Development of hypoallergenic ovalbumin with improving functional properties by AAPH and acrolein treatment

Abstract

Ovalbumin (OVA) is one of the major allergenic proteins in egg that contain numerous functional properties. Here, oxidation-induced changes to the structure, functional properties, and allergenicity of OVA were evaluated after 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH) and acrolein treatment. Oxidation complexes were prepared by the lipid peroxidation, which caused structural changes, and increased digestibility, foaming, and emulsifying properties. The IgE-binding capacity of OVA decreased after oxidation. KU812 cell assay showed that the histamine and IL-4 levels decreased upon oxidation with AAPH and acrolein. A mouse model study showed that oxidation caused a reduction in the allergenicity by reducing IgE and IgG1 levels and the production of Th2 cytokines after acrolein (1 mmol/L) and AAPH (5 mmol/L) treatment. Thus, OVA could cause changes to structural and functional properties, modulating Th1/Th2 immunobalance, and reducing potential allergenicity after oxidation by lipid peroxidation, which might provide an effective and potential method to process hypoallergenic OVA.

Keywords

• OVA
• Oxidation
• Allergenicity
• Hypoallergenicity
• Digestibility