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Proteins were reduced and alkylated in freshly prepared lysis buffer containing 1 % sodium deoxycholate (SDC), 10 mM tris(2-carboxyethyl) phosphinehydrochloride (TCEP) as a reducing agent, 40 mM chloroacetamide (CAA) as alkylating agent, and 100 mM TRIS, pH 8.0 supplemented with EDTA-free protease inhibitor (cOmplete Mini, Roche Diagnostics) as described previously (Post et al., 2017). Extracts were heated at 95 °C for 5 min, sonicated with a Bioruptor Plus (Diagenode) for 15 min with 50 % duty of 15 cycles. Next, denatured, reduced, and alkylated samples were diluted in SDC lysis buffer to a final concentration of proteins of 1 µg µl-1. Lys-C (Wako, Japan) was added for digestion at an enzyme:protein ratio of 1:75 and incubated for 4 h at 37 °C, followed by trypsin (Sigma) at an enzyme:protein ratio of 1:75 and incubated overnight at 37 °C. Then, samples were acidified with a 2 % final concentration of formic acid (FA) and SDC was precipitated, followed by centrifugation at 20,000 g for 20 min at 4 °C.  Digested peptides were purified using reverse-phase Sep-Pak 1cc (50 mg) tC18 cartridges (Waters, Ireland). Columns were activated with 100 % acetonitrile (ACN) and equilibrated with 0.1 % FA in water (loading buffer). Samples were diluted to pH<3 with loading buffer and applied to the column with one additional reload of the column flowthrough. tC18 cartridges were washed once with loading buffer, and peptides were eluted twice with 300 μl 80 % ACN in 0.1 % FA. The eluates were subsequently combined and dried by vacuum centrifugation and stored at -80 °C until subjected to nLC-MS analysis. Peptides were reconstituted in 2 % FA and analysed in triplicate on an Orbitrap Exploris 480 mass spectrometer (Thermo Scientific) coupled to an UltiMate 3000 UHPLC system (Thermo Scientific). Solvent A was 0.1 % FA in water, and Solvent B was 0.1 % FA in 80 % ACN:20 % water. Peptides were first trapped on a µ-precolumn (C18 PepMap100, 5 µm, 100 Å, 5 mm × 300 µm; Thermo Scientific) in 3 % Solvent B and then separated on an in-house-packed analytical column at 40 °C ReproSil-Pur 120Å C18-AQ, 2.4 µm, 75 µm x 50 cm (bulk media Dr. Maisch) at a flow rate of 300 nL min-1. For proteome analysis, the gradient of Solvent B was 3-9 % in 1 min, 9-35 % in 65 min, 35-55 % in 5 min, 55-99 % in 3 min, 99 % for 5 min, and re-equilibrated at 3 % for 10 min. Eluting peptides were online-injected into the mass spectrometer for data-dependent acquisition. The electrospray voltage was set at 2000 V, the ion transfer tube was set to 275 °C with an RF lens voltage of 40 %. Full MS scans were acquired at 60,000 resolution over m/z 375–1600 with a‘Standard’AGC target. Multiply charged precursor ions (m/z ≥120) were selected for fragmentation by higher-energy collisional dissociation (HCD, 28 % NCE), with 1.4 m/z isolation window, resolution of 15,000, and dynamic exclusion of 14 s."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS data were acquired with Thermo Scientific Xcalibur (version 4.6.67.17), and raw files were processed in FragPipe (v22.0) with the integrated MSFragger search engine (Kong et al., 2017; Teo et al., 2021) (v4.1). Data was searched against the protein sequences database derived from the genome A. oryzae RIB40  and against Pisum sativum UniProt database (downloaded in July 2023, containing 64,176 entries) with decoys and common contaminants appended. Standard parameter settings were used with semi-tryptic enzyme specificity, up to two missed cleavages, and precursor and fragment mass tolerances of 20 ppm. Variable modifications included methionine oxidation and protein N-terminal acetylation. Label-free quantification (‘Run MS1 quant’) (Yu et al., 2021) required ≥2 ions per protein, with match-between-runs enabled (top runs = 2). Peptide-spectrum matches (PSMs) were filtered to a 1 % false discovery rate (FDR) at the PSM, peptide, and protein levels using Philosopher (da Veiga Leprevost et al., 2020) and ProteinProphet (Nesvizhskii et al., 2003). Quantitative and identification results were exported for downstream analysis."],"omics_type":["Proteomics"],"labhead":["Kelly E. Stecker"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Biomolecular Mass Spectrometry and Proteomics, Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 CH Utrecht, the Netherlands"],"species":["Pisum Sativum (garden Pea)","Aspergillus Oryzae Rib40"],"publication":["42176576 Braat M, Braat N, Staliarova N, Vellozo-Echevarría T, Siwek HM, Kemmer JF, Barrett K, Meyer AS, Stecker KE, Wösten HAB. Spore inoculum size impacts substrate degradation and sporulation but not the secretome during colonization of whole yellow pea (Pisum sativum) by Aspergillus oryzae. Int J Food Microbiol. 