Heat-induced gelation of porcine blood plasma proteins as affected by pH.

Porcine plasma is a by-product of the meat industry that can be used as a food ingredient. It is a protein mixture, hence its composition can be modified to meet specific functionality requirements. In the present paper, the gelation properties of plasma and its two major fractions (serum and albumin) have been studied at pH 4.5, 6.0 and 7.5. Polyacrylamide gel electrophoresis (SDS-PAGE) revealed that albumin was the constituent that remained soluble to a larger extent during heat-treatments, and that acidic coagulation occurred at pH 4.5, making weak interactions the predominating ones between protein aggregates. Differential scanning calorimetry (DSC) and rheological tests showed that both the thermal stability and the gelation point of protein solutions were lower as pH decreased. The textural properties and water-holding capacities of plasma and albumin gels were more pH-dependent than serum. Albumin gels were the weakest and those of plasma at pH 7.5, the strongest. It has been determined that interactions between protein fractions play a key role in the gelling properties due to synergistic effects. This knowledge should be useful in the engineering of a plasma derivative product designed for specific food requirements, by reformulating its natural composition and enhanced by controlling pH.