食品科学与人类健康(英文)2024,Vol.13Issue(5) :2617-2628.DOI:10.26599/FSHW.2022.9250210

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

Chi Zhang Qiaozhi Zhang Huatao Li Zhouzhou Cheng Shiyu Fan Hujun Xie Zhongshan Gao Yan Zhang Linglin Fu
食品科学与人类健康(英文)2024,Vol.13Issue(5) :2617-2628.DOI:10.26599/FSHW.2022.9250210

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

Chi Zhang 1Qiaozhi Zhang 1Huatao Li 1Zhouzhou Cheng 1Shiyu Fan 1Hujun Xie 1Zhongshan Gao 2Yan Zhang 3Linglin Fu1
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作者信息

  • 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
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Abstract

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 with β-lactoglobulin(β-LG),a major allergen in milk.The dominant phenolic compounds bound to β-LG with a diminished allergenicity were identified to investigate their respective role on the structural and allergenic properties of β-LG.Extracts from Vaccinium fruits and black soybeans were found to have great inhibitory effects on the IgE-and IgG-binding abilities of β-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 of β-LG to decrease the allergenicity of complexed β-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 of β-LG-polyphenol interactions and would benefit the development of polyphenol-fortified matrices with hypoallergenic potential.

Key words

Cow's milk allergy/β-Lactoglobulin/Protein-polyphenol interaction/Allergenicity/Conformational structure

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基金项目

Zhejiang Provincial Natural Science Foundation of China(LGN22C200027)

Zhejiang Provincial Natural Science Foundation of China(LZ23C200001)

出版年

2024
食品科学与人类健康(英文)

食品科学与人类健康(英文)

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