## 3 Results and Discussion  
The Influence of Pre-Treatment of the Protein Dispersions on the Properties of the CPC-Stabilized Emulsions  
Protein-stabilized emulsion formation by homogenization is widely used in both scientific research and the food industry to increase both protein solubility as well as emulsion stability [37]. According to [PERSON] et al. [38], non-thermal methods like high-pressure or high-hydrostatic pressure processing enhance the rheological, thermal, and functional properties of legume proteins with minimal effect on macro- and micronutrients and properties related to swallowing and digestion. Literature data indicate that both the high pressure and the number of passes through the homogenizer affect the physicochemical and functional properties of emulsions, as well as their stability [33; 34; 39; 40]; but it should be emphasized that HPH-induced effects are strongly dependent on matrix characteristics and treatment conditions [41]. In the protein-stabilized emulsion, as a result of high-pressure treatment, in addition to the reduction in size and homogeneity of the fat globules, there may also be protein unfolding and exposure of some reactive groups, such as free sulfhydryl and hydrophobic groups, thus further enhancing the functionality of proteins [39]. According to [PERSON] et al. [41], as HPH intensity increased, protein unfolding was favored, leading to increased solubility and oil-holding capacity and consequently to obtaining a novel plant-protein-based ingredient with improved techno-functionalities and digestibility, but over-processing conditions caused further protein aggregation and a general reduction in functionalities. In the present study, we prepared emulsions in HP homogenizer, but due to the limited solubility of legume proteins in water, it was also examined whether the number of passes of the protein dispersions through the two-stage HP homogenizer (50 MPa and 5 MPa at the first and second stages, respectively) affects the properties of the emulsions. The particle size distribution (PSD) (in cumulative and histogram forms) of chickpea protein dispersions, \(C_{\mathrm{s}}\) and \(C_{\mathrm{g}}\), passed once and twice through an HP homogenizer, is presented in Figure S1a, and the PSD of the e\(C_{\mathrm{s}}\) and e\(C_{\mathrm{g}}\) emulsions produced using these protein dispersions is shown in Figure S1b. The obtained granulometric curves of \(C_{\mathrm{s}}\) and \(C_{\mathrm{g}}\) clearly indicated that repeating the homogenization operation resulted in both a shift in PSD towards smaller particles, as well as a change in the shape of the histogram curve (Figure S1a). For \(C_{\mathrm{s}}\), the coarse particle fraction in the range of 20 to 100 \(\upmu\)m was redistributed as a result of second homogenization, and the three-modal histogram took a bimodal form with similar values of two modes of the smaller fractions in the range of 1 to 20 \(\upmu\)m and 0.1 to 1 \(\upmu\)m. The PSD curves of the \(C_{\mathrm{g}}\) were characterized by a bimodal shape with the main peak of the finer fraction in the range of 1 to 10 \(\upmu\)m and a clear decrease in the modal values as a result of repeated homogenization. The comparison of the corresponding curves obtained for the emulsions indicated that the PSD of e\(C_{\mathrm{s}}\) and e\(C_{\mathrm{g}}\) was highly consistent with respect to the protein dispersions, which was illustrated by the similar shape of the granulometric curves. The granulometric curves of the e\(C_{\mathrm{g}}\) indicated a strongly monomodal distribution in the \(<\)5 \(\upmu\)m range. The three-modal PSD of the e\(C_{\mathrm{s}}\) showed a fraction of fine particles in the range of 0.1 to 1 \(\upmu\)m as well as two fractions of coarse particles in the range of a few to over 100 \(\upmu\)m (Figure S1b). The ANOVA analysis showed that the type of protein concentrate (standard CPC or gelling CPC) turned out to be a factor significantly differentiating all parameters of the PSD, both the protein dispersions and the emulsions (Table S1).