Boiling and frying can alter the structure of peanut allergens and therefore change the IgE-binding capacity of the Ara h 1. In this research, we aim to clarify the connections between structural changes and the allergenicity alteration, and recommend an effective thermal method to minimize the allergenicity of Ara h 1. Anion exchange chromatography was used to isolate Ara h 1 from non/heat-treated peanuts. Ara h 1 in boiled peanuts has a relatively low hydrophobic index, reduced maximum emission wavelength in the fluorescence, less content of α-helix, and the lowest IgE-binding efficiency. On the contrary, Ara h 1 in fried peanuts present a much higher degeneration degree, a red shift in fluorescence, and a decrease in the content of α-helix. These data indicate that boiling can reduce the allergenicity of Ara h 1, thus can be utilized in peanut processing from a security point of view.
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