| Capillary zone electrophoresis was used to characterize soluble gluten proteins extracted from six different commercial wheat samples (with protein content varying from 8 to 13%). The objective of this study was to describe qualitatively separation patterns of wheat gluten treated with four different levels of DATEM (0, 0.3, 0.6 and 1.0%) and changes in proteins solubility, interactions and charge/mass ratio. Three different groups named A, B and C based on their migration profile were observed where group A represents positively charged peptides with the largest charge to mass ratios, group B represents positively charged peptides with reduced ratios, and finally group C are anions with greater ratios. DATEM's ability to induce changes in protein conformation was observed by (i) decrease in maximum peak intensity and (ii) an increase in resolution of peaks. DATEM decreases protein solubility at a concentration of 0.6% for flour 1C, 4C and 6C and 0.3% for flour 2C and 5C. DATEM's ability to increase interactions between gluten proteins, resulting in change in charge/mass ratio is flour dependent. However, flour 6C displayed a reversal in solubility at 1.0%, suggesting that DATEM at critical levels forms micelles, which leads to reduced interactions of DATEM with gluten. A proposed general mechanism by which DATEM influences overall protein spatial conformation is explained by a four and two stage model. |
