Academic Bibliography

 Search 200 years of publications by Ghent University researchers.
Advanced search
1 file | 2.50 MB
Add to list
  1. Search results
  2. Covalent conjugation with (-)-epigall...

Covalent conjugation with (-)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut

Weiyi He, Tingting Zhang, Tanja Cirkovic Velickovic (UGent) , Shuiming Li, Yansi Lyu, Linlin Wang, Jiang Yi, Zhigang Liu, Zhendan He and Xuli Wu
(2020) FOOD CHEMISTRY. 331.
Author
Organization
Abstract
Ara h1 is a major allergen from peanut. We investigated the effect of covalent conjugation of Ara h1 and dietary polyphenols on allergenicity and functional properties of Ara h1. Enzyme-linked immunosorbent assay revealed that the covalent conjugation of dietary polyphenols significantly reduced the IgE binding capacity of Ara h1. Covalent binding of dietary polyphenols with Ara h1 reduced histamine release by 40% in basophils. The decreased IgE binding capacity of Ara h1 could be ascribed to changes in protein conformation. The IgE epitope of Ara h1 might be blocked by polyphenols at the binding site. Analysis of pepsin digestion of Ara h1-polyphenol conjugates indicated that the covalent binding increased pepsin digestibility and reduced IgE binding capacity. Furthermore, covalent conjugation of Ara h1 with polyphenols decreased denaturation temperature and increased antioxidant activity. Ara h1 conjugated with polyphenols may be a promising approach for reducing the allergenicity of Ara h1.
Keywords
IN-VITRO, BETA-LACTOGLOBULIN, IGE-BINDING, PROTEIN, POLYPHENOLS, CAPACITY, Ara h1, EGCG, Chlorogenic acid, Covalent conjugation, Allergenicity

Downloads

  • Download
    (...).pdf
    • full text (Published version)
    • |
    • UGent only
    • |
    • PDF
    • |
    • 2.50 MB

Citation

Please use this url to cite or link to this publication:

MLA
He, Weiyi, et al. “Covalent Conjugation with (-)-Epigallo-Catechin 3-Gallate and Chlorogenic Acid Changes Allergenicity and Functional Properties of Ara H1 from Peanut.” FOOD CHEMISTRY, vol. 331, 2020, doi:10.1016/j.foodchem.2020.127355.
APA
He, W., Zhang, T., Cirkovic Velickovic, T., Li, S., Lyu, Y., Wang, L., … Wu, X. (2020). Covalent conjugation with (-)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut. FOOD CHEMISTRY, 331. https://doi.org/10.1016/j.foodchem.2020.127355
Chicago author-date
He, Weiyi, Tingting Zhang, Tanja Cirkovic Velickovic, Shuiming Li, Yansi Lyu, Linlin Wang, Jiang Yi, Zhigang Liu, Zhendan He, and Xuli Wu. 2020. “Covalent Conjugation with (-)-Epigallo-Catechin 3-Gallate and Chlorogenic Acid Changes Allergenicity and Functional Properties of Ara H1 from Peanut.” FOOD CHEMISTRY 331. https://doi.org/10.1016/j.foodchem.2020.127355.
Chicago author-date (all authors)
He, Weiyi, Tingting Zhang, Tanja Cirkovic Velickovic, Shuiming Li, Yansi Lyu, Linlin Wang, Jiang Yi, Zhigang Liu, Zhendan He, and Xuli Wu. 2020. “Covalent Conjugation with (-)-Epigallo-Catechin 3-Gallate and Chlorogenic Acid Changes Allergenicity and Functional Properties of Ara H1 from Peanut.” FOOD CHEMISTRY 331. doi:10.1016/j.foodchem.2020.127355.
Vancouver
1.
He W, Zhang T, Cirkovic Velickovic T, Li S, Lyu Y, Wang L, et al. Covalent conjugation with (-)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut. FOOD CHEMISTRY. 2020;331.
IEEE
[1]
W. He et al., “Covalent conjugation with (-)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut,” FOOD CHEMISTRY, vol. 331, 2020.
@article{8720928,
  abstract     = {{Ara h1 is a major allergen from peanut. We investigated the effect of covalent conjugation of Ara h1 and dietary polyphenols on allergenicity and functional properties of Ara h1. Enzyme-linked immunosorbent assay revealed that the covalent conjugation of dietary polyphenols significantly reduced the IgE binding capacity of Ara h1. Covalent binding of dietary polyphenols with Ara h1 reduced histamine release by 40% in basophils. The decreased IgE binding capacity of Ara h1 could be ascribed to changes in protein conformation. The IgE epitope of Ara h1 might be blocked by polyphenols at the binding site. Analysis of pepsin digestion of Ara h1-polyphenol conjugates indicated that the covalent binding increased pepsin digestibility and reduced IgE binding capacity. Furthermore, covalent conjugation of Ara h1 with polyphenols decreased denaturation temperature and increased antioxidant activity. Ara h1 conjugated with polyphenols may be a promising approach for reducing the allergenicity of Ara h1.}},
  articleno    = {{127355}},
  author       = {{He, Weiyi and Zhang, Tingting and Cirkovic Velickovic, Tanja and Li, Shuiming and Lyu, Yansi and Wang, Linlin and Yi, Jiang and Liu, Zhigang and He, Zhendan and Wu, Xuli}},
  issn         = {{0308-8146}},
  journal      = {{FOOD CHEMISTRY}},
  keywords     = {{IN-VITRO,BETA-LACTOGLOBULIN,IGE-BINDING,PROTEIN,POLYPHENOLS,CAPACITY,Ara h1,EGCG,Chlorogenic acid,Covalent conjugation,Allergenicity}},
  language     = {{eng}},
  pages        = {{11}},
  title        = {{Covalent conjugation with (-)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut}},
  url          = {{http://doi.org/10.1016/j.foodchem.2020.127355}},
  volume       = {{331}},
  year         = {{2020}},
}
Altmetric
View in Altmetric
Web of Science
Times cited: