Overcoming co‐product inhibition in the nicotinamide independent asymmetric bioreduction of activated CC‐bonds using flavin‐dependent ene‐reductases |
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Authors: | Christoph K Winkler Dorina Clay Esta van Heerden Kurt Faber |
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Institution: | 1. Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, , A‐8010 Graz, Austria;2. Department of Microbial, Biochemical and Food Biotechnology, University of the Free State, , 9300 Bloemfontein, South Africa |
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Abstract: | Eleven flavoproteins from the old yellow enzyme family were found to catalyze the disproportionation (“dismutation”) of conjugated enones. Incomplete conversions, which were attributed to enzyme inhibition by the co‐product phenol could be circumvented via in situ co‐product removal by scavenging the phenol using the polymeric adsorbent MP‐carbonate. The optimized system allowed to reduce an alkene activated by ester groups in a “coupled‐substrate” approach via nicotinamide‐free hydrogen transfer with >90% conversion and complete stereoselectivity. Biotechnol. Bioeng. 2013;110: 3085–3092. © 2013 The Authors. Biotechnology and Bioengineering Published by Willey Periodicals, Inc. |
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Keywords: | old yellow enzyme ene‐reductase disproportionation in situ co‐product removal |
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