Abstract
The wheat proteins soluble in chloroform-methanol mixtures are associated with several kinds of food allergies. A separation method based on capillary zone electrophoresis (CZE) with UV detection was developed for the analysis of these mixtures. An acidic phosphoric acid/β-alanine (pH 2.5) buffer containing HPMC, urea and acetonitrile was used for the separation. The capillary electrophoresis (CE) was able to complete the analysis in six minutes. The electrophoregrams of extracts of both durum and common wheat commercial cultivars were compared. The registered cultivar (cv.) Kamut® was included as a representative of rustic cereal species. A different number of peaks were detected in the profile relative to the tetraploid and exaploid analyzed cultivars. Three main peaks were observed for all tetraploid cultivars, while four peaks were detected for the common wheat cultivars. The peak corresponding to the α-amylase inhibitor type III was identified in the common wheat electrophoregram. The possibility of quantitative determination of this inhibitor has been investigated.
Highlights
Among the cereal crops, wheat is the most widely grown
More detailed information on wheat allergens is of great importance for the development of both less allergenic flours and better diagnostic tools
The aim of the present investigation was to develop a reliable method based on capillary zone electrophoresis (CZE) that will provide reproducible and quantitative measures of the wheat grain proteins soluble in chloroform/methanol mixture, some of which are relevant for wheat food allergy
Summary
Wheat is the most widely grown. Much of the world production is consumed by humans after processing to bread, pasta, biscuits, noodles, etc. Capillary zone electrophoresis (CZE) has been extensively applied to the analysis of wheat protein fractions (i.e., gliadins, glutenins and albumins) [11,12,13] for identifying grain variety by comparing the electrophoregrams [14], to investigate the variation of protein profiles within germplasm collections [15], to study the rate of protein accumulation in kernels [16,17], and so on Despite this great versatility of CE in terms of efficiency and speed of analysis to investigate the different wheat protein fractions, no protocol exists for the investigation of the CM protein fraction. The aim of the present investigation was to develop a reliable method based on CZE that will provide reproducible and quantitative measures of the wheat grain proteins soluble in chloroform/methanol mixture, some of which are relevant for wheat food allergy
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