Journal
FOOD CHEMISTRY
Volume 372, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.131308
Keywords
Phosphorylation; Bovine alpha-lactalbumin; Simulated in vitro digestion; Allergenicity; Digestive products
Funding
- Science Foundation for Young Scientists of Jiangxi Province [20202BABL215027]
- Chinese National Natural Science Foundation [31960457]
- Young Talent Cultivation Program of Jiangxi Normal University
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The study found that phosphorylation before digestion can significantly reduce the allergenicity of bovine α-lactalbumin, decrease allergic responses and related indicators, and help reduce allergic activity.
The effects of phosphorylation on the allergenicity of bovine a-lactalbumin (BLA) and digestive products were studied in vitro digestion. Two components with different molecular weight and conformation were obtained from natural and phosphorylated BLA. In vivo and in vitro assessment of allergenicity showed that phosphorylation prior to digestion significantly decreased the IgE/IgG binding capacity and allergic response in KU812 cells, and reduced the levels of IgG, IgE, IL-4 and histamine, with an increase in IFN-. levels in mouse serum, depending on the changes in BLA structures, producing numerous small peptides. There were four phosphorylated sites (S22, T29, S47 and S70) in the high molecular weight components of phosphorylated BLA after digestion. These phosphorylated sites could mask the linear epitopes of digestive products, resulting in reduced allergic activity. Phosphorylation prior to digestion of dairy products can reduce the risk of anaphylaxis in patients with milk allergy to some extent.
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