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Extracts were centrifuged at 4000 x g for 15 min at 4 °C. The supernatants were collected and heat-inactivated for 5 min at 95 °C, residual activity was checked using activity assay from chapter 2.6. Beer samples were degassed for 10 min at 40 Hz using ultrasonic bath and heat inactivated as well. Barley malt wort was produced using Weyermann Pilsner (Bamberg, Germany) malt extract which was diluted with bidest. water to obtain a wort of 12°P followed by autoclaving. Beer and wort samples were diluted 1:3 with 0.1 M ammonium acetate pH 4,5 containing 2 mM DTT prior to further extraction.  Incubation & peptide extraction  All matrices were obtained in triplicate and filtrated using 10 kDa spin-off columns (Millipore, Merck) at 12.000 x g for 15 min followed by buffer exchange to 0.1 M ammonium acetate pH 4,5 containing 1.5 M Urea, 2 mM DTT three times. Protein concentration using BCA-assay (Thermo Scientific No 23235, Micro BCA Protein Assay Kit) was conducted of the retentate. Following all matrixes were incubated with r-HvEPB in a ratio of 1:10 (µM protein concentration) at 42 °C for 24 h. Instead of r-HvEPB, bidest. H2O was added in equal volume as a reference. Samples were then heat inactivated (95 °C, 5 min) and 25 µl of each sample (in triplicate) was put on a 96 well filter plate (AcroPrep, Pall) with a cut-off of 10 kDa an centrifuged at 1500 x g for 30 min followed washing with 3 x 50 µl of 0.1 M ammonium acetate pH 4.5. Permeate was collected (“peptidome”) and vaccum dryed (45 °C) until complete dryness."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Peptidome and full proteome analyses using liquid chromatography based tandem mass spectrometry (LC-MS/MS) LC-MS/MS data acquisition of “peptidome” und “full proteome” samples was carried out on a Dionex Ultimate 3000 RSLCnano system coupled to an Orbitrap Fusion LUMOS mass spectrometer (ThermoFisher Scientific, Bremen). Injected peptides were delivered to a trap column (ReproSil-pur C18-AQ, 5 μm, Dr. Maisch, 20 mm × 75 μm, self-packed) at a flow rate of 5 μL/min in 0.1% formic acid in HPLC grade water. After 10 minutes of loading, peptides were transferred to an analytical column (ReproSil Gold C18-AQ, 3 μm, Dr. Maisch, 450 mm × 75 μm, self-packed) for one minute, and then separated using a 50 min gradient from 4% to 32% of solvent B (0.1% FA, 5% DMSO in acetonitrile) in solvent A (0.1% FA, 5% DMSO in HPLC grade water) at 300 nL/min flow rate. The Orbitrap Fusion LUMOS mass spectrometer was operated in data-dependent acquisition (DDA) and positive ionization mode. MS1 spectra (360–1300 m/z) were recorded at a resolution of 60k using a normalized automatic gain control (AGC) target value of 100% and a maximum injection time (maxIT) of 50 msec. A cycle time of 2 sec was set. Only precursors with charge states 2 to 6 were selected, and dynamic exclusion of 30 sec was enabled. Peptide fragmentation was performed using higher energy collision-induced dissociation (HCD) and a normalized collision energy (NCE) of 30%. The precursor isolation window width was set to 1.3 m/z. MS2 Resolution was 15k with a normalized automatic gain control (AGC) target value of 150% and maximum injection time (maxIT) of 22 msec. For peptidome analysis, all raw data were searched using FragPipe (v23.0) (MSFragger v4.2, IonQuant version 1.11.9) against the Hordeum vulgare subsp. vulgare (Domesticated barley) reference proteome from Uniprot (UP000011116, 35,907 protein entries, downloaded April 2025), appended with eight additional protein sequences from hordein proteins not covered in the barley reference proteome (P06470 B1-hordein, P06471 B3-hordein, I6TEV5 B3-hordein, Q41210 C-hordein, P80198 Gamma-hordein-3, P17990 Gamma-hordein-1  Q84LE9 D-Hordein, F2EGD5 Predicted protein). Within FragPipe, the “Nonspecific-peptidome” workflow was used, keeping all parameters default, including for example: Enzyme cleavage “nonspecific”; peptide length 7–65 amino acids; mass range 500–12000 Da; fixed modification: carbamidomethylation (C); variable modifications: oxidation (M), N-terminal acetylation, water loss on n-terminal glutamic acid, N-terminal glutamine cyclization, C-terminal amidation; allowing up to three modifications per peptide; rescoring using MSBooster.  The ”combined_peptide.tsv” results table was further processed using the in-house data visualisation platform omicsViewer (DOI: 10.1101/2022.03.10.483845), which included filtering for peptides detected in all three technical replicates of as least one “condition”, imputation of missing values by random distribution (width: 0.3, downshift 1.8), and determination of differential peptide abundance between EPB treated and untreated samples through Student t-test. The resulting p-values were adjusted by the Benjamini-Hochberg algorithm to control the false discovery rate. Only peptides with a fold change of ≥ 10 and an FDR-adjusted p-value < 0.01 were considered significant and used for cleavage motif analysis.   For the full proteome analysis of r-HvEPB (for purity check) and the four distinct technologically relevant matrices (raw barley, malt, wort and beer) protein detection were performed using the software MaxQuant (version 1.6.3.4). The r-HvEPB raw file was searched against the protein database from Komagataella phaffii (UP000000314, 5073 protein entries, downloaded July 2025) appended with the overexpressed r-HvEPB protein sequence. The mass spectrometric raw files from the four matrices samples were searched against the Hordeum vulgare subsp. vulgare (Domesticated barley) reference proteome from Uniprot (UP000011116, 35,907 protein entries, downloaded April 2025). In both searches, Trypsin/P was specified as proteolytic enzyme, carbamidomethylated cysteine was set as fixed modification, oxidation of methionine and acetylation at the protein N‐terminus was specified as variable modifications. Results were adjusted to 1% false discovery rate on peptide spectrum match (PSM) level and protein level employing a target‐decoy approach using reversed protein sequences. The minimal peptide length was defined as 7 amino acids and the “match-between-runs” functionality was disabled. Estimations of protein mass fractions were carried out using the “intensity-based absolute quantification” (iBAQ) function implemented in MaxQuant. By dividing the iBAQ value of a given protein through the summed iBAQ values of all proteins detected in a given sample “protein mass fractions” were calculated."],"omics_type":["Proteomics"],"labhead":["Christina Ludwig"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS) Technical University of Munich (TUM) Gregor-Mendel-Stasse 4 85354 Freising"],"species":["Hordeum Vulgare Subsp. Vulgare","Komagataella Phaffii"],"publication":["42034091 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. 2026 516:149314 10.1016/j.foodchem.2026.149314"],"submitter_mail":["tina.ludwig@tum.de"],"submitter_affiliation":["TU Munich"],"submitter_country":["Germany"],"pubmed_abstract":["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."],"pubmed_title":["Characterising peptidase activity of barley endoprotease B in complex technical matrices of the brewing process."],"pubmed_authors":["Kerpes Roland R, Ludwig Christina C, Dionisio Giuseppe G, Brinch-Pedersen Henrik H, Becker Thomas T"],"additional_accession":[]},"is_claimable":false,"name":"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. 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