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 106769
Title Vanillyl-alcohol oxidase, a tasteful biocatalyst
Author(s) Heuvel, R.H.H. van den; Fraaije, M.W.; Mattevi, A.; Laane, C.; Berkel, W.J.H. van
Source Journal of Molecular Catalysis. B, Enzymatic 11 (2001). - ISSN 1381-1177 - p. 185 - 188.
DOI https://doi.org/10.1016/S1381-1177(00)00062-X
Department(s) Biochemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2001
Abstract The covalent flavoenzyme vanillyl-alcohol oxidase (VAO) is a versatile biocatalyst. It converts a wide range of phenolic compounds by catalysing oxidation, deamination, demethylation, dehydrogenation and hydroxylation reactions. The production of natural vanillin, 4-hydroxybenzaldehyde, coniferyl alcohol and enantiomeric pure phenol derivatives is of interest for biotechnological applications. The hydroxylation of 4-alkylphenols is highly stereospecific for the (R)-isomer, whereas dehydrogenation of these substrates is specific for the cis- or trans-isomer. On the basis of crystallographic data, we suggest that the stereospecificity is related to the active site residue Asp170. Another important feature of VAO is the covalent flavin attachment. Studies from site-directed mutants suggest that the covalent flavin-protein interaction improves the catalytic performance as well as the long-term stability of VAO
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