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J Agric Food Chem. 2015 Mar 18;63(10):2660-7. doi: 10.1021/jf505461x. Epub 2015 Mar 5.

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

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†Istituto di Scienze dell'Alimentazione, Consiglio Nazionale delle Ricerche, via Roma 64, 83100 Avellino, Italy.
‡Dipartimento di Agraria, Università Federico II, via Università 100, 80055 Portici, Napoli, Italy.
§Institute of Food Research, Norwich Research Park, Norwich, Norfolk NR4 7UA, United Kingdom.


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 oral-gastro-duodenal digestion. The course of pasta protein digestion was monitored by SDS-PAGE, and gluten proteins were specifically analyzed by Western blot using sera of celiac patients. Among the allergens, nonspecific lipid-transfer protein was highly resistant to gastro-duodenal hydrolysis, while other digestion-stable allergens such as α-amylase/trypsin inhibitors were not detected being totally released in the pasta cooking water. To simulate the final stage of intestinal degradation, the gastro-duodenal digesta were incubated with porcine jejunal brush-border membrane hydrolases. Sixty-one peptides surviving the brush-border membrane 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.


alpha-amylase/trypsin inhibitor; brush border membrane; celiac disease; gluten; in vitro human digestion; nsLTP; pasta; wheat allergy

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