Dietary polyphenols reduced the allergenicity ofβ-lactoglobulin via non-covalent interactions:a study on the structure-allergenicity relationship  

作　　者：Chi Zhang Qiaozhi Zhang Huatao Li Zhouzhou Cheng Shiyu Fan Hujun Xie Zhongshan Gao Yan Zhang Linglin Fu 

机构地区：[1]School of Food Science and Biotechnology,Zhejiang Gongshang University,Hangzhou 310018,China [2]Allergy Research Center,Zhejiang University,Hangzhou 310018,China [3]Hebei Food Inspection and Research Institute,Hebei Food Safety Key Laboratory,Key Laboratory of Special Food Supervision Technology for State Market Regulation,Hebei Engineering Research Center for Special Food Safety and Health,Shijiazhuang 050227,China

出　　处：《Food Science and Human Wellness》2024年第5期2617-2628,共12页食品科学与人类健康（英文）

基　　金：supported by the Zhejiang Provincial Natural Science Foundation of China(LGN22C200027 and LZ23C200001).

摘　　要：Studies showed that complexation of polyphenols with milk allergens reduced their immunogenic potential.However,the relationship between structures of polyphenols and their hypoallergenic effects on milk allergens in association with physiological and conformational changes of the complexes remain unclear.In this study,polyphenols from eight botanical sources were extracted to prepare non-covalent complexes withβ-lactoglobulin(β-LG),a major allergen in milk.The dominant phenolic compounds bound toβ-LG with a diminished allergenicity were identified to investigate their respective role on the structural and allergenic properties ofβ-LG.Extracts from Vaccinium fruits and black soybeans were found to have great inhibitory effects on the IgE-and IgG-binding abilities ofβ-LG.Among the fourteen structure-related phenolic compounds,flavonoids and tannins with larger MWs and multi-hydroxyl substituents,notably rutin,EGCG,and ellagitannins were more potent to elicit changes on the conformational structures ofβ-LG to decrease the allergenicity of complexedβ-LG.Correlation analysis further demonstrated that a destabilized secondary structure and protein depolymerization caused by polyphenol-binding were closely related to the allergenicity property of formed complexes.This study provides insights into the understanding of structure-allergenicity relationship ofβ-LG-polyphenol interactions and would benefit the development of polyphenol-fortified matrices with hypoallergenic potential.

关 键 词：Cow’s milk allergy Β-LACTOGLOBULIN Protein-polyphenol interaction ALLERGENICITY Conformational structure 

分 类 号：TS201.4[轻工技术与工程—食品科学]