Activity-based protein profiling of xylan-degrading glycoside hydrolases in Aspergillus secretomes

ABSTRACT: Plant polysaccharides represent a virtually unlimited feedstock for the generation of biofuels and other commodities. However, the extraordinary recalcitrance of plant polysaccharides towards breakdown necessitates a continued search for enzymes that degrade these materials efficiently under defined conditions. Activity-based protein profiling (ABPP) 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 b-xylosidases and endo-xylanases in the secretome of Aspergillus niger, by the use of chemical probes inspired by the b-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.

INSTRUMENT(S): maXis

ORGANISM(S): Aspergillus Niger (ncbitaxon:5061)

SUBMITTER: Gideon J. Davies  

PROVIDER: MSV000083714 | MassIVE | Wed Apr 24 04:09:00 BST 2019

SECONDARY ACCESSION(S): PXD013618

REPOSITORIES: MassIVE