Tracking the fate of pasta (T. durum semolina) immunogenic proteins by in vitro simulated digestion.

The aim of the present study was to identify and characterize the celiacogenic/immunogenic proteins and peptides released during digestion of pasta (Triticum durum semolina). Cooked pasta was digested using a harmonized in vitro static model of the oral-gastro-intestinal digestion. The course of pasta protein digestion was monitored by SDS-PAGE, and gluten proteins were specifically analysed by Western-blot using sera of celiac patients. Among the allergens, non specific-lipid transfer protein was highly resistant to gastrointestinal hydrolysis, while other digestion stable allergens such as ?-amylase/trypsin-inhibitors were not detected being totally released in the pasta cooking water. To simulate the final stage of the intestinal degradation, the gastrointestinal digesta were incubated with porcine jejunal brush border membrane (BBM) hydrolases. Sixty-one peptides surviving the BBM peptidases were identified by liquid chromatography-mass spectrometry, including several gluten-derived sequences encrypting different motifs responsible for the induction of celiac disease. These results provide new insights into the persistence of wheat-derived peptides during digestion of cooked pasta samples.