Engineered alcohol oxidases catalyse transesterification in aqueous media without competing hydrolysis
Abstract
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 ( 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.
Article Details
Authors (11)
Bin Wu
Yunjian Ma
Chenhao Feng
Limei Ren
Chiara Domestici
Yutong Wang
Thomas Hilberath
Ulf Hanefeld
Evgeny A. Pidko
Inorganic Systems Engineering Group, Department of Chemical Engineering, Faculty of Applied Sciences, Delft University of Technology, Van der Maasweg 9, Delft 2629 HZ, The Netherlands
Frank Hollmann
Yonghua Wang