## 3 Results and Discussion
### Water-Binding Capacity and Oil-Binding Capacity  
The capacity of a protein to bind water, known as water-binding capacity (WBC), is strongly linked to the texture, mouthfeel, and viscosity of food products [43]. Oil-binding capacity (OBC), which refers to a protein's ability to retain absorbed oil, is also influenced by protein composition, pH, and ionic strength [30; 44]. The values for the WBC and OBC of the BSF larvae proteins are illustrated in Figure 3. It is worth noting that the inclusion of NaCl salt did not produce a statistically significant change in the WBC of the protein, as shown by the results (\(p<0.05\)). However, the AAFSISO demonstrated a higher WBC than the other proteins, although this difference was not statistically significant (\(p>0.05\)). The variations in WBC across protein fractions were attributed to the amino acids outlined in the preceding work (not reported), which were impacted by the extraction method employed. To date, no research has been undertaken to investigate the WBC of BSF larvae proteins obtained through various salt-facilitated methods. The outcomes of this investigation surpassed the WBC values reported for BSF larval flour fractions in the previous literature (0.4-0.8 g/g) [15]. The highest WBC was found in the AAFSISO isolate (4.45 g/g), which significantly exceeded the WBC values of different insect species fractions documented in the literature, including _Tenebrio molitor_ (1.87 g/g) [36] and _Spodoptera gregaria_ (2.18 g/g) [30]. Similarly, the highest WBC was noted in the flour of _Galleria sigillatus_ (2.34 g/g) and _Spodoptera gregaria_ (2.18 g/g), which is likely due to the significant presence of hydrophilic amino acids (390.6 and 371.4 mg/g, respectively) [36]. These findings also suggest that BSF larvae have the potential to be a valuable ingredient in the food industry, as proteins with WBCs ranging from 1.49 to 4.72 g/g are recommended for use in viscous foods [45]. Figure 3: Effect of extraction methods on water- and oil-binding capacity of black soldier fly larvae isolate obtained by AAF (alkaline–acid extraction), AAFSI (salting-in technique), AAFSO (salting-out technique), and AAFSISO (salting-in and out technique). Various letters suggest notable contrasts with statistical significance at \(p<0.05\). Error bars depict standard deviation. The OBC of proteins is often indicative of their ability to interact with lipids, which is closely connected to factors such as emulsifying properties, flavor retention, and shelf life. This capacity can be impacted by various factors, including the type of protein, oil applied, and hydrophobicity. Furthermore, the addition of salts had a significant (\(p<0.05\)) influence on the OBC of BSF larvae protein isolates. It is worth noting that a high degree of oil binding may be positively correlated with a protein's high hydrophobicity. The significance of the protein-binding capacity for oils or fats extends to the creation of meat substitutes and extenders, in addition to sausages, emulsions, and cake batteries [45]. AAFSI had the highest (\(p<0.05\)) OBC in comparison to other proteins (Figure 3). These results are consistent with our earlier findings regarding the solubility of AAFSI at pH 10 and its pronounced hydrophobic nature. The values obtained for the various isolates exhibited significant variation (\(p<0.05\)), with AAF having a content of 1.58 g/g, AAFSI at 2.17 g/g, AAFSO at 1.04 g/g, and AFFSISO at 1.36 g/g. These distinctions in the OBC could be a result of variations in the hydrophobicity or hydrophilicity of the protein surfaces, a characteristic that could be influenced by the extraction method used [19]. One can observe a significant variation between the protein isolates of AAFSI and AAFSO. This is due to the fact that precipitates obtained through salting-out may possess a distinct structure or conformation compared to those obtained via salting-in, which can influence their capacity to bind to oil.