Lv Liangtao, Qu Xin, Yang Ni, Ahmed Ishfaq
College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
Third Affiliated Hospital of Shenzhen University, Shenzhen 518020, China.
Food Chem X. 2021 Apr 20;10:100120. doi: 10.1016/j.fochx.2021.100120. eCollection 2021 Jun 30.
β-lactoglobulin (BLG) is a major allergen of milk. Since lipid peroxidation such as acrolein commonly exists during milk processing, it is necessary to evaluate its influence on BLG structure and potential allergenicity. The structure of acrolein-treated BLG was detected using SDS-PAGE, fluorescence, ultraviolet spectrum (UV), circular dichroism (CD) and LC-MS-MS, and the potential allergenicity was assessed by and assays. Results showed that acrolein could cause structural changes by BLG aggregation, which decreased the IgE binding capacity. Further, the release of mediators and cytokines decreased with acrolein treatment in RBL-2H3 cells. Mice showed lower allergenicity by the levels of BLG-specific antibody and the release of histamine and mMCP-1. These results explained that acrolein-induced BLG aggregation could damage the allergic epitopes and decrease the allergenicity of BLG in milk. The study will provide a new aspect to explore the natural phenomenon of allergen changes during food processing.
β-乳球蛋白（BLG）是牛奶中的主要过敏原。由于在牛奶加工过程中通常存在脂质过氧化反应，如丙烯醛的产生，因此有必要评估其对BLG结构和潜在致敏性的影响。使用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）、荧光、紫外光谱（UV）、圆二色性（CD）和液相色谱-串联质谱（LC-MS-MS）检测丙烯醛处理后的BLG结构，并通过 和 试验评估其潜在致敏性。结果表明，丙烯醛可通过BLG聚集导致结构变化，从而降低免疫球蛋白E（IgE）结合能力。此外，在RBL-2H3细胞中，丙烯醛处理后介质和细胞因子的释放减少。小鼠体内BLG特异性抗体水平以及组胺和小鼠肥大细胞蛋白酶-1（mMCP-1）的释放显示出较低的致敏性。这些结果表明，丙烯醛诱导的BLG聚集可能会破坏过敏表位并降低牛奶中BLG的致敏性。该研究将为探索食品加工过程中过敏原变化的自然现象提供一个新的视角。
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