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

Research output: Contribution to journalArticlepeer-review

  • External authors:
  • Ashley Philip Mattey
  • Fabio Parmeggiani
  • Ryan Williams
  • Helene Ledru
  • Andrea Marchesi
  • Lisa Seibt
  • Peter Both
  • Kun Huang
  • M. Carmen Galan
  • Jolanda Van Van Munster

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.

Bibliographical metadata

Original languageEnglish
JournalOrganic & biomolecular chemistry
DOIs
Publication statusPublished - 1 Jun 2021