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Thermal processing effects on peanut allergen Ara h 2 allergenicity in mice and its antigenic epitope structure

Zhang, Wenju, Zhu, Qingqing, Zhang, Tong, Cai, Qin, Chen, Qin
Food chemistry 2016 v.212 pp. 657-662
allergenicity, allergens, binding capacity, boiling, epitopes, frying, glycation, mice, peanuts, protein structure, roasting
Ara h 2 was purified from peanuts that were thermally treated by various processes, including boiling, glycation, frying and roasting. The allergenicity of Ara h 2 in Balb/c mice and the influence of thermal processing on the structural characteristics, and binding capacity of three core antigenic epitopes were studied. The results demonstrated that boiling, glycation and frying induced the down-regulation of the allergenicity of Ara h 2 in Balb/c mice, the collapse of its tertiary/secondary structure, and a reduction in the core epitope binding capacity; roasting showed a comparable allergenicity and the weakest inhibitory effect on core epitope binding capacity. These results indicate that thermal processing causes alteration of the protein structure and core epitopes of Ara h 2, and may affect its allergenicity.