Engineered alcohol oxidases catalyse transesterification in aqueous media without competing hydrolysis
- Bin Wu
- Yunjian Ma
- Chenhao Feng
- Limei Ren
- Chiara Domestici
- Yutong Wang
- Thomas Hilberath
- Ulf Hanefeld
- Evgeny A. Pidko
- Frank Hollmann
- Yonghua Wang
2026-01-30
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 ( Pc AOx-VPN) that also exhibits transesterification activity. Moreover, Pc AOx-VPN displays no detectable hydrolytic activity, owing to its hydrophobic active site, which effectively excludes water. These characteristics make Pc AOx-VPN a promising catalyst for transesterification reactions in aqueous media, a context that is typically compromised by competing hydrolysis.