A Promiscuous Glycosyltransferase Generates Poly-Β-1,4-glucan Derivatives That Facilitate Mass Spectrometry-Based Detection of Cellulolytic Enzymes.

Promiscuous activity of a glycosyltransferase was exploited to polymerise glucose from UDP-glucose via the generation of beta-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.