State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China.
Food Funct. 2020 Oct 21;11(10):9240-9251. doi: 10.1039/d0fo02028a.
Bovine α-lactalbumin (BLA) and β-lactoglobulin (BLG) are the most common and severe food allergens in milk and they can bind C18 unsaturated fatty acids (UFAs) and their bioactivities were changed. This study aims to determine the effects of C18 UFAs on the structures of BLA and BLG and their allergic properties, such as antigenicity and allergenicity. We reveal that C18 UFAs can efficiently promote the gradual unfolding of the structures of BLA and BLG and increase their hydrophobicity. Moreover, the IgG binding ability and the expression of IgG-dependent activation marker CD200R3 on basophils were remarkably promoted after C18 UFA treatment. Finally, we also observed that C18 UFAs can enhance the IgE binding ability and the degranulation capacity of human basophil KU812 cells (intracellular Ca2+, histamine, β-Hex, and IL-6). Collectively, these results suggested that C18 UFAs changed the structures of BLA and BLG, which contributed to their increased allergic potential.
牛α-乳白蛋白（BLA）和β-乳球蛋白（BLG）是牛奶中最常见和最严重的食物过敏原，它们可以结合 C18 不饱和脂肪酸（UFA），并改变其生物活性。本研究旨在确定 C18UFA 对 BLA 和 BLG 结构及其过敏特性（如抗原性和致敏性）的影响。我们揭示了 C18UFA 可以有效地促进 BLA 和 BLG 结构的逐渐展开，并增加其疏水性。此外，C18UFA 处理后，IgG 结合能力和嗜碱性粒细胞上 IgG 依赖性激活标记物 CD200R3 的表达显著增强。最后，我们还观察到 C18UFA 可以增强人嗜碱性粒细胞 KU812 细胞（细胞内 Ca2+、组氨酸、β-Hex 和 IL-6）的 IgE 结合能力和脱颗粒能力。总之，这些结果表明 C18UFA 改变了 BLA 和 BLG 的结构，这有助于增加它们的过敏潜力。
