Owing to its extensive use in human diet, wheat is among the most common causes of food-related allergies and intolerances. Gluten proteins and particularly the gliadin fractions represent the main factor triggering celiac disease. Given the extremely high structural heterogeneity of gliadins, generated by amino acid insertions, deletions and substitutions, the physico-chemical properties of gliadins can vary significantly among wheat genotypes (species, cultivars and breeding lines) influencing in parallel the immunoreactive properties and the susceptibility to enzymatic treatment [1]. Therefore, the structural characterization and the correlation with relevant toxicity, by tracking the fate upon gastrointestinal digestion of wheat-based commodities [2], gains significance to deepen the knowledge at the molecular level of the immunological pathway and to identify naturally low toxic wheat species and/or efficient detoxification technologies. Recent development in proteomics have contributed to give insights in this field, although the analytical capabilities of the proteomic approach are challenged by the complexity of the wheat seed proteome and particularly of the gluten protein fraction. Limited database entries available, complexity arising from sets of homologue proteins, large occurrence of repeated motifs, very low number of basic residues for tryptic hydrolysis represent drawbacks that complicate the comprehensive proteomic cataloguing of the gluten proteins. These challenging issues can only be addressed by the use of integrated, up-to-date analytical approaches, which together constitute the platform of modern food proteomics, and where a pivotal role is played by mass spectrometry.
Challenges in food proteomics for the selection of low toxicity wheat genotypes towards celiac disease patients
R Pilolli;L Monaci
2015
Abstract
Owing to its extensive use in human diet, wheat is among the most common causes of food-related allergies and intolerances. Gluten proteins and particularly the gliadin fractions represent the main factor triggering celiac disease. Given the extremely high structural heterogeneity of gliadins, generated by amino acid insertions, deletions and substitutions, the physico-chemical properties of gliadins can vary significantly among wheat genotypes (species, cultivars and breeding lines) influencing in parallel the immunoreactive properties and the susceptibility to enzymatic treatment [1]. Therefore, the structural characterization and the correlation with relevant toxicity, by tracking the fate upon gastrointestinal digestion of wheat-based commodities [2], gains significance to deepen the knowledge at the molecular level of the immunological pathway and to identify naturally low toxic wheat species and/or efficient detoxification technologies. Recent development in proteomics have contributed to give insights in this field, although the analytical capabilities of the proteomic approach are challenged by the complexity of the wheat seed proteome and particularly of the gluten protein fraction. Limited database entries available, complexity arising from sets of homologue proteins, large occurrence of repeated motifs, very low number of basic residues for tryptic hydrolysis represent drawbacks that complicate the comprehensive proteomic cataloguing of the gluten proteins. These challenging issues can only be addressed by the use of integrated, up-to-date analytical approaches, which together constitute the platform of modern food proteomics, and where a pivotal role is played by mass spectrometry.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
