Demonstrates a mutant alcohol oxidase enables transesterification in aqueous media, suggesting improved catalytic efficiency.
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.
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Wu et al. (2026) studied this question.
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