Abstract
In this study, a novel method called selective proteolysis was applied to the glycinin component of soy protein isolate (SPI), and a degraded glycinin hydrolysate (DGH) was obtained. The effects of high-intensity ultrasound (HIU) treatment (20 kHz at 400 W, 0, 5, 20, and 40 min) on the physical, structural, and aggregation properties of DGH were investigated with the aim to reveal the influence of the selectively hydrolyzing glycinin component on the HIU treatment of soy protein. The effects of HIU on DGH and a control SPI (CSPI) were both time-dependent. HIU induced the formation of soluble aggregates in both samples at an early stage, while it dissociated these newly formed aggregates after a longer duration. Selectively hydrolyzing glycinin contributed to the soluble aggregation by exposing the compact protein structure and producing small protein fractions. The larger extent of hydrophobic interactions and disulfide bonds imparted a higher stability to the soluble protein aggregates formed in DGH. As a result, DGH displayed more ordered secondary structures, a higher solubility, and better gelling properties after the HIU treatment, especially at 20 min. The results of this study will be beneficial to the scientific community as well as industrial application.
Highlights
High-intensity ultrasound (HIU), which has frequency in the range of 20–100 kHz and power in the range of 10–1000 W/cm2, has drawn considerable attention recently as a promising nonthermal processing method with little impact on the environment [1]
Compared with control SPI (CSPI), the degraded glycinin hydrolysate (DGH) nanoparticles formed soluble aggregates while it disassociated them after a longer duration (40 min)
With a larger size and higher stability, which could be attributed to the existence of small protein fractions nanoparticles formed soluble aggregates with a larger size and higher stability, which could be and the larger extent of hydrophobic interactions as well as disulfide bonds
Summary
High-intensity ultrasound (HIU), which has frequency in the range of 20–100 kHz and power in the range of 10–1000 W/cm , has drawn considerable attention recently as a promising nonthermal processing method with little impact on the environment [1]. The ultrasonic treatment of soy protein has been studied in the last decade, since soy protein is one of the most promising plant proteins in the food industry. Arzeni et al [4] found that HIU could reduce the viscosity and particle size of commercial SPI. Upon their treatment, the free sulfhydryl groups remained unchanged
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