biostudies-literatureScott CJRUKRI | Biotechnology and Biological Sciences Research CouncilUKRI | Engineering and Physical Sciences Research Council (EPSRC)European Research CouncilUKRI | Engineering and Physical Sciences Research CouncilRoyal Society Ken Murray Research ProfessorBiotechnology and Biological Sciences Research Councile0394323https://www.ebi.ac.uk/biostudies/studies/S-EPMC11218486biostudies-literatureUnknown12(7)<i>Parascedosporium putredinis</i> NO1 is a plant biomass-degrading ascomycete with a propensity to target the most recalcitrant components of lignocellulose. Here we applied proteomics and activity-based protein profiling (ABPP) to investigate the ability of <i>P. putredinis</i> NO1 to tailor its secretome for growth on different lignocellulosic substrates. Proteomic analysis of soluble and insoluble culture fractions following the growth of <i>P. putredinis</i> NO1 on six lignocellulosic substrates highlights the adaptability of the response of the <i>P. putredinis</i> NO1 secretome to different substrates. Differences in protein abundance profiles were maintained and observed across substrates after bioinformatic filtering of the data to remove intracellular protein contamination to ideMicrobiology spectrum<i>Parascedosporium putredinis</i> NO1 tailors its secretome for different lignocellulosic substrates.PMC11218486BB/P027717/1BB/W003309/1ERC-2020-SyG-951231EP/K039660/1, EP/M028127/1BB/M011151/1BB/W000695/1951231BB/P027717/1, BB/W000695/1, BB/W003309/1, BB/S01196X/1, BB/M011151/1McGregor NGSLeadbeater DRSetchfield AOverkleeft HSBruce NCAbood AScott CJRDowle AHoßbach JOates NCDavies GJfalse<i>Parascedosporium putredinis</i> NO1 tailors its secretome for different lignocellulosic substrates.<i>Parascedosporium putredinis</i> NO1 is a plant biomass-degrading ascomycete with a propensity to target the most recalcitrant components of lignocellulose. Here we applied proteomics and activity-based protein profiling (ABPP) to investigate the ability of <i>P. putredinis</i> NO1 to tailor its secretome for growth on different lignocellulosic substrates. Proteomic analysis of soluble and insoluble culture fractions following the growth of <i>P. putredinis</i> NO1 on six lignocellulosic substrates highlights the adaptability of the response of the <i>P. putredinis</i> NO1 secretome to different substrates. Differences in protein abundance profiles were maintained and observed across substrates after bioinformatic filtering of the data to remove intracellular protein contamination to ide2024-01-01T00:00:00Z2024 Jul2025-04-04T11:25:18.898Z2025-04-04T11:25:18.898ZS-EPMC112184863875798410.1128/spectrum.03943-23