Functional properties of sesame and perilla meal proteins extracted using hot water

In this study, proteins were extracted from sesame and perilla meals (agricultural by-products) by using hot-water defatting and acid precipitation, and their functional properties were compared with those of a commercial soy protein isolate (SPI). According to the SDS-PAGE results, the sesame meal protein extract (SMPE) exhibited a higher content of hydrophobic amino acids than the perilla meal protein extract (PMPE), alongside a relatively lower intensity of the 7S globulin band. SMPE showed 1.41-fold higher solubility than SPI at pH 10 and 1.72- and 1.66-fold higher emulsifying activity indices (EAIs) at pH 8 and 10, respectively. PMPE exhibited similar trends in solubility and EAI as SPI at the corresponding pH values. However, the emulsifying stability indices of SMPE and PMPE were lower than that of SPI. In particular, the fat absorption capacity of SMPE was significantly higher than those of SPI and PMPE, likely because of its higher content of hydrophobic or nonpolar amino acid residues. These results suggest that SMPE and PMPE are promising alternative protein sources for food applications and may promote value-added utilization of plant-derived by-products in the food industry.