Engineered alcohol oxidases catalyse transesterification in aqueous media without competing hydrolysis
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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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.