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Jelena Radosavljević

Researcher at University of Belgrade

Publications -  25
Citations -  597

Jelena Radosavljević is an academic researcher from University of Belgrade. The author has contributed to research in topics: Insulin & Insulin receptor. The author has an hindex of 9, co-authored 24 publications receiving 457 citations. Previous affiliations of Jelena Radosavljević include Academy of Sciences of the Czech Republic.

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Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed.

TL;DR: A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions and (b) masking of total antioxidant capacity ofprotein- polyphenol complexes.
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Digestibility and allergenicity assessment of enzymatically crosslinked β‐casein

TL;DR: The laccase/ caffeic acid and mushroom tyrosinase/caffeic Acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes.
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Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity

TL;DR: The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglUTins.
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Influence of peanut matrix on stability of allergens in gastric-simulated digesta : 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

TL;DR: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6, but the IgE reactivity of short digestion‐resistant peptides (SDRPs) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated.
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Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy.

TL;DR: Enzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut.