Formate Oxidase (FOx) from Aspergillus oryzae
One Catalyst Enables Diverse H 2 O 2 -Dependent Biocatalytic Oxidation Reactions
F. Tieves (TU Delft - BT/Biocatalysis)
S.J. Willot (TU Delft - BT/Biocatalysis)
M. M.C.H. Van Schie (TU Delft - BT/Biocatalysis)
Marine Rauch (TU Delft - BT/Biocatalysis)
Sabry H H Younes (Sohag University, TU Delft - BT/Biocatalysis)
Wuyuan Zhang (TU Delft - BT/Biocatalysis)
J. Dong (TU Delft - BT/Biocatalysis)
Patricia Gomez de Santos (TU Delft - BT/Biocatalysis)
F. Hollmann (TU Delft - BT/Biocatalysis)
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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.
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