Simulated in vitro digestion of α-lactalbumin modified by phosphorylation: Detection of digestive products and allergenicity

• Published in: Food chemistry 2022-03, Vol.372, p.131308-131308, Article 131308
• Main Authors: Chen, Wen-mei, Shao, Yan-hong, Wang, Zhi, Liu, Jun, Tu, Zong-cai
• Format: Article
• Language: English
• Subjects: Allergenicity; Allergens; Animals; Bovine α-lactalbumin; Cattle; Digestion; Digestive products; Immunoglobulin E; Lactalbumin; Mice; Phosphorylation; Simulated in vitro digestion
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2021.131308

[Display omitted] •Phosphorylation combined with enzymic hydrolysis decreased α-lactalbumin allergenicity.•Isolation and identification of peptides derived from phosphorylated α -lactalbumin digestion.•Phosphorylated sites masked the allergic areas of the digestive products. The effects of phosphorylation on the allergenicity of bovine α-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-γ 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.