PXD061695-1

PXD061695 is an original dataset announced via ProteomeXchange.

Title	Genomic and Secretomic analysis 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, 30_7, and 67, with putative roles in xylan degradation. We also report on the heterologous expression and functional characterization of the GH30_7 xylanase BmXyn30A from B. mokoenaii, which exhibits both glucoronoxylanase and xylobiohydrolase activities. Distinct differences were observed in the xylooligosaccharide profiles generated by BmXyn30A compared to the previously characterized GH11 xylanase BmXyn11A. Furthermore, we demonstrate the synergistic effects between BmXyn30A and BmXyn11A during the hydrolysis of beechwood glucuronoxylan, where the enzymes exhibited complementary roles that enhanced the deconstruction of this complex hemicellulose substrate. These findings broaden our understanding of the xylanolytic systems in yeasts and underscore the potential of Blastobotrys species as cell factories and natural xylanase producers. The enzymes they produce hold promise for biorefining applications, enabling efficient utilization of renewable, xylan-rich plant biomass resources.
HostingRepository	PRIDE
AnnounceDate	2025-08-25
AnnouncementXML	Submission_2025-08-24_16:37:55.935.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Proteomics Core Facility
SpeciesList	scientific name: Blastobotrys; NCBI TaxID: 43971;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2025-03-11 05:33:17	ID requested
⏵ 1	2025-08-24 16:37:56	announced

Ravn J, Ristinmaa AS, Mazurkewich S, Dias GB, Larsbrink J, Geijer C, Genomic and secretomic analyses of Blastobotrys yeasts reveal key xylanases for biomass decomposition. Appl Microbiol Biotechnol, 109(1):175(2025) [pubmed]

10.1007/s00253-025-13556-5;

submitter keyword: GH11, xylan, GH30,Xylanolytic yeast

Jonas Ravn
contact affiliation	Department of Life Sciences, Chalmers University of Technology, 412 96, Gothenburg, Sweden
contact email	ravn@chalmers.se
lab head
Proteomics Core Facility
contact affiliation	SAMBIO Core Facilities, Sahgrenska Academy, University of Gothenburg
contact email	gupcf@outlook.com
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/08/PXD061695

PRIDE project URI

• PRIDE
  1. PXD061695
     1. Label: PRIDE project
     2. Name: Genomic and Secretomic analysis of Blastobotrys yeasts reveal key xylanases for biomass decomposition