Abstract
The reduction of acetophenone to ( R)-phenylethanol catalysed by the alcohol dehydrogenase from Lactobacillus brevis in combination with electrochemical regeneration of NADPH mediated by a rhodium complex is reported. The reaction in buffer solution was optimised with regard to high productivity (up to 14 gL −1d −1) and enantioselectivity (>99.9%). Enzyme stability under the reaction conditions was increased either by addition of bovine serum albumin as a sacrificial protein or by immobilisation, leading to full conversion and enzyme ttn’s of up to 75,000. To improve the utilisation of cofactor and mediator as well as to broaden the substrate spectrum to more hydrophobic substrates, we introduced an organic phase of methyl tert-butyl ether. This is the first reported two-phase approach for electrochemical cofactor regeneration, which yielded mediator and cofactor ttn’s twice as high as in the one-phase approach. Furthermore, a concentrated product solution of 180 mM enantiopure ( R)-phenylethanol was obtained, facilitating product work-up.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call