## 3 Results and Discussion
### Emulsifying Properties  
The emulsion activity index (EAI) and emulsion stability are two key parameters for the emulsifying properties of proteins. EAI is a measure of the ability of emulsifiers to form an emulsion, while emulsion stability evaluates the capacity of the emulsifier to stabilize the emulsion within a given time period [17; 46]. The emulsion activity and emulsion stability of the different protein mixtures are shown in Figure 1. Treatment T2 with 100% lentils showed the highest emulsifying activity, followed by T4 and T8, which have a higher proportion of lentils in the formulation. The emulsifying properties of plant proteins are intrinsically linked to their amphiphilic nature, which connects hydrophilic and hydrophobic areas and thus facilitates interaction at the water-oil interfaces. Hydrophobicity allows the proteins to accumulate in the oil phase, while hydrophilicity promotes adsorption in the aqueous phase. Once adsorbed, the proteins reduce the interfacial tension and stabilize the emulsion by forming a viscoelastic layer that prevents the droplets from coalescing [22; 47]. Protein adsorption at the interface generally occurs in two stages. First, the proteins migrate and bind at the oil-water interface [48]. Once the protein molecules are transported and bound to the interface, their hydrophobic part promotes adsorption. Lentil protein has a higher hydrophobicity [49] compared to pea and fava bean protein, which could explain its greater activity at the surface to form the emulsion. However, its stabilizing effect is low. Ref. [45] observed that pea protein was able to stabilize the emulsion longer than lentil protein. It has been suggested that this phenomenon is related to the high negative charge on the surface of the pea protein that coats the oil droplets. Previous studies with pea, lentil, and bean proteins at a pH of 7 gave EAI and ESI values for fava beans: 8 m\({}^{2}\)/g, 14 [41], 28 m\({}^{2}\)/g, 25 min [50]; lentil protein: 18 to 25 m\({}^{2}\)/g, 12 to 18 min [37]; and pea protein: 13.1 to 14.1 m\({}^{2}\)/g, 53 to 95 min [51], 19.3 \(\pm\) 0.2 m\({}^{2}\)/g, 61.6 \(\pm\) 0.2 min [52]. The values found in this work are consistent with those in the literature. Lentil protein in combination with pea protein showed better ESI average values, while T5, a combination of pea and fava protein in equal amounts, showed lower average values than pea and fava protein alone.  
The T10 mixture (Figure 1) showed better results in terms of the emulsifying and stabilizing effect of the final emulsion. The combination in equal proportions favored both EAI and ESI. Lentil proteins are believed to be responsible for the rapid adsorption at the interface. Lentil proteins usually have a considerable amount of hydrophilic amino acid residues, such as glutamine/glutamic acid, asparagine/aspartic acid, lysine, and arginine [37], which contribute to hydrogen bonds and electrostatic interactions [53] Since pea and bean proteins are more soluble, they can stabilize the emulsion [49; 54]. Due to the higher solubility of proteins, more solubilized proteins can be rapidly adsorbed at the oil-water interface, which facilitates the formation of densely packed films around oil droplets [55]. The T10 treatment, which combines lentil, bean, and pea proteins in equal proportions, showed the best results in terms of the emulsifying effect and stabilization. This synergistic combination improves both the emulsifying ability (EAI) and the emulsion stability index (ESI) and makes the T10 mixture effective.