Salt and pH-Induced Attractive Interactions on the Rheology of Food Protein-Stabilized Nanoemulsions.

This research aimed to investigate the possibility of forming gelled nanoemulsions (NEs) by inducing attractive interactions among the nanodroplets. The effect of salt concentration and changes in pH on the stability and gelation behavior of 2, 4, and 5% sodium caseinate (SC) and whey protein isolate (WPI)-stabilized 40% canola oil-in-water NEs were investigated. For the effect of salt, sodium chloride was added in a concentration of 0.1, 0.5, and 1 M in the continuous phase of the NEs at neutral pH, whereas to study the effect of acidification, the pH of the NEs was adjusted to the isoelectric point (pI) of the proteins. The addition of salt led to attractive gelation in WPI NEs because of a screening of charge. In contrast, the gel strength of SC-stabilized NEs was reduced with salt, which was attributed to the loss of close packing of droplets and their surrounding repulsive barriers because of charge screening and to the steric barrier of interfacial SC preventing droplet aggregation. All the NEs with pH at the pI of proteins transformed into strong attractive gels made of droplet aggregates irrespective of the type or concentration of protein because of the complete charge neutralization. The strength of the acidified NE gels increased with a decrease in droplet size and the type of protein used. Overall, research on the effect of different environmental factors on the stability and gelation behavior of protein-stabilized NEs could be useful for possible applications of these nanoscale materials in various food systems.