Ellagic acid‐loaded soy protein isolate self‐assembled particles: Characterization, stability, and antioxidant activity

Abstract

AbstractThe limited water solubility and bioactivity of lipophilic phytochemicals may be enhanced by delivery systems. Ellagic acid (EA) has antioxidant and anti‐inflammatory properties, but low solubility and instability limit its use in the food industry. In this study, the pH‐shift method was applied to encapsulate EA with soy protein isolate (SPI). The interaction, encapsulation, and protective potential of the EA‐loaded soy SPI complexes (SPI–EA) were investigated. The fluorescence spectra results suggest that the reaction between SPI and EA is spontaneous, with hydrophobic interactions predominating. Binding of EA molecules quenches the intrinsic fluorescence of SPI, mainly static quenching, with a binding site involved in the binding process. The ultraviolet (UV)–visible spectroscopy of the SPI–EA complexes included the characteristic absorption peaks of both SPI and EA, and the scanning electron microscopy images further indicated that the EA had been successfully embedded in SPI. Fourier transform infrared spectroscopy illustrates that EA has significantly changed the secondary structure of the SPI, primarily in the form of a decreased content of α‐helix structures and an increased content of β‐sheet and random coil structures. The encapsulation efficiency of EA was concentration‐dependent, up to 81.08%. The addition of EA reduces the size of SPI particles (d < 155 nm). In addition, the SPI–EA complex showed up to 81.05% and 96.46% 1,1‐diphenyl‐2‐picrylhydrazyl and 2,2′‐azino‐bis (3‐ethylbenzothiazoline‐6‐sulfonic acid) radical scavenging activity. TGA showed that the degradation temperature of SPI–EA complex could be extended up to 300°C. And by encapsulation of EA, the loss of EA under the action of UV light, heat treatment, and high concentration of salt ion sensitive environment can be reduced.Practical ApplicationEllagic acid (EA), a natural bioactive with low water solubility and stability, can be enhanced by forming an inclusion complex with soy protein isolate (SPI). SPI–EA complex has broad potential applications in the food, beverage, and pharmaceutical industries. Multiple spectral analyses have contributed to our understanding of the formation and interaction mechanisms of the SPI–EA complex under pH‐driven conditions. Stability assays have also aided in the development of dietary resources for EA.