Rheological properties of Uzbekistan wheat gluten as a function of disulfide and h-bond contents during conditioning

Rheological properties of wheat gluten as a function of the presence of free sulfhydryls and disulfide bonds in addition to their ratio during various conditioning regimes were studied. It was shown that coagulation of the gluten as the temperature increased was accompanied by a decrease in the number of free sulfhydryls and an increase in the number of rheologically active disulfide bonds. Changes occurring in the gliadin and glutenin fractions during various conditioning regimes were seen using IR spectroscopy. It was found that the relative strength of absorption bands due to H-bonds increased as the treatment temperature was raised above 60°C. Significant changes in the protein molecule structure that caused substantial changes in its rheological properties because of thiol-disulfide exchange reactions and H-bond strength occurred during the conditioning.