Thermal and Functional Properties of Porcine Sarcoplasmic Proteins: A Comparison with Some Wateroluble Animal Proteins

Abstract

To understand the thermal and functional properties of porcine sarcoplasmic proteins (SP), the gelation and emulsion properties were compared with those of porcine blood plasma (BP), egg albumin (EA) and whey protein isolates (WPI). Differential scanning calorimetric analysis showed that the denaturation temperature of SP was lower than the other proteins. The solubility of SP decreased at above 60°C. On the other hand, those of BP and EA decreased at above 70°C and that of WPI decreased at above 80°C. The surface hydrophobicity of SP greatly increased after heating. Thermal gelation of more than 1% SP occurred at 80°C for 30min. But at 5% protein concentration, the gel strength of SP was lowest among all proteins used. The stability of SP emulsion heated was higher than those of any other proteins'emulsions. The fat binding capacity of SP was higher after that of BP. These results suggested that functional properties of SP would affect textural properties of emulsion type food like sausage and meat patties.