Effect of pH on the emulsifying performance of protein-polysaccharide complexes

Protein-polysaccharide complexes have been successfully used for emulsion stabilization. However, it is unclear how the complex's surface charge influences aggregation stability and coalescence stability of emulsions, and whether a low charged interfacial film can still maintain the coalescence stability of oil droplets. In the present study, the effects of pH (around the pI of protein) on the aggregation and coalescence stability of emulsions were investigated.

Whey protein isolate (WPI) and peach gum polysaccharides (PGP) complexes (WPI-PGP complexes) were synthesized at pH 3, 4 and 5. Their sizes were 598, 274 and 183 nm, respectively, and their ζ-potentials were +2.9, -8.6 and -22.8 mV, respectively. Interface rheological experiments showed that WPI-PGP complex at pH 3 had the lowest interfacial tension, and formed the softest film compared to the complexes at pH 4 and 5. Microfluidic experiments showed that all WPI-PGP complexes were able to stabilize droplets against coalescence within short timescales (milliseconds). At pH 3, no coalescence was observed even under conditions where the continuous phase flow influenced the shape of oil droplets (from spheres to ellipsoids). At pH 4 and 5, the model emulsions were stable over 16 days of storage, extensive aggregation and creaming occurred at pH 3 after 8 days. Importantly, no coalescence took place.

The present study confirmed that the aggregation stability of the emulsions was mainly determined by the surface charge of the complex, whereas the coalescence stability of emulsions is expectedly determined by steric repulsion, providing new insights into how to prepare stable food emulsions. © 2024 Society of Chemical Industry.