This study evaluated how deep eutectic solvent (DES)-based protein extraction influences the heat-induced gelation of fava bean proteins, in comparison with alkaline and salt extraction methods, using commercial soy protein isolate as a reference. The final storage modulus (G') differed significantly among the gels (p ALK-FBG (4.67 ± 0.30 mg/mL) > SS-FBG (2.62 ± 0.32 mg/mL). Disulfide bond content was not significantly different between DES-FBG (2.67 ± 0.60 mg/mL) and SS-FBG (1.69 ± 0.57 mg/mL) (p > 0.05), but both were higher than ALK-FBG (1.35 ± 0.08 mg/mL) and the CSG (0.32 ± 0.02 mg/mL). This indicates that the relatively higher hydrophobic and disulfide interactions in DES-FBG contribute to the formation of a strong gel network, as supported by its homogeneous, well-connected, fine-stranded microstructure. In contrast, ALK-FBG and SS-FBG formed weak gel networks characterized by irregular, loosely stacked protein aggregates with larger pores. Overall, the findings demonstrate that DES-based protein extraction is a promising and sustainable alternative for developing plant-based gel products.
Hewage et al. (Fri,) studied this question.