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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.

Author information

1
†Istituto di Scienze dell'Alimentazione, Consiglio Nazionale delle Ricerche, via Roma 64, 83100 Avellino, Italy.
2
‡Dipartimento di Agraria, Università Federico II, via Università 100, 80055 Portici, Napoli, Italy.
3
§Institute of Food Research, Norwich Research Park, Norwich, Norfolk NR4 7UA, United Kingdom.

Abstract

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.

KEYWORDS:

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

PMID:
25682706
DOI:
10.1021/jf505461x
[Indexed for MEDLINE]

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