## 4 Discussion
This characteristic makes foams more compact, homogeneous, and very attractive for bakery products, ice creams, and high-quality confection items. Regarding coagulation, the SMH had the highest HCC of 83.06% and showed no significant difference with the soybean hydrolysate (\(p>0.05\)). Factors such as temperature, polarity, ionic strength, and pH influence coagulation; however, these parameters remained standard for all samples. Therefore, soybean-maize and soybean proteins' coagulation depended on the structure, size, and type of interaction (electrostatic and hydrophobic) [43]. Regarding the isolates, the SMI showed proper coagulation while SI was the lowest with 40%. The low coagulation of SI could be due to the high amount of reducing sugars and non-protein solids that interfered with protein-protein interactions. This result agrees with findings reported by [PERSON] et al., [45], who observed that the protein coagulation capacity of taro, pigeon pea, and rice was reduced by the presence of carbohydrates, fiber, and other solids. The coagulation characteristics that possessed the soybean-maize proteins make them well suited to develop analogs of cheeses, yogurts, creams, beverages, dressings, puddings, jellies, jams, and others. The Kruskal-Wallis test determined that the isolates and hydrolysates of soybean and soybean-maize have different physicochemical characteristics and functional properties. Regarding the electrophoretic profile, the SI presented the typical pattern of electrophoresis: lipoxygenase was observed at 109.88 kDa and 71.74, 68.80 and 53.33 kDa the \(\alpha\), \(\alpha^{\prime}\) and \(\beta\) units of \(\beta\)-congylcinin, respectively. The acidic subunits (A\({}_{3}\), y A\({}_{14}\), A\({}_{1b}\), A\({}_{2}\) y A\({}_{4}\) indicated by the letter A) and basic (B) glycinin at 47.88 and 21.52 kDa appear in the gel, respectively. This pattern is consistent with the reports by [PERSON] et al. [5] to soybean proteins. This isolate showed the lowest solubility (NSI), and this could also be due to the factors mentioned above and the low amount or partial hydrolysis of glycinin basic (B), as shown in the gel. [PERSON] et al. [7] reported that the glycinin fraction had higher solubility than \(\beta\)-congylcinin and also that soybean proteins provided better foaming stability as determined for this sample. The SMI presented a profile similar to soybean but exhibited three additional bands to the typical pattern of 56, 55, and 52 kDa, which could be proteins provided by the maize germ. According to [PERSON] et al., [8], bands around 50 kDa correspond to maize globulins. [PERSON] [46] reported that solubility, surface hydrophobicity, and molecular flexibility influence the emulsifying capacity of globular proteins. Therefore, the maize germ globulins are probably responsible for the high emulsifying capacity and excellent emulsion stability presented by the soy-maize proteins. This result is consistent with reports by [PERSON] and [PERSON] [41], who determined a high emulsifying capacity and emulsion stability for proteins extracted from maize germ. The band of glycinin was evident, and its presence, according to [PERSON] et al. [7], justifies the excellent solubility. The same authors reported that glycinin possesses better emulsifying activity (EAI) because it has more exposed hydrophobic residues than \(\beta\)-congylcinin. The SH protein did not show the typical band related to lipoxygenase, possibly because it was hydrolyzed into lower molecular weight moieties. Moreover, the \(\beta\)-congbycinin subunits were slightly hydrolyzed because the band intensity of the subfractions \(\alpha,\alpha^{\prime}\) slightly decreased while the \(\beta\) almost disappeared. Regarding glycine, the acid subunits' intensity decreased while the basic subunits were not observed in the SH. This sample also showed low NSI possibly related to the absence of basic glycinin, and in contrast, the isolate showed less FS possibly related to the hydrolysis of the fraction \(\beta\) of \(\beta\)-congbycinin.