Investigation into potential allergenicity of DBD plasma-treated casein digestion products based on immunoglobulin E linear epitopes and the sensitized-cell model

The study aimed to investigate the allergenicity change in casein treated with dielectric barrier discharge (DBD) plasma during in vitro simulated digestion, focusing on the immunoglobulin E (IgE) linear epitopes and utilizing a sensitized-cell model. Results indicated that prior treatment with DBD...

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Veröffentlicht in:Food chemistry 2024-07, Vol.447, p.138940-138940, Article 138940
Hauptverfasser: Zhang, Yongniu, Ren, Er-Fang, Wen, Tao, Lyu, Shijun, Gai, Lili, Chen, Siyu, Li, Kai, Han, Zhong, Niu, Fuge, Niu, Debao
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Sprache:eng
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Zusammenfassung:The study aimed to investigate the allergenicity change in casein treated with dielectric barrier discharge (DBD) plasma during in vitro simulated digestion, focusing on the immunoglobulin E (IgE) linear epitopes and utilizing a sensitized-cell model. Results indicated that prior treatment with DBD plasma treatment (4 min) before simulated digestion led to a 10.5% reduction in the IgE-binding capacity of casein digestion products. Moreover, the release of biologically active substances induced from KU812 cells, including β-HEX release rate, human histamine, IL-4, IL-6, and TNF-α, decreased by 2.1, 28.1, 20.6, 11.6, and 17.3%, respectively. Through a combined analysis of LC-MS/MS and immunoinformatics tools, it was revealed that DBD plasma treatment promoted the degradation of the IgE linear epitopes of casein during digestion, particularly those located in the α-helix region of αs1-CN and αs2-CN. These findings suggest that DBD plasma treatment prior to digestion may alleviate casein allergic reactions. [Display omitted] •Plasma treatment reduces the allergenicity of casein after digestion.•KU812 degranulation was inhibited by plasma-treated casein after digestion.•Five critical amino acids for casein IgE linear epitopes were predicted.•Plasma treatment promoted the epitope degradation of casein during digestion.•Epitope degradation in the α-helix region of αs1-CN and αs2-CN is dominant.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2024.138940