Change in conformational, digestive and immunological characteristics of bovine allergen β-lactoglobulin induced by metal ions in combination with heating. (1st December 2021)

• Record Type: Journal Article
• Authors: Fei, Shuangwen; Zhou, Jianwen; Wu, Yong; Tong, Ping; Gao, Jingyan; Chen, Hongbing; Li, Xin
• Is Part Of: Food chemistry. Volume 364(2021)
• Publication Date: 2021-12-01
• Subjects: HRP Horseradish peroxidase -- AP Ammonium persulfate -- SDS-PAGE Sodium dodecyl sulfate–polyacrylamide gel electrophoresis -- CD Circular dichroism -- DTNB Dinitrobenzoic acid -- SGF Simulated gastric fluid -- SIF Simulated intestinal fluid -- ELISA Enzyme-linked immunosorbent assay -- PBS Phosphate-buffered saline -- OPD O-Phenylenediamine -- ESEM Environmental scanning electron microscopy; Aggregation -- Allergenicity -- Bovine β-lactoglobulin -- Metal ions; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2021.130030
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: 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. Abstract: 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.