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
TL;DR
Scientists engineered an enzyme that can perform a key chemical reaction in water without unwanted side reactions.
Contribution
A mutant alcohol oxidase was developed that enables transesterification in aqueous media without hydrolysis.
Findings
PcAOx-VPN mutant shows transesterification activity in water.
The enzyme lacks hydrolytic activity due to its hydrophobic active site.
This enzyme is promising for aqueous transesterification without competing hydrolysis.
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. Transesterification reactions are essential in organic chemistry, however, performing these reactions in aqueous media is challenging due to the competing hydrolysis reaction. Here, the authors report a mutant of alcohol oxidase from Phanerochaete…
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Taxonomy
TopicsEnzyme Catalysis and Immobilization · Enzyme-mediated dye degradation · Metal-Catalyzed Oxygenation Mechanisms