamide adenine dinucleotide regeneration system present in Escherichiacoli cells was exploited for the oxidation and deracemisation of secondary alcohols with the overexpressed alcohol dehydrogenase from Rhodococcus ruber DSM 44541 (E.coli/ADH-A). Thus, various racemic alcohols were selectively oxidised with lyophilised or resting E.coli/ADH-A cells without need for an external cofactor or co-substrate. The addition of these substrates to the E.coli/ADH-A cells in buffer afforded the corresponding ketones and the remaining enantioenriched (R)-alcohols. This methodology was used for the desymmetrisation of a meso-diol and for the synthesis of the highly valuable raspberry ketone. Moreover, a biocatalytic concurrent process was developed with the resting cells of E.coli/ADH-A, ADH from Lactobacillus brevis, and glucose dehydrogenase for the deracemisation of various secondary alcohols, which afforded the desired enantiopure alcohols in more than 99% ee starting from the racemic mixture. The reaction time of deracemisation of 1-phenylethanol was estimated to be less than 30min. The stereoinversion of (S)-1-phenylethanol to its pure (R)-enantiomer was also achieved, which provided a biocatalytic alternative to the chemical Mitsunobu inversion reaction.
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