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Advisor(s)
Abstract(s)
Hen's egg allergy has been climbing in all countries due to eggs ubiquity in foodstuffs. This allergy
is an IgE mediated reaction that affects mainly infants and young children. So far, the processes
used to decrease the allergenicity of egg proteins, such as cooking, thermal processing, storage
and enzymatic digestion have not been totally effective. Previous studies demonstrated that
proteins form complexes with phenolic compounds, so the aim of this work was to analyze the
effect of these compounds in ovalbumin (OVA) conformation and its possible application to
reduce eggs allergenicity. OVA was incubated at different temperatures with phenolic compounds
(caffeic, chlorogenic, ferulic, gallic and tannic acids; resveratrol and quercetin) and was analyzed
by circular dichroism (CD), Attenuated Total Reflection–Fourier Transform Infra-Red (ATRFTIR)
spectroscopy and fluorescence. Changes in the secondary structure of OVA were evidenced
by CD and ATR-FTIR. Also, protein fluorescence decreased with increasing concentrations of
phenolic compounds. The thermodynamic analysis suggested that electrostatic interactions are
important in the binding process, and the quenching mechanism occur by contact. This was
confirmed by docking where the phenolic compounds bind specifically to some regions of the
protein, including those with the allergenic epitopes.
Description
Keywords
Egg allergy Hypoallergenic eggs Interactions Ovalbumin