ovalbumin and sodium-carbonate

Ovalbumin (OVA) is a major allergen in hen egg. During thermal processing, reducing sugars contained in the hen egg white might easily undergo glycation with OVA, but few studies have been conducted on its corresponding immunoreactivity changes. The aim of the present study was to assess changes of the antigenicity, potential allergenicity and conformation of OVA after glycation in a wet-thermal processing system under different concentrations of sodium carbonate-bicarbonate buffer.. IgE binding of the glycated OVA was increased after glycation, and the higher the sodium carbonate-bicarbonate buffer concentration, the higher the IgE binding capacity. The increase in IgE binding of OVA corresponded well with the disruption of the disulfide bond, which exposed the epitopes initially buried. Antigenicity of the glycated OVA was increased, and the amount of the increase varied among samples treated under different buffer concentrations.. Glycation increased the allergenic potential for OVA, with the amount of increase varying with different sodium carbonate-bicarbonate buffer concentrations.

Topics: Allergens; Animals; Buffers; Carbonates; Egg Hypersensitivity; Epitopes; Glycosylation; Hot Temperature; Humans; Hydrophobic and Hydrophilic Interactions; Immunoglobulin E; Immunoglobulin G; Models, Molecular; Ovalbumin; Protein Conformation; Rabbits; Sodium Bicarbonate