## 3 Results and Discussion
### Foaming Capacity and Stability  
Foaming capacity (FC) is the ability of protein molecules to rapidly dissolve and unfurl, thereby forming a cohesive layer around a gas bubble, while foaming stability (FS) involves forming a stable foam through intermolecular polymerization that captures air [14]. Excellent foaming properties require proteins to swiftly migrate to the air-water interface, where they unfurl and reorganize [30]. Furthermore, foam properties are closely tied to protein solubility, and high solubility is a fundamental requirement for optimal FC. The FS and FC of BSF larvae isolates were measured and presented in Figure 4. In our study, all four isolates exhibited exceptional FC values, which exceeded those reported for _Tenebrio Molitor_ and _Schistocerca gregaria_ (34.67% and 19.33%, respectively) as per the findings of [30].  
The differences in the FC of AAF and AAFSI proteins were not significantly lower (\(p<0.05\)) in comparison to the differences observed in AAFSO and AAFSISO proteins, which had values of 11.00% and 14.79%, respectively. The outcomes demonstrated that salting-out-assisted treatments significantly boosted (\(p<0.05\)) the FC. Correspondingly, the FS results revealed that AAFSISO proteins exhibited the highest stability at 99.99%, followed by AAFSO at 84.50%. The presence of ammonium sulfate as a salt ion may enhance both FC and FS by exposing hydrophilic residues and improving protein solubility during the isolation step [14]. This result aligns with the findings of a study conducted by [17], in which the FS of cashew nutshell protein demonstrated an increase from 56.03% to 76.91% at the 60 min mark following salt addition. This increase in FS was attributed to the enhanced surface activity and solubility of the protein.  
On the contrary, the low foaming capacity can be attributed to the globular proteins that are highly ordered and resist surface denaturation. For proteins to function effectively as foaming agents, they must possess the ability to (i) undergo rapid conformational changes and rearrangements at the interface and (ii) rapidly adsorb at the air-water interface during bubbling. In a study by [46], the comparison was made between the foaming properties of mealworm and cricket powders, and those of protein concentrates derived from yellow pea and faba bean. In a comparison between pulse proteins and cricket proteins, the cricket proteins produced foam that was more stable over time, while the pulse proteins generated more foam overall. These differences in FC could arise from the distinct conformational characteristics of the proteins. It has been established that the FC of proteins can be influenced by factors such as the balance of hydrophilic/hydrophobic groups and solubility, as well as the protein's composition and structural properties [46]. Globular proteins, such as those found at the air-water interface, possess a reduced capacity to unfold, which in turn restricts their ability to capture air bubbles [47]. The scientific community is currently exploring alternatives to eggs, a widely used foaming agent in food products [23]. Presently, the food industry utilizes protein concentrates and isolates derived from wheat, soy, and dairy as ingredients. Nevertheless, both consumers and food processors are seeking alternative sources of protein to mitigate the allergenic concerns associated with the eight priority allergens, which comprise egg, soy, wheat, fish, peanut, crustaceans, dairy, and tree nuts. The findings of this study indicate that the AAFSISO protein preparation exhibits promising foaming properties and could be considered as a potential foaming agent for use in food applications.