Abstract
Continuous operation of alcohol dehydrogenase (ADH) catalysed enantioselective reduction in a biphasic sytem showed gains in productivity and stability of the overall reaction system. The total turnover numbers obtained for the cofactor NADP + are high with up to 1.5× 10 4. Productivity for (R)-2-butanol with Lactobacillus brevis ADH was up to 26 kmol (mol enzyme) -1. Enantioselectivity was greater than 0.99 for (R)-phenylethanol and up to 0.99 for (R)-butanol. © Müller et al.
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CITATION STYLE
Müller, P., Bangasser, B. L., Greiner, L., Na’amnieh, S., Bäuerlein, P. S., Vogt, D., & Müller, C. (2011). Stable continuous operation of a biphasic enantioselective enzymatic reduction. Open Catalysis Journal, 4(1), 113–116. https://doi.org/10.2174/1876214X01104010113
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