Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 490678
Title Complete enzymatic oxidation of methanol to carbon dioxide: towards more eco-efficient regeneration systems for reduced nicotinamide cofactors
Author(s) Kara, S.; Schrittwieser, J.H.; Gargiulo, S.; Ni, Y.; Yanase, H.; Opperman, D.J.; Berkel, W.J.H. van; Hollmann, F.
Source Advanced Synthesis and Catalysis 357 (2015)8. - ISSN 1615-4150 - p. 1687 - 1691.
DOI https://doi.org/10.1002/adsc.201500173
Department(s) VLAG
Biochemistry
Publication type Refereed Article in a scientific journal
Publication year 2015
Keyword(s) pseudomonas-putida f61 - formaldehyde dismutase - biocatalysis - reductions - aldehydes - reductase
Abstract A novel system for in situ regeneration of reduced nicotinamide cofactors (NADH) is proposed: through a cascade of alcohol dehydrogenase (ADH), formaldehyde dismutase (FDM) and formate dehydrogenase (FDH) complete oxidation of methanol to carbon dioxide (CO2) is coupled to the regeneration of NADH. As a consequence, from one equivalent of methanol three equivalents of NADH can be obtained. The feasibility of this cascade is demonstrated at the examples of an NADH-dependent reduction of conjugated C[DOUBLE BOND]C-double bonds (catalysed by an enoate reductase) and the NADH-dependent hydroxylation of phenols (catalysed by a monooxygenase). The major limitation of the current regeneration system is the comparably poor catalytic efficiency of the methanol oxidation step (low kcat and high KM value of the ADH used) necessitating higher than theoretical methanol concentrations.
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