2026 458:111853 10.1016/j.ijfoodmicro.2026.111853"],"submitter_mail":["n.staliarova@uu.nl"],"submitter_affiliation":["Utrecht University"],"submitter_country":["Netherlands"],"doi":["10.6019/PXD070642"],"pubmed_abstract":["Aspergillus oryzae is used in solid-state fermentation (SSF) to produce plant-based foods. To this end, the substrate is inoculated with spores of this fungus. So far, the effect of inoculum size on SSF with A. oryzae has primarily focused on the production of specific enzymes. Therefore, the aim of this study was to examine the impact of inoculum size on the full secretome, combined with enzyme activity assays, assessment of colonization, substrate degradation, and sporulation. To this end, A. oryzae was grown for 7 days on whole yellow pea (Pisum sativum). Fluorescence microscopy with a GFP-expressing A. oryzae strain showed that peas had been colonized externally and internally, irrespective of inoculum size. Yet, the highest inoculum size resulted in a stronger pea biomass reduction when compared to the lowest inoculum size. By contrast, sporulation decreased with increasing inoculum size. Notably, proteomics revealed no effect of inoculum size on the protein profiles of aqueous extracts of the colonized peas. Amylases and proteases were the most abundant secreted proteins, which was consistent with their high activity in the aqueous extracts. Proteomics also identified β-1,3-glucanases and chitinases, indicating hyphal lysis. Indeed, 10-19% of the fungal proteins detected in the aqueous extracts lacked signal peptides. These data contribute to our understanding of colonization of substrates by A. oryzae and may be used to optimize SSF with this food grade fungus."],"pubmed_title":["Spore inoculum size impacts substrate degradation and sporulation but not the secretome during colonization of whole yellow pea (Pisum sativum) by Aspergillus oryzae."],"pubmed_authors":["Braat Maaike M, Braat Nienke N, Staliarova Nadzeya N, Vellozo-Echevarría Tomás T, Siwek Hania M HM, Kemmer Julius F JF, Barrett Kristian K, Meyer Anne S AS, Stecker Kelly E KE, Wösten Han A B HAB"],"additional_accession":[]},"is_claimable":false,"name":"Spore inoculum size impacts substrate degradation and sporulation but not the secretome during colonization of whole yellow pea (Pisum sativum) by Aspergillus oryzae","description":"Aspergillus oryzae is used in solid-state fermentation (SSF) to produce plant-based foods. To this end, the substrate is inoculated with spores of this fungus. So far, the effect of inoculum size on SSF with A. oryzae has primarily focused on the production of specific enzymes. Therefore, the aim of this study was to examine the impact of inoculum size on the full secretome, combined with enzyme activity assays, assessment of colonization, substrate degradation, and sporulation. To this end, A. oryzae was grown for 7 days on whole yellow pea (Pisum sativum). Fluorescence microscopy with a GFP-expressing A. oryzae strain showed that peas had been colonized externally and internally, irrespective of inoculum size. Yet, the highest inoculum size resulted in a stronger pea biomass reduction when compared to the lowest inoculum size. By contrast, sporulation decreased with increasing inoculum size. Notably, proteomics revealed no effect of inoculum size on the protein profiles of aqueous extracts of the colonized peas. Amylases and proteases were the most abundant secreted proteins, which was consistent with their high activity in the aqueous extracts. Proteomics also identified β-1,3-glucanases and chitinases, indicating hyphal lysis. Indeed, 10–19% of the fungal proteins detected in the aqueous extracts lacked signal peptides. These data contribute to our understanding of colonization of substrates by A. oryzae and may be used to optimize SSF with this food grade fungus.","dates":{"publication":"2026-06-26","submission":"2025-11-12"},"accession":"PXD070642","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:441772","NEWT:48106","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606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