. 2022 Sep 7;8(9):e10572. doi: 10.1016/j.heliyon.2022.e10572

Table 5.

Techno-functional properties of SI proteins.

Outcomes	Reference
Low solubility and water adsorption capacity (7.96% and 2.16 g/g, respectively)	(Alcívar et al., 2020)
Water absorption index (3.2–4.4 g/g), water solubility index (12.4–26.2%), and solubility (10.7–38.0 mg/g)	(Jagersbeger, 2013)
Albumin fraction extracted with saline solution displayed notable protein solubility (63%), water-holding capacity (1.6 g/g), oil retention capacity (1.7 g/g), foaming (350%) and emulsifying (13.0 mL/g) abilities Heating at temperatures lower than 100 °C improves solubility, oil-holding capacity, foaming and emulsifying capacities
Increased protein solubility up to 63% as pH increased from 3.0 to 7.0 and significantly dropped (up to approximately 18%) at pH 10.0	(Li et al., 2018)
2% salt addition reduces solubility of protein fraction	(Mercado et al., 2015)
Oil absorption capacity (1.4 g/g), foaming capacity (55% at 1% concentration and pH 8.0), foam stability (33.7% at 1% of concentration, pH 8.0 at 120 min), and emulsifying capacity (59.1%), generally higher than soy protein isolates
Lower water holding (1.8 g/g) and gelling capacities (15%) compared to soy protein isolates
Protein isolates extracted by alkaline water (pH 12.0) presented 84.4% solubility, foam stability of 30% at pH 8.0, and emulsifying, water retention, oil absorption, gelling, and foaming (pH 8.0) capacities of 53.5%, 4.7 g/g, 267.1%, 13%, and 49%, respectively	(Cuñaña, 2018)