Enzymatic network for production of ether amines from alcohols.

Autor: Palacio CM; Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Nijenborgh 4, Groningen, 9747AG, The Netherlands., Crismaru CG; Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Nijenborgh 4, Groningen, 9747AG, The Netherlands., Bartsch S; Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Nijenborgh 4, Groningen, 9747AG, The Netherlands., Navickas V; White Biotechnology Research, BASF SE, Ludwigshafen, Germany., Ditrich K; White Biotechnology Research, BASF SE, Ludwigshafen, Germany., Breuer M; White Biotechnology Research, BASF SE, Ludwigshafen, Germany., Abu R; Department of Chemical and Biochemical Engineering, Technical University of Denmark, Lyngby, Denmark., Woodley JM; Department of Chemical and Biochemical Engineering, Technical University of Denmark, Lyngby, Denmark., Baldenius K; White Biotechnology Research, BASF SE, Ludwigshafen, Germany., Wu B; Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Nijenborgh 4, Groningen, 9747AG, The Netherlands., Janssen DB; Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Nijenborgh 4, Groningen, 9747AG, The Netherlands. d.b.janssen@rug.nl.
Jazyk: angličtina
Zdroj: Biotechnology and bioengineering [Biotechnol Bioeng] 2016 Sep; Vol. 113 (9), pp. 1853-61. Date of Electronic Publication: 2016 Mar 09.
DOI: 10.1002/bit.25954
Abstrakt: 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. © 2016 Wiley Periodicals, Inc.
(© 2016 Wiley Periodicals, Inc.)
Databáze: MEDLINE
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