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*

*Corresponding author for this work

Research output: Contribution to journalShort communication peer-review

Abstract

Promiscuous activity of a glycosyltransferase was exploited to polymerise glucose from UDP-glucoseviathe 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 date1 Jun 2021
DOIs
Publication statusFirst published - 1 Jun 2021

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