@conference{
author = "Đukić, Teodora and Khulal, Urmila and Smiljanić, Katarina and Vasović, Tamara and Aćimović, Jelena and Rajković, Andreja and Ćirković Veličković, Tanja",
year = "2024",
abstract = "Protein modifications (PMs) are covalent changes occurring on amino acid (AA) side chains of
proteins via enzymatic action or spontaneously. They increase the protein structure complexity
from the level of the genome to the proteome, and can determine their activity and, interactions1.
It has been shown, on myofibrillar fish proteins that oxidative modifications depending on their
saturation can decrease or enhance protein digestability2. Thus in this study shellfish meat samples
were subjected to cooking followed by simulated INFOGEST in vitro gastrointestinal digestion
protocol. Mass Spectrometry and in gel based proteomics, were used to detect PMs and digestion
resistan peptides of raw and cooked shellfish meat samples with a foucs on major shellfish allergens:
sarcoplasmic calcium-binding protein (SBP) and tropomyosin (TPM). Lastly, identified PMs
were marked on TPM alignment from shrimp, oyster and abalone species, to gain insight into their
pattern on the known IgE binding epitopes. Focusing on oxidative PMs, mostly on oxidation of Met,
it was confirmed that, in all shellfish samples, PMs on TPM and SBP were more predominant after
cooking. For instance in abalone, double oxidation of Met was only detected in cooked samples
(sulfone M68 and M81). Another indicator of oxidative stress, 4-hydroxynonenal (HNE), was identified
on shrimp TPM and, notably HNE was 21 times more abundant in the cooked sample. Study
highlights the susceptibility of immunodominant epitopes in major shellfish allergens to oxidative
PMs, which could impact interactions with the immune system in sensitive individuals. Significant
resistance to digestion was demonstrated by paramyosin fragments in abalone and oyster suggesting
the need for further analysis of their allergenicity. SBP of raw shrimp was strikingly resistant
to both gastric and intestinal digestion. Moreover, our results indicate that oxidative modifications
may decrease the stability of proteins like shrimp TPM, making them more digestible in thermally
treated samples, highlighting a potential strategy for reducing allergenicity.",
publisher = "University of Belgrade – Faculty of Chemistry",
journal = "VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia June 6th, 2024",
title = "Insights into oxidative protein modifications in shellfish allergens: Impact of GI digestion following thermal treatment",
pages = "10-10",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6539"
}
