Physicochemical and functional characteristics of a gourd (Cucurbita argyrosperma Huber) seed protein isolate subjected to high-intensity ultrasound

Abstract

The impact of high-intensity ultrasound (HIU, 20 kHz) on the physicochemical and functional characteristics of gourd seed protein isolate (GoSPI) was studied. GoSPI was prepared from oil-free gourd seed flour through alkaline extraction (pH 11) and subsequent isoelectric precipitation (pH 4). The crude protein concentration of GoSPI ranged from 91.56 ± 0.17 % to 95.43 ± 0.18 %. Aqueous suspensions of GoSPI (1:3.5 w/v) were ultrasonicated at powers of 200, 400, and 600 W for 15 and 30 min. Glutelins (76.18 ± 0.15 %) were the major protein fraction in GoSPI. HIU decreased the moisture, ash, ether extract, and nitrogen-free extract contents and the hue angle, available water and a* and b* color parameters of the GoSPI in some treatments. The L* color parameter increased (7.70 %) after ultrasonication. HIU reduced the bulk density (52.63 %) and particle diameter (39.45 %), as confirmed by scanning electron microscopy, indicating that ultrasonication dissociated macromolecular aggregates in GoSPI. These structural changes enhanced the oil retention capacity and foam stability by up to 62.60 and 6.84 %, respectively, while the increases in the solvability, water retention capacity, and emulsifying activity index of GoSPI were 90.10, 19.80, and 43.34 %, respectively. The gelation, foaming capacity, and stability index of the emulsion showed no improvement due to HIU. HIU altered the secondary structure of GoSPI by decreasing the content of α-helices (49.66 %) and increasing the content of β-sheets (52.00 %) and β-turns (65.00 %). The electrophoretic profile of the GoSPI was not changed by HIU. The ultrasonicated GoSPI had greater functional attributes than those of the control GoSPI and could therefore be used as a functional food component.