@conference{
author = "Đukić, Teodora and Smiljanić, Katarina and Prodić, Ivana and Ćirković Veličković, Tanja",
year = "2023",
abstract = "A bottom-up proteomic study, using high-resolution tandem mass spectrometry (HRMS) and, PEAKS Studio X+ was performed to investigate the impact of peanut roasting on readily soluble allergens and their post-translational modification (PTM) profiles. Among four major peanut allergen groups, we found that Ara h 3 prevails in raw peanut extract (PE), similar to Ara h 1, while the opposite is true for Ara h 6, which is enriched in roasted PE; Ara h 2 bands are near the same intensity. HRMS detected more than 40 different types of modification in raw and roasted samples. Distinct variations in the types and occurrence of specific amino acid PTMs were identified between allergens present in raw and roasted samples. Roasting affected the most frequent modifications by enrichment of OxM, HyP, carbamoylation (KR), and deamidation. The PTMs could also be mapped to the regions of IgE-binding epitopes of Ara h 1–3 and Ara h 6. As porcine trypsin is used for HRMS sample preparation and is also a digestive protease, hindrance effects to trypsin efficacy regarding PTMs was assessed. Roasting caused dihydroxylation and formylation PTMs with hindrance effects to trypsin efficacy, while methylation on several K/R showed opposite effects. In the case of methylated R342, results suggested facilitation of tryptic performance at modified residue compared to unmodified counterpart, while in the rest of seven genuine sequences containing modified residues, trend was opposite. Further exploration of how different PTMs could affect digestion efficiencies of major gastric and intestinal peptidases is currently in works and a much-needed assessment to better understand the role of PTMs.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society, Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology”",
title = "Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and their hinderence of trypsin digestion",
pages = "147-146",
url = "https://hdl.handle.net/21.15107/rcub_intor_887"
}