| Literature DB >> 26915048 |
Cyntia M Palacio1, Ciprian G Crismaru1, Sebastian Bartsch1, Vaidotas Navickas2, Klaus Ditrich2, Michael Breuer2, Rohana Abu3, John M Woodley3, Kai Baldenius2, Bian Wu1, Dick B Janssen4.
Abstract
We constructed an enzymatic network composed of three different enzymes for the synthesis of valuable ether amines. The enzymatic reactions are interconnected to catalyze the oxidation and subsequent transamination of the substrate and to provide cofactor recycling. This allows production of the desired ether amines from the corresponding ether alcohols with inorganic ammonium as the only additional substrate. To examine conversion, individual and overall reaction equilibria were established. Using these data, it was found that the experimentally observed conversions of up to 60% observed for reactions containing 10 mM alcohol and up to 280 mM ammonia corresponded well to predicted conversions. The results indicate that efficient amination can be driven by high concentrations of ammonia and may require improving enzyme robustness for scale-up. Biotechnol. Bioeng. 2016;113: 1853-1861.Entities:
Keywords: alcohol dehydrogenase; amination; aminotransferase; biocatalysis; ether amines
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Year: 2016 PMID: 26915048 DOI: 10.1002/bit.25954
Source DB: PubMed Journal: Biotechnol Bioeng ISSN: 0006-3592 Impact factor: 4.530