Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-6000
Main Title: Enzyme-modified particles for selective biocatalytic hydrogenation by hydrogen-driven NADH recycling
Author(s): Reeve, Holly A.
Lauterbach, Lars
Lenz, Oliver
Vincent, Kylie A.
Type: Article
Language Code: en
Abstract: We describe a new approach to selective H-2-driven hydrogenation that exploits a sequence of enzymes immobilised on carbon particles. We used a catalyst system that comprised alcohol dehydrogenase, hydrogenase and an NAD(+) reductase on carbon black to demonstrate a greater than 98% conversion of acetophenone to phenylethanol. Oxidation of H-2 by the hydrogenase provides electrons through the carbon for NAD(+) reduction to recycle the NADH cofactor required by the alcohol dehydrogenase. This biocatalytic system operates over the pH range 6-8 or in un-buffered water, and can function at low concentrations of the cofactor (10m NAD(+)) and at H-2 partial pressures below 1bar. Total turnover numbers >130000 during acetophenone reduction indicate high enzyme stability, and the immobilised enzymes can be recovered by a simple centrifugation step and re-used several times. This offers a route to convenient, atom-efficient operation of NADH-dependent oxidoreductases for selective hydrogenation catalysis.
URI: http://depositonce.tu-berlin.de/handle/11303/6492
http://dx.doi.org/10.14279/depositonce-6000
Issue Date: 2015
Date Available: 14-Jul-2017
DDC Class: 540 Chemie
Subject(s): biocatalysis
biotransformations
enzyme catalysis
hydrogenation
heterogeneous catalysis
Sponsor/Funder: EC/FP7/258600/EU/Understanding and Exploiting Biological Catalysts for Energy Cycling: Development of Infrared Spectroelectrochemistry for Studying Intermediates in Metalloenzyme Catalysis/EnergyBioCatalysis
EC/FP7/297503/EU/Modular beads for regeneration of bio-cofactors in enzyme-catalysed synthesis/HydRegen
DFG, EXC 314, Unifying Concepts in Catalysis
Creative Commons License: https://creativecommons.org/licenses/by-nc/4.0/
Journal Title: ChemCatChem
Publisher: Wiley-VCH
Publisher Place: Weinheim
Volume: 7
Issue: 21
Publisher DOI: 10.1002/cctc.201500766
Page Start: 3480
Page End: 3487
EISSN: 1867-3899
ISSN: 1867-3880
Appears in Collections:Technische Universität Berlin » Fakultäten & Zentralinstitute » Fakultät 2 Mathematik und Naturwissenschaften » Institut für Chemie » Fachgebiet Physikalische Chemie / Biophysikalische Chemie » Publications

Files in This Item:
File Description SizeFormat 
10.1002.cctc.201500766.pdf1.3 MBAdobe PDFThumbnail
View/Open


Items in DepositOnce are protected by copyright, with all rights reserved, unless otherwise indicated.