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ntributions NM, GJD, HSO, and JGB designed and planned the study. MH prepared fungal cultures. CB and SS prepared activitybased probes employed in this study. NM collected secretome samples and performed activitybased protein profil ing experiments. NM collected and analysed proteomic data. DN performed bioinformatic analysis. NM and MS ready P. pastoris strains, produced and purified recombinant enzymes, and performed activity assays. NM wrote the manuscript with input from all the authors. All authors read and approved the final manuscript. Funding The authors thank the All-natural Sciences and Engineering Study Council of Canada (PostDoctoral Fellowship to NGSM), the Royal Society (Ken Murray Investigation Professorship to GJD), the Biotechnology and Biological Sciences Research Council (BBSRC) (grant BB/R001162/1 to GJD), the French National Investigation Agency (ANR13BIME0002 to JGB), the Netherlands Organization for Scientific Analysis (NWO Leading grant 2018714.018.002 to HSO), and also the European Analysis Council (ERC2011AdG290836 “Chembiosphing” to HSO, ERC2020SyG951231 “Carbocentre” to GJD and HSO). Proteomics data were collected in the York Centre of Excellence in Mass Spectrometry, which was designed thanks to a major capital investment through Science City York, sup ported by Yorkshire Forward with funds in the Northern Way Initiative, and subsequent assistance from EPSRC (EP/K039660/1; EP/M028127/1). Availability of information and components Pichia pastoris strains and samples of recombinant proteins could be available from Gideon Davies ([email protected]). Samples of ABPCel, ABPXyl, and ABPGlc could be available from Herman Overkleeft (h.s.overkleeft@lic. leidenuniv.nl). Basidiomycete fungi are accessible in the fungal culture collection from the International Centre of Microbial Resources (CIRMCF) at the French National Institute for Agricultural analysis (INRA; Marseille, France). Genome sequences for each and every of the fungi employed within this study are readily available from Mycocosm (mycocosm.jgi.doe.gov/mycocosm/home) (DOE Joint Genome Institute, Walnut Creek, California). Other datasets applied and/or ana lysed through the current study are offered in the corresponding author on affordable request.Author facts 1 York Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington YO10 5DD, York, UK. 2 Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2300 RA Leiden, The Netherlands. three UMR1163 Bio diversitet Biotechnologie Fongiques, Facultdes Sciences de Luminy, INRAE, Aix Marseille Univ, 13288 Marseille, France. four Polytech Marseille, Aix Marseille Univ, 13288 Marseille, France. Received: 8 October 2021 Accepted: six JanuaryDeclarationsEthics approval and consent to participate Not Adenosine A1 receptor (A1R) Purity & Documentation applicable. Consent for publication Not applicable. Competing interests The authors declare no competing interests.References 1. Scheller HV, Ulvskov P. Hemicelluloses. Annu Rev Plant Biol. 2010;two(61):2639. 2. Luis AS, Briggs J, Zhang X, Farnell B, Ndeh D, Labourel A, et al. Dietary pectic glycans are degraded by coordinated BRDT custom synthesis enzyme pathways in human colonic Bacteroides. Nat Microbiol. 2018;three(two):210. three. Celiska E, Nicaud JM, Bialas W. Hydrolytic secretome engineering in Yarrowia lipolytica for consolidated bioprocessing on polysaccharide sources: overview on starch, cellulose, xylan, and inulin. Appl Microbiol Biotechnol. 2021;105(three):9759. 4. Schlembach I, Hosseinpour Tehrani H, Blank LM, B hs J, Wierckx N, Regestein L, et al. Consolidate

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