Engineered alcohol oxidases catalyse transesterification in aqueous media without competing hydrolysis

Journal Article (2026)
Author(s)

Bin Wu (South China University of Technology)

Yunjian Ma (South China University of Technology)

Limei Ren (TU Delft - Applied Sciences, Shijiazhuang Tiedao University)

Chiara Domestici (TU Delft - Applied Sciences)

Yutong Wang (TU Delft - Applied Sciences)

Thomas Hilberath (TU Delft - Applied Sciences)

Ulf Hanefeld (TU Delft - Applied Sciences)

Evgeny A. Pidko (TU Delft - Applied Sciences)

Frank Hollmann (TU Delft - Applied Sciences)

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Research Group
BT/Biocatalysis
DOI related publication
https://doi.org/10.1038/s41467-026-68899-y Final published version
More Info
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Publication Year
2026
Language
English
Research Group
BT/Biocatalysis
Journal title
Nature Communications
Issue number
1
Volume number
17
Article number
2183
Downloads counter
37
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Abstract

Transesterification reactions are fundamental transformations in organic chemistry, yet performing them in aqueous media is challenging because of the competing hydrolysis reaction. In this study, we describe a mutant of alcohol oxidase from Phanerochaete chrysosporium (PcAOx-VPN) that also exhibits transesterification activity. Moreover, PcAOx-VPN displays no detectable hydrolytic activity, owing to its hydrophobic active site, which effectively excludes water. These characteristics make PcAOx-VPN a promising catalyst for transesterification reactions in aqueous media, a context that is typically compromised by competing hydrolysis.