Simulated in vitro digestion of α-lactalbumin modified by phosphorylation: Detection of digestive products and allergenicity.
Simulated in vitro digestion of α-lactalbumin modified by phosphorylation: Detection of digestive products and allergenicity.
复制标题
磷酸化修饰的 α-乳清蛋白的模拟体外消化：消化产物和致敏性的检测。
DOI：
10.1016/j.foodchem.2021.131308
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发表时间：
2021
期刊：
影响因子：
8.8
通讯作者：
Z. Tu
中科院分区：
文献类型：
--
作者：
Wen;Yan;Zhi Wang;Jun Liu;Z. Tu
在体外消化中研究了磷酸化对牛α-乳清蛋白（BLA）及其消化产物致敏性的影响。从天然氨基酸和磷酸化氨基酸中得到两种分子量和构象不同的组分。体外变应原性评估显示，消化前磷酸化显著降低了KU812细胞的IgE/IgG结合能力和过敏反应，降低了IgG、IgE、IL-4和组胺的水平，小鼠血清中IFN-γ水平升高，这取决于BLA结构的变化，产生大量小肽。消化后的高分子量BLA磷酸化组分中有4个磷酸化位点（S22、T29、S47和S70）。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。乳制品消化前磷酸化可在一定程度上降低牛奶过敏患者发生过敏反应的风险。
The effects of phosphorylation on the allergenicity of bovine α-lactalbumin (BLA) and digestive products were studiedin vitrodigestion. Two components with different molecular weight and conformation were obtained from natural and phosphorylated BLA.In vivoandin vitroassessment 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.
影响因子：
6.1
作者：
H. Enomoto;Can-Peng Li;K. Morizane;H. Ibrahim;Y. Sugimoto;S. Ohki;H. Ohtomo;T. Aoki
通讯作者：
H. Enomoto;Can-Peng Li;K. Morizane;H. Ibrahim;Y. Sugimoto;S. Ohki;H. Ohtomo;T. Aoki