期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 63, 期 10, 页码 2660-2667出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf505461x
关键词
alpha-amylase/trypsin inhibitor; brush border membrane; celiac disease; gluten; in vitro human digestion; nsLTP; pasta; wheat allergy
资金
- BBSRC through an Institute Strategic Programme Grant [BB/J004545/1]
- EU [COST FA 1005]
- Italian Ministry of Economy and Finance
- ENEA [191/2009]
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 gastroduodenal hydrolysis, while other digestion-stable allergens such as alpha-amylase/trypsin inhibitors were not detected being totally released in the pasta cooking water. To simulate the final stage of intestinal degradation, the gastroduodenal 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.
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