当前位置: X-MOL 学术J. Food Biochem. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Potential allergenicity assessment after bovine apo-α-lactalbumin binding to calcium ion.
Journal of Food Biochemistry ( IF 4 ) Pub Date : 2020-07-15 , DOI: 10.1111/jfbc.13340
Meijia Huang 1, 2 , Xin Li 1, 2 , Ping Tong 1, 2 , Jinyan Gao 1, 2 , Juanli Yuan 1, 3 , Anshu Yang 1, 4 , Hongbing Chen 1, 4 , Yong Wu 1, 4
Affiliation  

Bovine α‐lactalbumin (α‐LA) is recognized as a major milk allergen. Generally, α‐LA in the natural state combines with a calcium ion, however, some studies have shown that calcium ions can binding the other metal binding sites in α‐LA as well. In our study, the optimal condition of calcium ion binding to α‐LA and the change of structure and allergenicity were explored. By optimizing the conditions, the maximum calcium binding amounts of apo‐α‐LA were obtained in a ratio of 1:4. The structure of α‐LA after removal of calcium obviously changed by the spectroscopic detection. For the digestive stability, there was no obvious change in three forms of α‐LA. While the allergenic properties were characterized by IgG/IgE inhibition ELISA and the human basophil KU812 degranulation assay. The results showed that IgG and IgE binding decreased, and the degranulation capacity of basophils weakened. Based on these results, calcium binding to apo‐α‐LA can reduce the potential allergenic properties.

中文翻译:

牛脱辅基-α-乳白蛋白与钙离子结合后的潜在致敏性评估。

牛α-乳白蛋白(α-LA)被认为是主要的牛奶过敏原。通常,处于自然状态的α‐LA与钙离子结合,但是,一些研究表明,钙离子也可以与α‐LA中的其他金属结合位点结合。在我们的研究中,探讨了钙离子与α‐LA结合的最佳条件以及结构和变应原性的变化。通过优化条件,以1:4的比例获得了apo-α-LA的最大钙结合量。光谱检测结果表明,去除钙后α-LA的结构发生了明显变化。对于消化稳定性,三种形式的α-LA没有明显变化。虽然通过IgG / IgE抑制ELISA和人嗜碱性粒细胞KU812脱颗粒测定法表征了变应原性质。结果显示IgG和IgE的结合减少,并且嗜碱性粒细胞的脱粒能力减弱。根据这些结果,钙与apo-α-LA的结合可以减少潜在的过敏性。
更新日期:2020-09-14
down
wechat
bug