## 3 Results and Discussion
### Emulsion Stability
#### 3.2.2 Heat- and Salt-Treated CPC-Stabilized Oil-in-Water Emulsions  
The method applied for the preparation of the protein powders, including isolation and recovery, affects their functional properties, in particular solubility [14]. In the present study, the commercial CPC powders despite the similar amino profile differed in the pH of their aqueous dispersions. The pH of the standard CPC water dispersion (-6.5) was closer to the pH of chickpea proteins (reported as 4.49 [19]) than the pH of gelling CPC (pH-7.5). The pH 7.5 is relatively distant above the pH of globulins, which promotes solubility through electrostatic repulsion and hydration of charged residues [20]. Therefore, both the properties and the stability of the emulsions obtained on the basis of these concentrates differed significantly (as described above). It was hypothesized that the influence of external factors on the properties and stability of the emulsion would also be different depending on the concentrate used for their stabilization. The stability of eCg and eCg after (a) heating at 95 \({}^{\circ}\)C, (b) addition of 0.1 M NaCl, and (c) heating up to 95 \({}^{\circ}\)C in the presence of 0.1 M NaCl was examined. Emulsions Stabilized by Gelling CPC  
For eCg, the presence of salt ions (Na+Cl-) had a stabilizing effect on the emulsion (\(TSI<3\) after 28 days of storage) (Table 1), prevented creaming (Figure 1b,d), and reduced the kinetics of destabilization (Figure S2a). Unheated eCg with 0.1 M NaCl (eCgN) was shear-thinning (\(n<1\)) fluid of higher viscosity than eCg (Table 2) and possible tendency to flocculation and syneresis manifested by the decrease in \(BS\) in the upper part of the measuring vial (Figure 1b) with a slight increase in \(d_{43}\) and \(spun\) (Table 1). It is a known phenomenon that salt addition produces a progressive increase in viscous and viscoelastic parameters, leading to improved stability against creaming without a significant influence on droplet size distribution [52]. A significant increase in \(d_{43}\) (Table 1) and three-modal PSD with the main fraction particles in the range of a few dozen to over 100 \(\upmu\)m for eCg heated in the presence of NaCl (eCgNT) (Figure S3a) accompanied by stabilization of the system (Figure 1b, Figure S2a) may indicate the formation of the gel structure. This assumption was confirmed by confocal microscopy images of the emulsion. The structure of eCg significantly changed after heating in the presence of NaCl, extensive droplet aggregation occurred, and a network of aggregated protein-stabilized emulsion droplets was created (Figure S4c). Similar results were presented by [PERSON] et al. [53] for soy protein-stabilized oil-in-water emulsions (pH 7.0) in the presence of 100 mM NaCl and exposed to high temperature (90 \({}^{\circ}\)C). Under the combined effect of salt and high temperature, the adsorbed proteins underwent a conformational change that led to increased exposure of non-polar groups. The hydrophobic attraction between the soy protein-coated oil droplets was high enough to overcome the electrostatic repulsion. In the present study, the network of aggregated protein-stabilized emulsion droplets was created as a result of two mutually reinforcing phenomena: (1) The presence of monovalent ions probably reduced the thickness of the electric double layer around the adsorbed and non-adsorbed proteins and, thus, also reduced the effective repulsion between the negatively charged oil droplets, facilitating aggregation (a relatively high ionic strength, 0.1 M NaCl, was used in these experiments to screen electrostatic effects). (2) Heat denaturation of globular proteins accompanied by the exposure of hydrophobic groups could facilitate depletion flocculation between droplets. Dietary proteins typically unfold and expose non-polar groups above 50 \({}^{\circ}\)C leading to protein aggregation and precipitation through hydrophobic and covalent interactions [20]. [PERSON] et al.