Abstract：
:In this work, the mechanism of the effect of lipid oxidation on the IgG/IgE binding ability of ovalbumin (OVA) was investigated via the peroxyl radicals produced by 2, 2'-azobis (2-amidinopropane) dihydrochloride to simulate lipid oxidation. Results showed that the structure of OVA unfolded partially with an increase in oxidation degree, leading to the exposure of the allergenic epitopes and increasing the IgG/IgE binding ability of OVA. Nine oxidation sites were found on the α-helix, and these sites may unwind the α-helix and expose the allergenic epitopes on the OVA surface, leading to antibody recognition and combination. Consequently, the IgG/IgE binding ability of OVA was increased. In conclusion, the allergenic capacity of OVA can be promoted by modifying peroxyl radical oxidation in processing egg products.
journal_name
Food Chemjournal_title
Food chemistryauthors
Zhang JJ,Tu ZC,Wang H,Hu YM,Du PC,Yang YPdoi
10.1016/j.foodchem.2020.127037subject
Has Abstractpub_date
2020-10-15 00:00:00pages
127037eissn
0308-8146issn
1873-7072pii
S0308-8146(20)30899-2journal_volume
327pub_type
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