Issue 25, 2021

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

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
19 May 2021
Accepted
26 May 2021
First published
01 Jun 2021
This article is Open Access
Creative Commons BY license

Org. Biomol. Chem., 2021,19, 5529-5533

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

G. S. Bulmer, A. P. Mattey, F. Parmeggiani, R. Williams, H. Ledru, A. Marchesi, L. S. Seibt, P. Both, K. Huang, M. C. Galan, S. L. Flitsch, A. P. Green and J. M. van Munster, Org. Biomol. Chem., 2021, 19, 5529 DOI: 10.1039/D1OB00971K

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