Engineered alcohol oxidases catalyse transesterification in aqueous media without competing hydrolysis.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 41617720.
- Also identified by DOI 10.1038/s41467-026-68899-y and PMC identifier 12960964.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Alcohol Oxidoreductases
- Phanerochaete
- Fungal Proteins