Thermally processed peanut proteins can form higher order structures, are less soluble, more resistant to digestive enzymes, and bind higher levels of IgE than raw peanut proteins.  In a majority of patients, roasted peanuts also resulted in a higher skin prick test reactivity.  To determine if processing-induced structural changes in allergens contribute to increased IgE binding, Ara h 1, 2 and 3 were purified from raw and roasted peanuts and the secondary structure and IgE binding were compared by immunoblotting with sera from peanut allergic patients.  Circular dichroism (CD) was used to monitor the structural changes.  While the structure of the allergens purified following roasting was not significantly altered compared to the raw, the IgE binding and SPT to the roasted samples were higher. It is highly likely that the chemical modifications incurred by roasting are important for IgE binding and immunogenicity of the major peanut allergens.

Effect of thermal processing on peanut allergens

245th National Meeting (2013)

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