6yp1

Publication Abstract from PubMed

Cellulases and related beta-1,4-glucanases are essential components of lignocellulose-degrading enzyme mixtures. The detection of beta-1,4-glucanase activity typically relies on monitoring the breakdown of purified lignocellulose-derived substrates or synthetic chromogenic substrates, limiting the activities which can be detected and complicating the tracing of activity back to specific components within complex enzyme mixtures. As a tool for the rapid detection and identification of beta-1,4-glucanases, a series of glycosylated cyclophellitol inhibitors mimicking beta-1,4-glucan oligosaccharides have been synthesised. These compounds are highly efficient inhibitors of HiCel7B, a well-known GH7 endo-beta-1,4-glucanase. An elaborated activity-based probe facilitated the direct detection and identification of beta-1,4-glucanases within a complex fungal secretome without any detectable cross-reactivity with beta-d-glucosidases. These probes and inhibitors add valuable new capacity to the growing toolbox of cyclophellitol-derived probes for the activity-based profiling of biomass-degrading enzymes.

Glycosylated cyclophellitol-derived activity-based probes and inhibitors for cellulases.,de Boer C, McGregor NGS, Peterse E, Schroder SP, Florea BI, Jiang J, Reijngoud J, Ram AFJ, van Wezel GP, van der Marel GA, Codee JDC, Overkleeft HS, Davies GJ RSC Chem Biol. 2020 Jul 28;1(3):148-155. doi: 10.1039/d0cb00045k. eCollection, 2020 Aug 1. PMID:34458755^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.