Formate Oxidase (FOx) from Aspergillus oryzae

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

Journal Article (2019)
Author(s)

Florian Tieves (TU Delft - Applied Sciences)

Sébastien Jean Paul Willot (TU Delft - Applied Sciences)

Morten Martinus Cornelis Harald van Schie (TU Delft - Applied Sciences)

Marine Charlène Renée Rauch (TU Delft - Applied Sciences)

Sabry Hamdy Hamed Younes (Sohag University, TU Delft - Applied Sciences)

Wuyuan Zhang (TU Delft - Applied Sciences)

Jia Jia Dong (TU Delft - Applied Sciences)

Patricia Gomez de Santos (TU Delft - Applied Sciences)

Frank Hollmann (TU Delft - Applied Sciences)

Research Group
BT/Biocatalysis
DOI related publication
https://doi.org/10.1002/anie.201902380 Final published version
More Info
expand_more
Publication Year
2019
Language
English
Research Group
BT/Biocatalysis
Issue number
23
Volume number
58
Pages (from-to)
7873-7877
Downloads counter
364
Collections
Institutional Repository
Reuse Rights

Other than for strictly personal use, it is not permitted to download, forward or distribute the text or part of it, without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license such as Creative Commons.

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.