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Guang Pu Xue Yu Guang Pu Fen Xi ; 33(8): 2128-31, 2013 Aug.
Artigo em Chinês | MEDLINE | ID: mdl-24159861

RESUMO

The thermal denaturation of peanut allergen Ara h1, its interaction with reducing sugars and the corresponding changes in allergenicity were investigated by circular dichroism (CD), fluorescence and ELISA method comprehensively. The experimental results indicate that the secondary structure of Ara h1 changes significantly along with decreasing alpha-helical structure and its allergenicity with the temperature higher than 85 degrees C, and that both xylose and fructose can stabilize Ara h1 protein structure through interacting with Ara h1 protein and decrease its allergenicity obviously. This study should be helpful to the further understanding of sensitization mechanism of food allergy and be useful for the guidance on reasonable manufacturing of peanut foods.


Assuntos
Antígenos de Plantas/química , Arachis/química , Carboidratos/química , Glicoproteínas/química , Proteínas de Plantas/química , Desnaturação Proteica , Espectrometria de Fluorescência , Dicroísmo Circular , Temperatura Alta , Proteínas de Membrana
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