College of Veterinary Medicine, Henan Agricultural University, Zhengzhou, Henan, China.
College of Food Science and Technology, Henan Agricultural University, Zhengzhou, Henan, China.
J Food Sci. 2024 Sep;89(9):5559-5575. doi: 10.1111/1750-3841.17276. Epub 2024 Aug 16.
Ara h1 was the highest content of peanut allergen protein, identified as a biomarker of peanut allergen. In this study, Ara h1 was covalently complexed with caffeic acid (CA) to research the effects of covalent conjugation on the antigenicity and protein structural properties of Ara h1. After the covalent complexing of Ara h1 and CA, the IgG-binding capacity of Ara h1 was reduced compared with that of control Ara h1. Moreover, the structure of Ara h1 changed from ordered to disordered, the number of intermolecular hydrogen bonds decreased, and some hydrophobic groups were exposed or hydrophobic peptides were released. The carboxyl group in CA reacted with the amino group in Ara h1. The digestibility of Ara h1-CA was increased. The antigenicity of Ara h1-CA was undetectable after 30 min of digestion in vitro. These findings can serve as a reference for further research on hypoallergenic peanut products.
花生过敏原蛋白Ara h1 的含量最高,被鉴定为花生过敏原的生物标志物。本研究将 Ara h1 与咖啡酸(CA)共价结合,研究共价结合对 Ara h1 抗原性和蛋白质结构特性的影响。Ara h1 与 CA 共价结合后,与对照 Ara h1 相比,Ara h1 的 IgG 结合能力降低。此外,Ara h1 的结构从有序变为无序,分子间氢键数量减少,一些疏水性基团暴露或疏水性肽释放。CA 中的羧基与 Ara h1 中的氨基反应。Ara h1-CA 的消化率增加。Ara h1-CA 的抗原性在体外消化 30 分钟后无法检测到。这些发现可以为进一步研究低致敏性花生产品提供参考。