{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ravn J"],"funding":["Horizon 2020","Novo Nordisk Fonden","Chalmers University of Technology"],"pagination":["175"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12316802"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["109(1)"],"pubmed_abstract":["Xylanolytic enzyme systems in ascomycetous yeasts remain underexplored, despite the presence of yeasts in various xylan-rich ecological niches. In this study, we investigated the secreted xylanolytic machineries of three Blastobotrys species-B. mokoenaii, B. illinoisensis, and B. malaysiensis-by integrating genome annotation, bioinformatics, and secretome analyses of cultures grown on beechwood glucuronoxylan. Our findings demonstrate that these yeasts effectively hydrolyze xylan through the secretion of xylanases from the glycoside hydrolase (GH) family 11, which play a central role in cleaving the xylan backbone. Additionally, the yeasts produce a diverse array of other CAZymes, including members of GH families 3, 5, and 67, with putative roles in xylan degradation. We also report on the"],"journal":["Applied microbiology and biotechnology"],"pubmed_title":["Genomic and secretomic analyses of Blastobotrys yeasts reveal key xylanases for biomass decomposition."],"pmcid":["PMC12316802"],"funding_grant_id":["NNF22OC0079899","964430"],"pubmed_authors":["Ristinmaa AS","Dias GB","Geijer C","Larsbrink J","Ravn J","Mazurkewich S"],"additional_accession":[]},"is_claimable":false,"name":"Genomic and secretomic analyses of Blastobotrys yeasts reveal key xylanases for biomass decomposition.","description":"Xylanolytic enzyme systems in ascomycetous yeasts remain underexplored, despite the presence of yeasts in various xylan-rich ecological niches. In this study, we investigated the secreted xylanolytic machineries of three Blastobotrys species-B. mokoenaii, B. illinoisensis, and B. malaysiensis-by integrating genome annotation, bioinformatics, and secretome analyses of cultures grown on beechwood glucuronoxylan. Our findings demonstrate that these yeasts effectively hydrolyze xylan through the secretion of xylanases from the glycoside hydrolase (GH) family 11, which play a central role in cleaving the xylan backbone. Additionally, the yeasts produce a diverse array of other CAZymes, including members of GH families 3, 5, and 67, with putative roles in xylan degradation. We also report on the","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-06-08T06:51:38.705Z","creation":"2025-08-13T03:06:41.525Z"},"accession":"S-EPMC12316802","cross_references":{"pubmed":["40748385"],"doi":["10.1007/s00253-025-13556-5"]}}