Relation Between Gelation Behavior of Ground Chicken Muscle and Soybean Proteins and Their Differential Scanning Calorimetric Studies

Abstract
The thermal denaturation of ground chicken muscle, soybean protein, and the mixture of both were investigated by differential scanning calorimetry (DSC) under different salt concentration. The relationship between DSC analysis and the properties of heat‐induced gels from these samples were determined. The DSC thermograms of ground chicken muscle showed three endothermic peaks and those of soybean protein showed two peaks. The DSC thermogram of their mixture showed three peaks. When NaCl was added to ground chicken muscle the endothermic peaks shifted to lower temperatures and the rheological values of heat‐induced gels increased. When NaCl was added to soybean protein, the endothermic peaks shifted to higher temperatures and the rheological values of heat‐induced gels decreased.