Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut
Samo za registrovane korisnike
2020
Autori
He, WeiyiZhang, Tingting
Ćirković-Veličković, Tanja
Li, Shuiming
Lyu, Yansi
Wang, Linlin
Yi, Jiang
Liu, Zhigang
He, Zhendan
Wu, Xuli
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Ključne reči:
Allergenicity / Ara h1 / Chlorogenic acid / Covalent conjugation / EGCGIzvor:
Food Chemistry, 2020, 331, 127355-Izdavač:
- Elsevier
Finansiranje / projekti:
- Innovation Project of Universities in Guangdong Province (2018KTSCX192)
- Key-Area Research and Development Program of Guangdong Province (2019B020213001)
- Medical Technological Research Funding of Guangdong Province (B2018041)
- Research Funding of Shenzhen (JCYJ20170818143841444)
- Research Funding of Shenzhen (JCYJ20180305163606176)
DOI: 10.1016/j.foodchem.2020.127355
ISSN: 0308-8146
WoS: 000559806600003
Scopus: 2-s2.0-85086800094
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - He, Weiyi AU - Zhang, Tingting AU - Ćirković-Veličković, Tanja AU - Li, Shuiming AU - Lyu, Yansi AU - Wang, Linlin AU - Yi, Jiang AU - Liu, Zhigang AU - He, Zhendan AU - Wu, Xuli PY - 2020 UR - https://cherry.chem.bg.ac.rs/handle/123456789/4053 AB - 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. PB - Elsevier T2 - Food Chemistry T1 - Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut VL - 331 SP - 127355 DO - 10.1016/j.foodchem.2020.127355 ER -
@article{ author = "He, Weiyi and Zhang, Tingting and Ćirković-Veličković, Tanja and Li, Shuiming and Lyu, Yansi and Wang, Linlin and Yi, Jiang and Liu, Zhigang and He, Zhendan and Wu, Xuli", year = "2020", 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.", publisher = "Elsevier", journal = "Food Chemistry", title = "Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut", volume = "331", pages = "127355", doi = "10.1016/j.foodchem.2020.127355" }
He, W., Zhang, T., Ćirković-Veličković, T., Li, S., Lyu, Y., Wang, L., Yi, J., Liu, Z., He, Z.,& Wu, X.. (2020). Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut. in Food Chemistry Elsevier., 331, 127355. https://doi.org/10.1016/j.foodchem.2020.127355
He W, Zhang T, Ćirković-Veličković T, Li S, Lyu Y, Wang L, Yi J, Liu Z, He Z, Wu X. Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut. in Food Chemistry. 2020;331:127355. doi:10.1016/j.foodchem.2020.127355 .
He, Weiyi, Zhang, Tingting, Ćirković-Veličković, Tanja, Li, Shuiming, Lyu, Yansi, Wang, Linlin, Yi, Jiang, Liu, Zhigang, He, Zhendan, Wu, Xuli, "Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut" in Food Chemistry, 331 (2020):127355, https://doi.org/10.1016/j.foodchem.2020.127355 . .