4.6 Article

Overcoming Co-Product Inhibition in the Nicotinamide Independent Asymmetric Bioreduction of Activated C=C-Bonds Using Flavin- Dependent Ene-Reductases

Journal

BIOTECHNOLOGY AND BIOENGINEERING
Volume 110, Issue 12, Pages 3085-3092

Publisher

WILEY
DOI: 10.1002/bit.24981

Keywords

old yellow enzyme; ene-reductase; disproportionation; in situ co-product removal

Funding

  1. FWF (Vienna) [P22722]
  2. Austrian Science Fund (FWF) [P 22722] Funding Source: researchfish
  3. Austrian Science Fund (FWF) [P22722] Funding Source: Austrian Science Fund (FWF)

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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. (c) 2013 The Authors. Biotechnology and Bioengineering Published by Willey Periodicals, Inc.

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