A promiscuous glycosyltransferase generates poly-β-1,4-glucan derivatives that facilitate mass spectrometry-based detection of cellulolytic enzymes

Gregory S Bulmer, Ashley P Mattey, Fabio Parmeggiani, Ryan Williams, Helene Ledru, Andrea Marchesi, Lisa S Seibt, Peter Both, Kun Huang, M Carmen Galan, Sabine L Flitsch, Anthony P Green, Jolanda M van Munster

Research output: Contribution to journalArticle (Academic Journal)peer-review

Abstract

Promiscuous activity of a glycosyltransferase was exploited to polymerise glucose from UDP-glucose via the generation of β-1,4-glycosidic linkages. The biocatalyst was incorporated into biocatalytic cascades and chemo-enzymatic strategies to synthesise cello-oligosaccharides with tailored functionalities on a scale suitable for employment in mass spectrometry-based assays. The resulting glycan structures enabled reporting of the activity and selectivity of celluloltic enzymes.

Original languageEnglish
Pages (from-to)5529-5533
Number of pages5
JournalOrganic and Biomolecular Chemistry
Volume19
Issue number25
Early online date8 Jun 2021
DOIs
Publication statusPublished - 7 Jul 2021

Bibliographical note

Publisher Copyright:
© The Royal Society of Chemistry 2021.

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