Dietary polyphenols reduced the allergenicity of β-lactoglobulin via non-covalent interactions: a study on the structure-allergenicity relationship
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...
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| Language: | English |
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Tsinghua University Press
2024-09-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | https://www.sciopen.com/article/10.26599/FSHW.2022.9250210 |
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| author | Chi Zhang Qiaozhi Zhang Huatao Li Zhouzhou Cheng Shiyu Fan Hujun Xie Zhongshan Gao Yan Zhang Linglin Fu |
| author_facet | Chi Zhang Qiaozhi Zhang Huatao Li Zhouzhou Cheng Shiyu Fan Hujun Xie Zhongshan Gao Yan Zhang Linglin Fu |
| author_sort | Chi Zhang |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-b5d804acdd7542a7bc3d0ef8cfe9443c |
| institution | Kabale University |
| issn | 2097-0765 2213-4530 |
| language | English |
| publishDate | 2024-09-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-b5d804acdd7542a7bc3d0ef8cfe9443c2025-01-10T06:56:56ZengTsinghua University PressFood Science and Human Wellness2097-07652213-45302024-09-011352617262810.26599/FSHW.2022.9250210Dietary polyphenols reduced the allergenicity of β-lactoglobulin via non-covalent interactions: a study on the structure-allergenicity relationshipChi Zhang0Qiaozhi Zhang1Huatao Li2Zhouzhou Cheng3Shiyu Fan4Hujun Xie5Zhongshan Gao6Yan Zhang7Linglin Fu8School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaSchool of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaSchool of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaSchool of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaSchool of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaSchool of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaAllergy Research Center, Zhejiang University, Hangzhou 310018, ChinaHebei 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, ChinaSchool of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaStudies 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.https://www.sciopen.com/article/10.26599/FSHW.2022.9250210cow’s milk allergyβ-lactoglobulinprotein-polyphenol interactionallergenicityconformational structure |
| spellingShingle | Chi Zhang Qiaozhi Zhang Huatao Li Zhouzhou Cheng Shiyu Fan Hujun Xie Zhongshan Gao Yan Zhang Linglin Fu Dietary polyphenols reduced the allergenicity of β-lactoglobulin via non-covalent interactions: a study on the structure-allergenicity relationship Food Science and Human Wellness cow’s milk allergy β-lactoglobulin protein-polyphenol interaction allergenicity conformational structure |
| title | Dietary polyphenols reduced the allergenicity of β-lactoglobulin via non-covalent interactions: a study on the structure-allergenicity relationship |
| title_full | Dietary polyphenols reduced the allergenicity of β-lactoglobulin via non-covalent interactions: a study on the structure-allergenicity relationship |
| title_fullStr | Dietary polyphenols reduced the allergenicity of β-lactoglobulin via non-covalent interactions: a study on the structure-allergenicity relationship |
| title_full_unstemmed | Dietary polyphenols reduced the allergenicity of β-lactoglobulin via non-covalent interactions: a study on the structure-allergenicity relationship |
| title_short | Dietary polyphenols reduced the allergenicity of β-lactoglobulin via non-covalent interactions: a study on the structure-allergenicity relationship |
| title_sort | dietary polyphenols reduced the allergenicity of β lactoglobulin via non covalent interactions a study on the structure allergenicity relationship |
| topic | cow’s milk allergy β-lactoglobulin protein-polyphenol interaction allergenicity conformational structure |
| url | https://www.sciopen.com/article/10.26599/FSHW.2022.9250210 |
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