“…6 , the EAI of PPI–Ara conjugates increased significantly from 15.1 to 19.7 and 19.3 m 2 /g with increasing ultrasonic power (longer treatment time). The hydrophobicity of the protein surface decreases when the degree of glycosylation is induced by ultrasound, and the hydrophilic and hydrophobic ratios on the molecular surface reach equilibrium, promoting the rapid adsorption of proteins at the oil–water interface, reducing the interfacial tension [49] . Fig.…”
“…6 , the EAI of PPI–Ara conjugates increased significantly from 15.1 to 19.7 and 19.3 m 2 /g with increasing ultrasonic power (longer treatment time). The hydrophobicity of the protein surface decreases when the degree of glycosylation is induced by ultrasound, and the hydrophilic and hydrophobic ratios on the molecular surface reach equilibrium, promoting the rapid adsorption of proteins at the oil–water interface, reducing the interfacial tension [49] . Fig.…”
“…Better emulsifying performance of the double emulsion was observed at 125 W ultrasonic power, with the corresponding EAI and ESI values being 1.61 ± 0.38 m 2 /g and 98.37 ± 0.21 %, respectively. The cavitation effect and physical shear stress of ultrasound treatment effectively reduce the large sized nutrient particles (proteins, polysaccharides, and other edible components) in the outer aqueous phase, improving their dispersibility and solubility; in addition, the powerful micro-jet generated by ultrasound treatment renders greater uniformity to the emulsion system with better emulsifying properties [33] , [34] . Interestingly, the emulsifying properties of the double emulsion did not improve further after ultrasonic treatment at 150 W. This may be because a high ultrasonic power may disrupt the spatial structure of the protein to thus form aggregates, leading to a decrease in the emulsifying properties of the emulsion system, consistent with that reported earlier [35] .…”
Section: Resultsmentioning
confidence: 99%
“…Heat sterilization is a common processing method in the food industry, as it can effectively inhibit the growth and reproduction of microorganisms [33] . Therefore, it was necessary to study the effect of temperature on the stability of LOPs double emulsion under 125 W ultrasonic treatment.…”
“…As shown in Table 2 , the free sulfhydryl content of group A presented significantly higher than that of group B ( p < 0.05), and the disulfide bond content showed an opposite trend, indicating the unfolded structure content of group A was higher. This might be due to the fact that the optimal ultrasonic intensity can break disulfide bonds, thus exposing more sulfhydryl groups [ 14 ], while in group B, the mild ultrasonic intensity could not effectively unfold the protein structure, and the excessive ultrasonic intensity induced protein aggregation, thus promoting the formation of disulfide bonds [ 22 , 24 ]. In addition, the content of free sulfhydryl in IAP was higher than that in INP in the two groups, indicating that IAP was more flexible than INP.…”
Section: Resultsmentioning
confidence: 99%
“…The MDD of IAP and INP in group A was significantly lower than that in group B ( p < 0.05), and the λ max of IAP and INP in group A was larger than that in group B, indicating that IAP and INP aggregated in group B. This phenomenon might be attributed to the optimal ultrasonic intensity-unfolded protein structure, but the excessive ultrasonic intensity led to protein aggregates, while mild ultrasonic intensity could not effectively unfold the protein structure [ 20 , 24 ]. In addition, the MDD of INP in the two groups was greater than that of IAP, and the λ max had an opposite trend, which might be due to the fact that highly unfolded protein is prone to arranging on the oil–aqueous interface during RBPE formation, forming a viscoelastic membrane [ 5 ].…”
To provide a strategy for improving the stability of rice bran protein emulsion (RBPE), rice bran proteins (RBPs) with different oxidation extents were prepared from fresh rice bran (RB) stored for different times (0, 1, 3, 5, 10 d), and RBPE was prepared with ultrasonic treatment. The ultrasonic conditions were optimized according to the results of the RBPE’s stability (when RB stored for 0, 1, 3, 5, 10 d, the optimal ultrasonic treatment conditions of RBPE were 500 w and 50 min, 400 w and 30 min, 400 w and 30 min, 300 w and 20 min, 500 w and 50 min, respectively). Additionally, the structural characteristics and the flexibility of RBPE interface protein were characterized, and the results showed that compared with native protein and excessive oxidized protein, the unfolded structure content and flexibility of interface protein of RBPE prepared by moderate oxidized protein under optimal ultrasonic intensity was higher. Furthermore, the correlation analysis showed that the RBPE stability was significantly correlated with the structural characteristics and flexibility of the RBPE interface protein (p < 0.05). In summary, ultrasonic treatment affected the interface protein’s structural characteristics and flexibility, improving the stability of RBPE prepared from oxidized RBP.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
