## 3 Results and Discussion
### Emulsion Stability
#### 3.2.2 Heat- and Salt-Treated CPC-Stabilized Oil-in-Water Emulsions
[54] claimed that chicken protein concentration above 1.5% promotes depletion flocculation, as the water-oil interface is already saturated by protein molecules. In turn, [PERSON] and co-workers [55] suggest a concentration of 1% as the interface saturation point in lentil protein-stabilized emulsion with an oil fraction of 10%. Therefore, it can be assumed that, in the present study, the continuous phase contained a fraction of the non-adsorbed protein, as the oil phase content was fixed at 3.2% with a balanced ratio of protein concentrate to oil (1:1 \(w/w\)). In our previous study [33], we have shown that when the whey protein-coated droplets in oil-in-water emulsions (prepared in the same way as eC\({}_{\mathrm{s}}\) and eC\({}_{\mathrm{g}}\)) are in close proximity and/or the continuous phase contains a fraction of the non-adsorbed protein, the emulsion gelation may occur. Shear rheological properties indicated that eC\({}_{\mathrm{g}}\) with 0.1 M NaCl yielded shear-thinning fluids of very high viscosity (\(\eta\) = 60.13 mPa\(\cdot\)s) if it was additionally heated (Table 2). The data were fitted to the Herschel-Bulkley model, and the obtained values of yield stress and consistency index were very high. Also in the case of the chickpea protein dispersion, after heating with 0.1 M NaCl, a similar trend was observed with \(k\) and \(\tau_{0}\) having lower values, as well as the viscosity and VRI (Table S2) than those of the corresponding emulsions. The presented results are in accordance with the findings of [PERSON] et al. [56] for systems in which an oil acted as an active filler, and the increased \(\tau_{0}\) and \(k\) parameters corresponded to increased resistance to shear and reinforcement of the structure in the continuous phase. It should be noted that heating alone did not improve the eC\({}_{\mathrm{g}}\) stability. The _TSI_ values of the heated emulsions were slightly higher than those for unheated ones (Table 1, Figure S2a), and the same destabilization mechanism was observed (Figure 1a,c)--creaming during 28 days of storage. Also, the shear rheological properties remained practically unchanged (Table 2), and the eC\({}_{\mathrm{g}}\) was still a low-viscosity Newtonian fluid after heating with slightly higher \(d_{43}\) and _span_ values (Table 1). It can be concluded that at high temperatures, despite the unfolding of proteins and the exposure of their hydrophobic parts, the electrostatic repulsion was large enough to overcome attractive interactions between protein molecules enabling the creation of a network of spatial connections. Similar results have been reported previously for soy protein-stabilized emulsions [52]. Emulsions Stabilized by Standard CPC  
The unsatisfactory stability of eC\({}_{\mathrm{s}}\) was initially improved after heat- and/or salt treatment (from D to C category of _TSI_ after 1 day) (Table 1). However, the obtained _TSI_ values after 7 days (Table 1) and the presented destabilization kinetics (Figure S2b) indicate that in the long term, it was heating (with or without salt) rather than the presence of salt that caused the _TSI_ to be lowered. As for eC\({}_{\mathrm{g}}\), the addition of 0.1 M NaCl prevented creaming (Figure 1f) and also reduced sedimentation if the emulsion was additionally heated (Figure 1h). However, unheated eC\({}_{\mathrm{s}}\) with 0.1 M NaCl was the least stable over the 28-day period (Figure S2b). In the presence of salt, a clear layer was formed in the upper part of the emulsions (Figure S5b), which resulted in receiving transmission signals at a height of more than 30 mm (Figure S6a), or more than 36 mm if the emulsion was additionally heated (Figure S6b). The separation of the emulsion in the presence of salt into two phases during storage may indicate dehydration by salting-out. In the presence of dissociated Na\({}^{+}\) and Cl\({}^{-}\) ions, the solubility of the protein decreased as a result of competition with salt ions for interaction with the solvent molecules, which led to protein precipitation over a long period of storage.