PXD067323 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Characterizing Peptidase Activity of Barley Endoprotease B in Complex Technical Matrices of the Beer Brewing Process |
| Description | Barley cysteine endoprotease B (HvEPB) is an important enzyme in plant biology and food production. Pilot-scale fed-batch fermentation with Komagataella phaffii in minimal FM22 medium enabled controlled recombinant HvEPB (r-HvEPB) secretion. Peptidomics across four technological brewing matrices - raw barley, malt, wort and beer - revealed hydrophobic P2 preference (V, L, Y) and heterogeneous P1 selection (T, Q, G), with certain residues disfavoured (S, A, G at P2; P, I, L at P1). Cleavage motifs shifted depending on the underlying matrix, primarily reflecting differences in substrates properties and availability. Immunogenic gluten peptides, particularly from C- and B-hordeins, were efficiently cleaved. Enzyme-linked immunosorbent assay confirmed 85-89% gluten reduction across all four matrices under controlled in vitro incubation. r-HvEPB hydrolysed brewing-relevant hordeins, α/β-amylases, while LTP I and serpin Z4 were less cleaved. Weighted motif analysis and inhibition trials underscored HvEPB's pivotal role as a broad-specificity endoprotease in malt-based systems, with r-HvEPB showing significantly higher gluten hydrolysis than endogenous malt proteases. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-07-28 |
| AnnouncementXML | Submission_2026-07-28_05:48:31.254.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Christina Ludwig |
| SpeciesList | scientific name: Komagataella phaffii; NCBI TaxID: NEWT:460519; scientific name: Hordeum vulgare subsp. vulgare; NCBI TaxID: NEWT:112509; |
| ModificationList | iodoacetamide derivatized residue |
| Instrument | Orbitrap Fusion Lumos |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|
| 0 | 2025-08-13 14:29:15 | ID requested | |
| ⏵ 1 | 2026-07-28 05:48:32 | announced | |
Publication List
| 10.1016/j.foodchem.2026.149314; |
| Kerpes R, Ludwig C, Dionisio G, Brinch-Pedersen H, Becker T, Characterising peptidase activity of barley endoprotease B in complex technical matrices of the brewing process. Food Chem, 516():149314(2026) [pubmed] |
Keyword List
| submitter keyword: beer,Endoprotease B, EPB, proteolysis, peptidases, gluten |
Contact List
| Christina Ludwig |
|---|
| contact affiliation | Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS) Technical University of Munich (TUM) Gregor-Mendel-Stasse 4 85354 Freising |
| contact email | tina.ludwig@tum.de |
| lab head | |
| Christina Ludwig |
|---|
| contact affiliation | TU Munich |
| contact email | tina.ludwig@tum.de |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
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| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD067323
- Label: PRIDE project
- Name: Characterizing Peptidase Activity of Barley Endoprotease B in Complex Technical Matrices of the Beer Brewing Process
