## 3 Results and Discussion
### Accelerated Tests--Stability to Centrifugation and Extreme Heat Treatment
All other emulsions remained stable, proving that they could withstand heat treatment at 80 \({}^{\circ}\)C. The fava bean protein was able to thermally stabilize the emulsion with lentils and also the emulsion with peas and lentils. Ref. [64] found a peak of denaturation of the lentil protein between 118 and 123 \({}^{\circ}\)C, temperatures way above those tested in the present study. However, the lentil protein was not able to withstand such stress, so the solid part settled at the bottom of the tube. This sedimentation was also observed by [PERSON] [65] in samples with lentil protein that were not treated with high pressure when subjected to the accelerated stability test. A wide range of commercial plant-based milk substitutes analyzed in another study showed high deposition rates for almost all products due to insoluble plant material via flocculation and precipitation [36; 66]. In HCT (Time of Thermal Coagulation) analysis, coagulation is induced by applying heat in order to measure the thermal stability of the sample. Methods of this type can be useful to some extent to simulate batch sterilization in an autoclave, where the heating of the sample is as slow as in laboratory-scale thermal stability tests. The mixed protein suspensions had a thermal clotting time (HCT) of 13.53 \(\pm\) 2.11 to 25.78 \(\pm\) 0.67 min in an oil bath at 140 \({}^{\circ}\)C (Table 2). The T2 treatment had the shortest thermal clotting time. The longest time was observed in the mixtures with the highest concentration of pea and bean protein. The combination of lentil protein with pea or bean resulted in a prolongation of the clotting time. In a study with lentil protein at 3.3% (\(w/w\)), a value of 8.28 min was determined for thermal stability [65]. In general, it can be stated that the proteins were stabilized to a certain degree and protected from heat-induced coagulation. As long as the proteins are at the interface with the oil, their hydrophobic groups are aligned with the oil phase so that no interactions are forced between the exposed hydrophobic sites of the protein molecules. However, as the degree of denaturation increases, the proteins may lose their ability to stabilize the interface, and eventually, the system becomes unstable, leading to exposure of the hydrophobic groups and aggregation. Ref. [67] observed that HCT increased from 2.8 to 6.7 min when pH was increased from 6.3 to 7.2. This heat-induced coagulation is determined by a balance between attractive and repulsive forces, as an increase in the latter has been shown to increase HCT. The charge distribution between amino acid side chains is altered by pH, and for lentil proteins, negative charges increase with increasing pH, resulting in greater repulsion between lentil proteins. The results of this work are consistent with those obtained by 65. The surface charge of the emulsions, with the lentil protein having the highest charge (\(-\)23.77 \(\pm\) 2.33), showed a shorter coagulation stability time, while the other emulsions, which had longer HCT times, showed lower surface charges. This inverse correlation was observed in the correlation test, although it did not reach significant values (r = \(-\)3.64; \(p\) < 0.05), indicating a weak correlation.