Formate Oxidase (FOx) from Aspergillus oryzae

One Catalyst Enables Diverse H 2 O 2 -Dependent Biocatalytic Oxidation Reactions

Journal article (2019)

Authors

F. Tieves BT/Biocatalysis - AS
S.J. Willot BT/Biocatalysis - AS
M.M.C.H. van Schie BT/Biocatalysis - AS
M.C.R. Rauch BT/Biocatalysis - AS
S.H.H. Younes Sohag University, BT/Biocatalysis - AS
W. Zhang BT/Biocatalysis - AS
J. Dong BT/Biocatalysis - AS
P. Gomez de Santos BT/Biocatalysis - AS
F. Hollmann BT/Biocatalysis - AS
Research Group
BT/Biocatalysis (AS) (TU Delft)
Copyright: © 2019 F. Tieves, S.J. Willot, M.M.C.H. van Schie, M.C.R. Rauch, S.H.H. Younes, W. Zhang, J. Dong, P. Gomez de Santos, F. Hollmann
DOI: https://doi.org/10.1002/anie.201902380
More Info
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Published Date

2019

Language

English

Faculty

Applied Sciences

Department

BT/Biotechnologie

Research Group

BT/Biocatalysis

Abstract


An increasing number of biocatalytic oxidation reactions rely on H
2
O
2
as a clean oxidant. The poor robustness of most enzymes towards H
2
O
2
, however, necessitates more efficient systems for in situ H
2
O
2
generation. In analogy to the well-known formate dehydrogenase to promote NADH-dependent reactions, we here propose employing formate oxidase (FOx) to promote H
2
O
2
-dependent enzymatic oxidation reactions. Even under non-optimised conditions, high turnover numbers for coupled FOx/peroxygenase catalysis were achieved.