The Influence of pH on the Emulsification Properties of Heated Whey Protein-Pectin Complexes

Interactions between proteins and polysaccharides could improve protein functional properties. Most studies focus on the formation of complex coacervates at pHs < pI. Much less attention has been given to the interactions at pHs > pI, especially when the mixtures are heated. The objective of this study was to investigate the emulsification properties of heated whey protein isolate (WPI) and pectin complexes formed at near neutral pHs. Heated soluble complexes (Cpxs) were formed by heating mixed WPI (3 wt% protein) and pectin (0 to 0.60 wt%) at pH 6.0, 6.5, or 7.0 at 85 °C for 30 min. Emulsions (5 wt% oil, 0.5 wt% protein, and pH 5.5) were characterized by measuring droplet size, zeta potential, rheological properties, and creaming stability. The results showed that, regardless of heating pH, Cpxs formed more stable emulsions with significantly smaller droplet sizes, higher negative charges, and less shear-thinning behavior in comparison to emulsions stabilized by heated WPI (p < 0.05). At fixed pectin concentrations, the emulsions stabilized by Cpx formed at pH 7.0 were the most stable. Increasing pectin concentrations led to a decrease in mean droplet sizes and an increase in negative charge. Maximum stability was achieved with the emulsion stabilized by Cpx formed with 0.60 wt% pectin at pH 7.0. The formation of Cpxs under proper conditions will allow for the utilization of WPI in a wider range of applications and fulfill the consumer need for clean label food products.