{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Torres-Sanchez E"],"funding":["Sistema General de Regalías Colombia","Sistema General de Regalías (SGR)"],"pagination":["3275"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11506952"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(20)"],"pubmed_abstract":["Sacha Inchi (<i>Plukenetia volubilis</i>) oil press-cake (SIPC) represents a new source of proteins of high biological value, with promissory food applications. However, knowledge of these proteins remains limited. In this study, a Sacha Inchi protein concentrate (SPC) was extracted from the SIPC, and proteomic analysis was performed to identify the major alkaline-soluble proteins. The electrophoretic profile highlighted the efficacy of alkaline pH and moderate temperature to extract the major proteins, from which a group of proteins, not previously reported, were registered. LC-MS/MS analyses produced abundant high-quality fragmentation spectra. Utilizing the Euphorbiaceae database (DB), 226 proteins were identified, with numerous well-assigned spectra remaining unidentified. PEAKS Studio"],"journal":["Foods (Basel, Switzerland)"],"pubmed_title":["Proteomic Analysis of the Major Alkali-Soluble Inca Peanut (<i>Plukenetia volubilis</i>) Proteins."],"pmcid":["PMC11506952"],"funding_grant_id":["2020000100169","BPIN2020000100169"],"pubmed_authors":["Morato E","Gutierrez LF","Torres-Sanchez E","Hernandez-Ledesma B"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic Analysis of the Major Alkali-Soluble Inca Peanut (<i>Plukenetia volubilis</i>) Proteins.","description":"Sacha Inchi (<i>Plukenetia volubilis</i>) oil press-cake (SIPC) represents a new source of proteins of high biological value, with promissory food applications. However, knowledge of these proteins remains limited. In this study, a Sacha Inchi protein concentrate (SPC) was extracted from the SIPC, and proteomic analysis was performed to identify the major alkaline-soluble proteins. The electrophoretic profile highlighted the efficacy of alkaline pH and moderate temperature to extract the major proteins, from which a group of proteins, not previously reported, were registered. LC-MS/MS analyses produced abundant high-quality fragmentation spectra. Utilizing the Euphorbiaceae database (DB), 226 proteins were identified, with numerous well-assigned spectra remaining unidentified. PEAKS Studio","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-07-08T03:18:39.276Z","creation":"2025-04-04T11:42:51.446Z"},"accession":"S-EPMC11506952","cross_references":{"pubmed":["39456337"],"doi":["10.3390/foods13203275"]}}