ntributions NM, GJD, HSO, and JGB created and planned the study. MH prepared fungal cultures. CB and SS prepared activitybased probes utilized in this study. NM collected secretome samples and performed activitybased protein profil ing experiments. NM collected and analysed proteomic data. DN performed bioinformatic evaluation. NM and MS ready P. pastoris strains, produced and purified recombinant enzymes, and performed activity assays. NM wrote the manuscript with input from all of the authors. All authors study and authorized the final manuscript. Funding The authors thank the Natural Sciences and Engineering Research Council of Canada (PostDoctoral Fellowship to NGSM), the Royal Society (Ken Murray Study Professorship to GJD), the Biotechnology and Biological Sciences Research Council (BBSRC) (grant BB/R001162/1 to GJD), the French National Analysis Agency (ANR13BIME0002 to JGB), the Netherlands Organization for Scientific Investigation (NWO Top rated grant 2018714.018.002 to HSO), as well as the European Research Council (ERC2011AdG290836 “Chembiosphing” to HSO, ERC2020SyG951231 “Carbocentre” to GJD and HSO). Proteomics data had been collected at the York Centre of Excellence in Mass Spectrometry, which was created due to a major capital investment through Science City York, sup ported by Yorkshire Forward with funds from the Northern Way Initiative, and subsequent help from EPSRC (EP/K039660/1; EP/M028127/1). Availability of information and materials Pichia pastoris strains and samples of recombinant proteins could be readily available from Gideon Davies (Gideon.davies@york.ac.uk). Samples of ABPCel, ABPXyl, and ABPGlc might be offered from Herman Overkleeft (h.s.overkleeft@lic. leidenuniv.nl). Basidiomycete fungi are accessible in the fungal culture collection of the International Centre of Microbial Sources (CIRMCF) at the French National Institute for Agricultural study (INRA; Marseille, France). Genome sequences for each in the fungi utilized within this study are accessible from Mycocosm (mycocosm.jgi.doe.gov/mycocosm/home) (DOE Joint Genome Institute, Walnut Creek, California). Other datasets utilised and/or ana lysed for the duration of the present study are readily available from the corresponding author on reasonable request.Author specifics 1 York Structural Biology Laboratory, Division of Chemistry, The University of York, Heslington YO10 5DD, York, UK. two Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2300 RA Leiden, The Netherlands. 3 UMR1163 Bio diversitet Biotechnologie Fongiques, Facultdes Sciences de Luminy, INRAE, Aix Marseille Univ, 13288 Marseille, France. 4 Polytech Marseille, Aix Marseille Univ, 13288 Marseille, France. Received: eight October 2021 Accepted: six JanuaryDeclarationsEthics approval and consent to participate Not applicable. Consent for publication Not applicable. Competing interests The authors declare no competing interests.References 1. Scheller HV, Ulvskov P. ACAT2 web Hemicelluloses. Annu Rev Plant Biol. 2010;2(61):2639. 2. Luis AS, Briggs J, Zhang X, Farnell B, Ndeh D, Labourel A, et al. Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides. Nat Microbiol. 2018;three(two):210. three. Celiska E, Nicaud JM, Bialas W. Hydrolytic secretome engineering in Yarrowia ALK2 site lipolytica for consolidated bioprocessing on polysaccharide resources: evaluation on starch, cellulose, xylan, and inulin. Appl Microbiol Biotechnol. 2021;105(3):9759. 4. Schlembach I, Hosseinpour Tehrani H, Blank LM, B hs J, Wierckx N, Regestein L, et al. Consolidate