National R & D Center for Freshwater Fish Processing, and Engineering Research Center of Freshwater Fish High-value Utilization of Jiangxi Province, College of Life Science, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
National R & D Center for Freshwater Fish Processing, and Engineering Research Center of Freshwater Fish High-value Utilization of Jiangxi Province, College of Life Science, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
Food Chem. 2022 Mar 15;372:131308. doi: 10.1016/j.foodchem.2021.131308. Epub 2021 Oct 5.
The effects of phosphorylation on the allergenicity of bovine α-lactalbumin (BLA) and digestive products were studied in vitro digestion. Two components with different molecular weight and conformation were obtained from natural and phosphorylated BLA. In vivo and in vitro assessment of allergenicity showed that phosphorylation prior to digestion significantly decreased the IgE/IgG binding capacity and allergic response in KU812 cells, and reduced the levels of IgG, IgE, IL-4 and histamine, with an increase in IFN-γ levels in mouse serum, depending on the changes in BLA structures, producing numerous small peptides. There were four phosphorylated sites (S22, T29, S47 and S70) in the high molecular weight components of phosphorylated BLA after digestion. These phosphorylated sites could mask the linear epitopes of digestive products, resulting in reduced allergic activity. Phosphorylation prior to digestion of dairy products can reduce the risk of anaphylaxis in patients with milk allergy to some extent.
研究了磷酸化对牛α-乳白蛋白（BLA）及其消化产物变应原性的影响。从天然和磷酸化 BLA 中获得了两种具有不同分子量和构象的成分。体内和体外变应原性评估表明，消化前的磷酸化显著降低了 KU812 细胞中的 IgE/IgG 结合能力和过敏反应，并降低了 IgG、IgE、IL-4 和组氨酸水平，同时 IFN-γ水平在小鼠血清中升高，这取决于 BLA 结构的变化，产生了许多小肽。在磷酸化 BLA 的高分子量成分中，有四个磷酸化位点（S22、T29、S47 和 S70）在消化后。这些磷酸化位点可以掩盖消化产物的线性表位，从而降低过敏活性。在消化乳制品之前进行磷酸化可以在一定程度上降低牛奶过敏患者发生过敏反应的风险。
