Effect of pH on Structural Properties of Heat-Induced Whey Protein Gels

Abstract

Formation and structure of whey protein heat-induced gels (100 mg mL^-1) through heat treatment at 80 ^°C and pH modifications at three pH values of acidic (2), isoelectric (5.6) and neutral (7) were studied. The obtained results indicated that the nature of the primary gel networks was different at each pH value. The heat-induced gels produced at pH of 2 and 7, had acceptable overall shape and consistency which confirmed the significant effect of pH on the regular gel structures. Conversely, the amorphous gel structure was observed at isoelectric pH. According to Atomic Force Microscopy images, the structural unfolding of the protein during denaturation and formation of the fibrillar structures was observed in gel at pH of 2 and stranded aggregates at pH of 7. In terms of textural analysis, in samples at pH of 2 and 7, the required force to fracture gel structure was approximately equal and less than that of the sample at pH of 5.6 which goes back to the amorphous large protein aggregates in gel network at isoelectric pH. The ordered, regular and stable gel structures and high ionic balance were reflected in color parameters and lower amounts of moisture content in the gel matrix of samples at pH of 2 and 7 (P<0.05). The well-organized structure and stable gels network along with their desirable functional characteristics, might reinforce their application as food ingredients in terms of improving the qualitative and textural qualities of food products. This property can facilitate the use of these protein gels in novel food systems.