Investigation into IgG/IgE binding capacity and gut microbiota of digestion products derived from glycated ovalbumin

Gut microbiota plays an important role in food allergy. The immunoglobulin G (IgG)/immunoglobulin E (IgE) binding capacity and human gut microbiota changes of digestion products derived from glycated ovalbumin (OVA) were investigated. Gastrointestinal digestion effectively destroyed the primary structure of glycated OVA, resulting in a significantly higher digestibility than gastric digestion, and more abundant peptides < 3 kDa. Moreover, gastric and gastrointestinal digestion products have different fluorescence quenching and red shift of fluorescence peaks, and possess different conformational structures. These changes resulted in a decrease in 28.7 % of the IgE binding capacity of gastrointestinal digestion products beyond that of pepsin. Moreover, gastrointestinal digestion products of glycated OVA increased significantly the proportion of Subdoligranulum , Collinsella , and Bifidobacterium . Therefore, gastrointestinal digestion products of glycated OVA altered human intestinal microbiota, reducing the risk of potential allergy.