Effects of ultrasound extraction on the physicochemical and emulsifying properties of rice bran protein

Abstract

In this study, rice bran protein was prepared by ultrasound-assisted extraction, and its physicochemical and emulsifying properties were also evaluated. Results demonstrated that a significant increase in protein yield was observed when ultrasound-assisted method was employed for extracting protein. Noticeably, obtained rice bran protein possessed excellent physicochemical properties, such as oil absorption capacity, protein solubility and foaming property. More hydrophobic groups were exposed in the process of ultrasound-assisted extraction, which led to the increase of surface hydrophobicity. More importantly, the ultrasound-assisted extraction could improve emulsifying properties of rice bran protein, and the emulsions prepared using protein samples exhibited the great stability. Besides, it was also found that emulsifying properties of protein samples presented a decrease trend with increasing ultrasound power and time. All in all, ultrasound-assisted extraction is a suitable alternative process for preparing rice bran protein.

Optimizing foam quality characteristics of model food using Taguchi‐based fuzzy logic method

“…As the sonication time increased, the SNR value also increased. This finding was supported by Sun et al (2021) who reported that US treatment improved foamability by modifying protein solubility. This situation may be attributed to the partial denaturation of proteins caused by cavitation, which leads to the exposure of nonpolar amino acids to the surrounding liquid, thereby increasing the surface hydrophobicity (Sheng et al, 2018).…”

“…As the sonication time increased, the SNR value also increased. This finding was supported bySun et al (2021) who reported that US treatment improved foamability by modifying protein solubility. This situation may be attributed to the partial Note: S = 0.0180093, R 2 = 99.58, R 2 (adj) = 98.34, and R 2 (pred) = 51.58.…”

“…US application causes an increase in the surface hydrophobicity and flexibility of the protein (Jambrak et al, 2009). Additionally, the proteins undergo partial denaturation and the exposed hydrophobic groups can interact with hydrophilic substances, leading to the formation of soluble/insoluble complexes (Sun et al, 2021).…”

Covalent binding of ultrasound-treated japonica rice bran protein to catechin: Structural and functional properties of the complex

“…Studies have shown that ultrasound treatment of protein can reduce particle size and improve its solubility and emulsifiability [15] . The study by Sun et al [16] demonstrated that ultrasound treatment improved the solubility, emulsifying properties, and stability of rice bran protein. A similar conclusion appeared in the study of Wang et al [17] , where the structure of JRBP was changed by the combined treatment of ultrasound and chlorogenic acid to obtain a complex with good functional properties to broaden its application in food processing emulsifiers.…”