{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077201/271123_Samuel_3.raw"],"Pepxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077201/spider.pep.xml"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077201/spider.mzidentml_1_2_0.xml"],"Mzxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077201/271123_Samuel_3.raw.mzxml"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077201/271123_Samuel_3.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077201/271123_Samuel_3.raw.mgf"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077201/spider.summary.html","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077201/spider.proteins.html"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["b.hernandez@csic.es"],"submitter":["Blanca Pardo de Donlebún"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077201"],"sample_protocol":["Consortia biomasses were first suspended in 50 µL of sample buffer before being ap-plied to 1.2-cm-wide wells of a traditional SDS-PAGE gel (0.75 mm thick, 4% stacking and 10% resolving; Bio-Rad, Hercules, CA, USA). When the front got 3 mm into the resolving gel, the run was stopped. The whole proteome was then concentrated in the stack-ing/resolving gel interface. Coomassie staining (Bio-Rad) was used to see the unseparated protein bands, which were removed, cut into 2 × 2 mm cubes and put in 0.5 ml microcen-trifuge tubes. The gel fragments were destained using acetonitrile:water (ACN:H2O, 1:1), subjected to reduction and alkylation (disulfide bonds from cysteine residues were reduced with 10 mM dithiothreitol (DTT) for 1 h at 56˚C, followed by alkylation of thiol groups with 10 mM iodoacetamide for 30 min at room temperature in darkness) and subsequently digested in situ with sequencing grade trypsin (Promega, Madison, WI, USA) as outlined by Shevchenko et al., with minor modifications. By employing enough ACN to remove all liquid, the gel pieces were shrunk. The gel fragments were dried in a speedvac after the ACN was pipetted out. The dried gel fragments were re-swollen in 100 mM Tris-HCl pH 8, 10 mM calcium chloride (CaCl2) and 60 ng/µl trypsin at a pro-tein:enzyme (w/w) ratio of 5:1. The tubes were incubated at 37˚C for 12 h after being placed on ice for 2 h. 0.2% RapiGest (Waters, Milford, MA, USA) was present during the digestion process. Finally, 1% trifluoroacetic acid (TFA) was added to stop digestion. Prior to the mass spectrometric measurement, whole supernatants were dried and desalted onto OMIX Pipette tips C18 (Agilent Technologies, Santa Clara, CA, USA). The desalted protein digests were then dried, resuspended in 10 µl of 0.1% formic acid and subjected to RP-LC-MS/MS analysis in an Easy-nLC 1200 system coupled to an ion trap LTQ-Orbitrap-Velos-Pro hybrid mass spectrometer (Thermo Scientific, Waltham, MA, USA). The peptides were concentrated (online) by reverse phase chromatography us-ing a 0.1 mm × 20 mm C18 RP precolumn (Thermo Scientific) and then separated using a 0.075 mm x 250 mm bioZen 2.6 µm Peptide XB-C18 RP column (Phenomenex, Torrance, CA, USA) at 0.25 μl/min. A 180-min dual gradient was used to elute the peptides. The gradient profile (solvent A: 0.1% formic acid in water, solvent B: 0.1% formic acid, 80% ACN in water) was set at 5−25% solvent B for 135 min, 25−40% solvent B for 45 min, 40−100% solvent B for 2 min, and 100% solvent B for 18 min. A Nano-bore emitter Stain-less Steel ID 30 μm (Proxeon, Odense, Denmark) interface was used for ESI ionization at a spray voltage of 2.1 kV with a 60% S-Lens. 30.000 was the Orbitrap resolution. Fol-lowing twenty data-dependent MS/MS scans (Top 20) with an isolation width of 2 u (in mass-to-charge ratio units), a normalized collision energy of 35% and dynamic exclusion performed for 60-second intervals, peptides were detected in survey scans ranging from 400 to 1600 amu (1 μscan). Rejecting unassigned and singly charged protonated ions was made possible by charge-state screening."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Finally, peptide identification from raw data was carried out using PEAKS Studio v11.5 search engine (Bioinformatics Solutions Inc., Waterloo, Ontario, Canada). Database search was performed against UniProt-A. platensis + UniProt-C. vulgaris for C1 and Uni-Prot-Kamptonema sp. + UniProt-N. oculata + UniProt-T. suecica + UniProt-C. vulgaris for C2 (decoy-fusion database). The searches were conducted with the following limitations: tolerances of 20 ppm for precursor ions and 0.6 Da for MS/MS fragment ions, tryptic cleavage after arginine and lysine (semispecific), up to two missed cleavage sites and the searches were performed allowing optional methionine oxidation and cysteine carbamidomethylation. False discovery rates (FDR) for PSM and for protein was set to 0.01. Proteins were deemed reliably identified only if at least two distinct peptides were found using LC/MS/MS analysis."],"omics_type":["Proteomics"],"labhead":["Blanca Hernández-Ledesma"],"instrument_platform":[""],"labhead_affiliation":["Department of Bioactivity and Food Analysis, Institute of Food Science Research (CIAL, CSIC-UAM, CEI UAM+CSIC), Nicolás Cabrera 9, 28049 Madrid, Spain"],"submission_type":["COMPLETE"],"species":["Arthrospira Platensis","Chlorella Vulgaris"],"publication":["10.3390/MD24050184"],"submitter_mail":["blanca.pardo@csic.es"],"submitter_affiliation":["Consejo Superior de Investigaciones Científicas (CSIC)"],"submitter_country":["Spain"],"doi":["10.6019/PXD077201"],"additional_accession":[]},"is_claimable":false,"name":"Enhancing the Recovery of Antioxidant Compounds from Microalgae-Cyanobacteria Consortia through Alcalase Hydrolysis: a Focus on Bioactive Peptides","description":"Microalgae and cyanobacteria represent an emerging and sustainable source of bioactive compounds for the food, cosmeceutical, and pharmaceutical sectors. In this study, the potential of two microalgae-cyanobacteria consortia, consortium 1 (C1) consisting of Chlorel-la vulgaris and Arthrospira platensis, and consortium 2 (C2) consisting of Kamptonema sp., Nannochloropsis oculata, Tetraselmis suecica, and Chlorella vulgaris, as a source of bioactive peptides was evaluated. Firstly, protein extraction from both biomasses was optimized by testing different protein solubilization and precipitation pHs, with pH 10 and pH 5 providing the best results in terms of protein recovery in both cases. Selected protein ex-tracts, with protein contents of 28.50 ± 2.69 % (C1) and 8.46 ± 0.45 % (C2), were further hy-drolyzed with Alcalase, evaluating the impact of the incubation time on peptide release and the antioxidant capacity of hydrolysates. 1 h of hydrolysis proved to be enough for antioxidant capacity increase. In addition, in silico hydrolysis with Alcalase of the proteins identified in C1 and C2 was evaluated, assessing the potential bioactivity of the peptides produced, more specifically their antioxidant capacity. Our findings demonstrate that both microalgae-cyanobacteria consortia are valuable sources of bioactive compounds with antioxidant capacity, with potential interest as functional ingredients for the food, cosmeceutical, and pharmaceutical 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