化学
乳清蛋白
水溶液中的金属离子
金属
离子
β-乳球蛋白
构象变化
过敏原
生物物理学
食品科学
免疫学
生物化学
生物
过敏
有机化学
作者
Shuangwen Fei,Jianwen Zhou,Yong Wu,Ping Tong,Jingyan Gao,Hongbing Chen,Xin Li
出处
期刊:Food Chemistry
[Elsevier]
日期:2021-12-01
卷期号:364: 130030-130030
被引量:3
标识
DOI:10.1016/j.foodchem.2021.130030
摘要
• Heat treatment and divalent cations had impact on the aggregation of β-lactoglobulin. • Ca 2+ and Zn 2+ increased the particle size of β-lactoglobulin aggregates. • Cu 2+ effected the conformational structure of β-lactoglobulin strongly. • Free sulfhydryl content was significantly declined after Cu 2+ treatment. • Cu 2+ enhanced peptic digestion of β-lactoglobulin and decreased its antigenicity. Aggregation of bovine β-lactoglobulin is affected easily by external factors. In this study, effects of metal ions combining with temperature on aggregation of β-lactoglobulin were explored. The conformational characteristics of aggregates were detected by environment scanning electron microscope, CD spectrum and free sulfhydryl group, respectively. Digestive and immunological characteristics were assessed by simulated digestion in vitro and ELISA respectively. The results showed that the morphology of β-lactoglobulin aggregates became more amorphous in Cu 2+ and Mg 2+ treated samples and more constricted in Zu 2+ -induced protein. Among them, Cu 2+ altered the secondary structure of β-lactoglobulin aggregates and free sulfhydryl content most as well as that in gastric digestion. However, all ion-treated groups had similar digestive stability in intestinal digestion. Specially, Ca 2+ and Mg 2+ made the antigenicity and potential allergenicity of β-lactoglobulin aggregates decrease, which helps us understand the role of metal ions in immunological characteristics.
科研通智能强力驱动
Strongly Powered by AbleSci AI