Dynamic and Functional Profiling of Xylan-Degrading Enzymes in Aspergillus Secretomes Using Activity-Based Probes

Sybrin P. Schröder, Casper De Boer, Nicholas G.S. McGregor, Rhianna J. Rowland, Olga Moroz, Elena Blagova, Jos Reijngoud, Mark Arentshorst, David Osborn, Marc D. Morant, Eric Abbate, Mary A. Stringer, Kristian B.R.M. Krogh, Lluís Raich, Carme Rovira, Jean Guy Berrin, Gilles P. Van Wezel, Arthur F.J. Ram, Bogdan I. Florea, Gijsbert A. Van Der MarelJeroen D.C. Codée, Keith S. Wilson, Liang Wu*, Gideon J. Davies, Herman S. Overkleeft

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Plant polysaccharides represent a virtually unlimited feedstock for the generation of biofuels and other commodities. However, the extraordinary recalcitrance of plant polysaccharides toward breakdown necessitates a continued search for enzymes that degrade these materials efficiently under defined conditions. Activity-based protein profiling provides a route for the functional discovery of such enzymes in complex mixtures and under industrially relevant conditions. Here, we show the detection and identification of β-xylosidases and endo-β-1,4-xylanases in the secretomes of Aspergillus niger, by the use of chemical probes inspired by the β-glucosidase inhibitor cyclophellitol. Furthermore, we demonstrate the use of these activity-based probes (ABPs) to assess enzyme-substrate specificities, thermal stabilities, and other biotechnologically relevant parameters. Our experiments highlight the utility of ABPs as promising tools for the discovery of relevant enzymes useful for biomass breakdown.

Original languageEnglish
Pages (from-to)1067-1078
Number of pages12
JournalACS Central Science
Issue number6
Early online date24 May 2019
Publication statusPublished - 26 Jun 2019

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© 2019 American Chemical Society.

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