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 - BT/Biocatalysis, Shijiazhuang Tiedao University)

Chiara Domestici (TU Delft - BT/Biocatalysis)

Yutong Wang (TU Delft - BT/Biocatalysis)

Thomas Hilberath (TU Delft - BT/Biocatalysis)

Ulf Hanefeld (TU Delft - BT/Biocatalysis)

Evgeny A. Pidko (TU Delft - ChemE/Inorganic Systems Engineering)

Frank Hollmann (TU Delft - BT/Biocatalysis)

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DOI related publication
https://doi.org/10.1038/s41467-026-68899-y Final published version
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Publication Year
2026
Language
English
Journal title
Nature Communications
Issue number
1
Volume number
17
Article number
2183
Downloads counter
29
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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.