{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_G-2-3_21102019.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_B-2-2_21102019.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_G-2-1_21102019.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_B-2-1_21102019.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_B-2-3_21102019.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_G-2-2_21102019.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_G-2-3_21102019.raw"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_B-2-3_21102019.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_B-2-1_21102019.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_G-2-3_21102019.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_G-2-2_21102019.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_G-2-1_21102019.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD026193/MAngelesCastillejo_sol42-19_B-2-2_21102019.mgf"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["hdardilab@unal.edu.co"],"submitter":["Carolina Vega-Oliveros"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":["Not available"],"submitter_keywords":["Submerged fermentation","Mushroom","Shiitake","Shotgun","Agaricales"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD026193"],"tissue":["Mycelium"],"sample_protocol":["The strain of L. edodes was obtained from the company Shroom supply (https://shroomsupply.com/, United States). Mycelium was used for liquid state fermentation - LSF culture. It was add to the following culture broths, with their short name and composition in (g/L): GPY: glucose (20) OXOID®, Peptone (2,5) Panreac® and yeast extract (2.5) Merck®, BIE: Bienestarina - Colombian mixed flour (30). LSF was carried out at 150 revolutions per minute (rpm) and 27 + 1°C in an orbital shaker (Electrilab S.A.S., Bogotá D.C., Colombia). After 10 days of cultivation, the fresh mycelium was collected by filtration with Whatman No. 4, then it was deep-frozen (-80°C) and lyophilized (2.5 L Labconco Freezone Co., Kansas City, USA). Three independent lyophilized mycelia (20 mg) obtained from each liquid culture media evaluated were macerated with liquid nitrogen and used for protein extraction. Then, protein extraction was performed using TCA-Acetone precipitation and subsequent extraction with phenol as previously reported (Jorrin-Novo, 2014; Vega-Oliveros et al., 2017). For quantifying protein concentration in the extract, Bradford's method was used, employing bovine serum albumin (BSA) as standard. A standard SDS-PAGE step was introduced for protein sample cleaning (removal of detergents and other contaminants) according to (Valledor & Weckwerth, 2014) for 80 ug mycelium protein extract. Protein analyses were performed at the Proteomics Facility of the Research Support Central Service (SCAI) of the University of Cordoba. The nano-LC Dionex Ultimate 3000 nano UPLC equipment (Thermo Scientific) coupled to a nanoelectrospray ionization source and a trihybrid analyzer Thermo Orbitrap Fusion mass spectrometer (Thermo Scientific), operating in the positive ion mode were used. The specific settings used for MSMS analyses are described elsewhere (Castillejo et al., 2020). The LC settings were like (Romero-Rodríguez et al., 2019)"],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The raw data obtained from the MS analysis were processed with the software Proteome Discoverer v. 2.1.0.81 (Thermo Scientific). MS2 spectra were searched with the SEQUEST engine against the FASTA database obtained from the L. edodes database (with 12046 sequences) downloaded on 10/28/2019 from Uniprot (www.uniprot.org). Precursor mass tolerance was set at 10 ppm and fragment ion mass tolerance fixed at 0.1 Da. In silico peptide lists were generated by theoretical tryptic digestion, allowing up to two missed cleavages, carbamidomethylation of cysteines as a fixed modification, and oxidation of methionine as a variable modification. Peptides were classified into protein groups according to the law of parsimony and filtered to FDR = 1% and XCorr ≥ 2. The protein identification had > 2 peptides, a Score > 2, and Coverage > 10%. Quantification of proteins from the shotgun analysis was performed using the normalized Spectral Count values. The NSAF (Normalized spectral abundance factor) method was used for normalization, which accounts for protein size and variability between runs to normalize relative protein abundance between samples (Dowle et al., 2016). Those proteins consistently present in the three biological replicates were considered for further statistical analysis. The function assignment of the identified proteins was made based on the classification of groups of eukaryotic orthologs (KOG). For this, we used the databases available in JGI – MycoCosm (e-value < 10-3), specifically with the L. edodes B17 v1.1, L. edodes W1-26 v1.0 and L. edodes NBRC 111202 strains database in (https://mycocosm.jgi.doe.gov/agaricomycotina/agaricomycotina.info.html) (Chen et al., 2016; Park et al., 2017; Sakamoto et al., 2017; Shim et al., 2016). A univariant (ANOVA)/ multivariant (PCA) analysis of the entire dataset was performed to determine quantitative differences using a fold change (FC) ratio between the treatment group – BIE and the control group - GPY ≥2.0 or ≤ 0.5 were considered. Likewise, tests were applied to compare variances with the Volcano graph (α = 0.05). As complementary statistical software, the MetaboAnalyst tool was used (https://www.metaboanalyst.ca/MetaboAnalyst/home.xhtml). Also, it was revised the functional protein association networks comparing against the nearest mushroom species (Moniliophthora roreri, NCBI taxonomy Id: 221103) using the web resource https://string-db.org/"],"omics_type":["Proteomics"],"labhead":["Harold D. Ardila"],"instrument_platform":[""],"labhead_affiliation":["Associate professor Universidad Nacional de Colombia campus Bogotá Facultad de Ciencias Departamento de Química Investigation group: Actividades Metabólicas Vegetales"],"submission_type":["PARTIAL"],"species":["Fungi","Lentinula Edodes"],"publication":["10.1016/J.BCAB.2026.104095"],"submitter_mail":["cvegao@unal.edu.co"],"submitter_affiliation":["Doctorate Student"],"submitter_country":["Colombia"],"additional_accession":[]},"is_claimable":false,"name":"Effect of the substrate on the protein profile of the edible mushroom Lentinula edodes for its potential biotechnological applicationEffect of the substrate on the protein profile of the edible mushroom Lentinula edodes for its potential biotechnological application","description":"Some mushroom proteins and peptides have reported biological activities increasing interest due to their potential as nutraceuticals. It is necessary to research optimizing the substrates for biomass and protein production to improve the biotechnological approaches. This study evaluated the effect on biomass production and total intra-protein in Lentinula edodes grown by liquid-state fermentation (LSF) for eight culture mediums. The higher total protein content was found on bienestarina media (BIE), glucose, peptone, and yeast extract media (GPY). The protein profile using a shotgun proteomics approach by LC-MSMS showed the media's marked influence on protein production. Most proteins identified using the BIE medium did not appear when the mushroom grew in the GPY.  Some of the detected proteins included lectins and enzymes, are used in industrial applications. These results would indicate that BIE promotes in L. edodes the production of proteins with potential for its application to the biotechnology 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