运用圆二色光谱（CD）和荧光光谱以及ELISA方法对花生蛋白Ara h1的热变性及其与还原糖的相互作用, 以及过敏原性的变化进行了系统研究。 实验表明, 温度高于85 ℃时, Ara h1蛋白的二级结构才发生显著变化, 表现为α螺旋结构的相对含量减少, β折叠及无规卷曲等结构的相对含量增加, 其过敏原性也相应降低; 木糖、 果糖能与Ara h1蛋白进行相互作用进而有效稳定其蛋白结构, 并显著降低其过敏原性。 研究结果对食物过敏原致敏机理的深入研究, 以及花生食品的合理加工具有重要的理论指导意义。

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 α-helical structure and its allergenicity with the temperature higher than 85 ℃, 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.