Effects of Different Thermal Processing Methods on the Structure and Allergenicity of Peanut Allergen Ara H 1
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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.
Hou T, Yan J, Li X, Niu L, Rao H, Hao J Food Chem X. 2024; 24:101876.
PMID: 39444440 PMC: 11497363. DOI: 10.1016/j.fochx.2024.101876.
Shu E, Wang S, Kong X, Sun X, Yang Q, Chen Q Food Technol Biotechnol. 2024; 62(1):4-14.
PMID: 38601963 PMC: 11002447. DOI: 10.17113/ftb.62.01.24.8064.
Olas B Foods. 2024; 13(2).
PMID: 38254543 PMC: 10814286. DOI: 10.3390/foods13020242.
Cohen C, Mazer B, Jean-Claude B Molecules. 2024; 29(1).
PMID: 38202743 PMC: 10780471. DOI: 10.3390/molecules29010162.
Shen M, Yang X, Wang Z, Sha X, Zhang X, Sun J Molecules. 2023; 28(17).
PMID: 37687106 PMC: 10489151. DOI: 10.3390/molecules28176277.