Mechanism of the Reduced IgG/IgE Binding Abilities of Glycated β-Lactoglobulin and Its Digests through High-Resolution Mass Spectrometry.

Glycation between proteins and reducing sugars is the common chemical modification in food protein, and many studies have focused on the allergenicity of the glycated protein. However, a systemic study on the allergenicity change of its digests is lacking. In this work, we explored the change rule of the digestibility and allergenicity of glycated β-Lg during gastrointestinal digestion and interpreted the mechanism using high-resolution mass spectrometry. Glycation with arabinose increased the resistance of β-Lg to digestive enzyme, with a low hydrolysis value. Indirect competitive ELISA showed that the IgG/IgE binding rates of β-Lg were reduced after glycation and further reduced after digestion, in comparison with the digests of unglycated β-Lg. There are two reasons for this phenomenon. On the one hand, 11 glycated sites were determined in the lowest allergenicity arabinose-β-Lg conjugation (Ara-β-Lg), which was distributed in the IgG and IgE linear allergic epitopes of β-Lg. On the other hand, glycation masking linear allergenic epitopes had a more significant effect on reducing allergenicity in comparison to digestive enzyme hydrolysis. These results indicated that the allergenicity of Ara-β-Lg in the human body might be lower than that of unglycated β-Lg.