TNO Quality of Life, Zeist, The Netherlands.
Mol Nutr Food Res. 2010 Dec;54(12):1711-21. doi: 10.1002/mnfr.201000011.
There are differences in stability to pepsin between the major allergens in peanut; however, data are from different reports using different digestion models. This study provides a comprehensive comparison of the digestibility of the major peanut allergens.
Peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 were incubated with pepsin to mimic the effect of gastric digestion. Samples were analyzed using SDS-PAGE. To further investigate resistance to digestion, Ara h 2 was additionally subjected to digestion with trypsin and residual peptides were characterized. Ara h 1 and Ara h 3 were rapidly hydrolyzed by pepsin. On the contrary, Ara h 2 and Ara h 6 were resistant to pepsin digestion, even at very high concentrations of pepsin. In fact, limited proteolysis could only be demonstrated by SDS-PAGE performed under reducing conditions, indicating an important role for the disulfide bridges in maintaining the quaternary structure of Ara h 2 and Ara h 6. Trypsin digestion of Ara h 2 similarly resulted in large residual peptides and these were identified.
Ara h 2 and Ara h 6 are considerably more stable towards digestion than Ara h 1 and Ara h 3.
花生中的主要过敏原之间存在对胃蛋白酶稳定性的差异；然而，这些数据来自使用不同消化模型的不同报告。本研究提供了对主要花生过敏原消化率的全面比较。
用胃蛋白酶孵育花生过敏原 Ara h 1、Ara h 2、Ara h 3 和 Ara h 6，模拟胃消化的作用。使用 SDS-PAGE 分析样品。为了进一步研究消化抗性，还对 Ara h 2 进行了胰蛋白酶消化，并且对残留肽进行了表征。Ara h 1 和 Ara h 3 被胃蛋白酶迅速水解。相反，Ara h 2 和 Ara h 6 对胃蛋白酶消化具有抗性，即使在胃蛋白酶的浓度非常高的情况下也是如此。实际上，仅在还原条件下进行的 SDS-PAGE 才能证明有限的蛋白水解，这表明二硫键在维持 Ara h 2 和 Ara h 6 的四级结构方面起着重要作用。Ara h 2 的胰蛋白酶消化同样导致大量残留肽，并且对这些肽进行了鉴定。
Ara h 2 和 Ara h 6 比 Ara h 1 和 Ara h 3 更能抵抗消化。
