Background The number of people who are aware of consuming healthy and natural foods are consistently increasing. Natural emulsifier-stabilized emulsions have attracted widespread attention in food industry. Ultrasound has a potentially wide range of applications in the preparation of food emulsions. Scope and approach This review briefly discussed the effects of ultrasound-assisted emulsification (UE) on emulsion formation along with introducing the different emulsifier stabilized emulsions. In special, the effects of UE on the emulsion properties such as viscosity, emulsifying properties, droplet size, zeta potential, emulsifier properties and oil phase properties have been summarized. Finally, the advantages and disadvantages of current studies on UE in food system were also discussed. Key findings and conclusions The review demonstrated that the process of UE may not be a simple process of breaking up droplets, but may be a more complicated process. UE can be used to prepare many emulsifier stabilized food emulsions such as protein, polysaccharide, protein-polysaccharide and protein-polysaccharide-surfactant. Proper UE treatment could improve the rheological properties and emulsifying properties, reduce the emulsion droplet size as well as increase the absolute zeta potential of emulsions. UE was shown to be a good method to unfold proteins and form good emulsions. However, the studies on sonication induced emulsifier properties were still limited. High-intensity ultrasound had no significant influence on the oil oxidation and oil profiles, whereas increased the anti-oxidative ability of some emulsions. Beside the large-scale ultrasonic devices should be developed, the effects of UE on emulsifier and oil phase during and after sonication should be further studied in the future.

Applications and effects of ultrasound assisted emulsification in the production of food emulsions: A review

Impact of tea polyphenols on the stability of oil-in-water emulsions coated by whey proteins.

Impact of heating treatments on physical stability and lipid-protein co-oxidation in oil-in-water emulsion prepared with soy protein isolates

Effects of proteins on emulsion stability: The role of proteins at the oil-water interface.

Polyunsaturated fatty acids (PUFAs) play an important role in promoting brain development, decreasing the incidence of cardiovascular diseases, and reducing inflammation. However, PUFAs are inherently unstable and susceptible to oxidative deterioration due to two or more double bonds in their structure. Delivery systems have been developed to provide effective encapsulation and protection for PUFAs, and finally fulfill their health benefits. Emulsion-based encapsulation is one of the most promising techniques for the delivery of PUFAs. The emulsion composition and structure, as well as the storage conditions are regarded as key factors to influence the stability of emulsions. To maximize the resistance of PUFAs in emulsions against oxidation, emulsion structure design has been particularly highlighted, and different methods for tailoring emulsion structure have been developed. The current work is focused on the careful design of emulsion structure to improve the oxidative stability of PUFAs. Different types of emulsions, including conventional emulsions, multilayer emulsions, gelled emulsions, and Pickering emulsions are introduced, and their protective effect for PUFAs are discussed. The major role of interfacial structure in emulsions is emphasized. The effects of emulsifiers and involved modification methods on the interfacial structure are presented to further improve the stability of PUFAs during storage.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/1541-4337.12621

Emulsion structure design for improving the oxidative stability of polyunsaturated fatty acids.

The impact of interfacial composition on lipid and protein co-oxidation in oil-in-water emulsions containing a mixture of proteins and surfactants was investigated. The emulsions consisted of 5% v/v walnut oil, 0.5% w/v whey protein isolate (WPI), and 0 to 0.4% w/v Tween 20 (pH 3 and pH 7). The protein surface load, magnitude of the ξ-potential, and mean particle diameter of the emulsions decreased as the Tween 20 concentration was increased, indicating the whey proteins were displaced by this nonionic surfactant. The whey proteins were displaced from the lipid droplet surfaces more readily at pH 3 than at pH 7, which may have been due to differences in the conformation or interactions of the proteins at the droplet surfaces at different pH values. Emulsions stabilized by whey proteins alone had relatively low lipid oxidation rates when incubated in the dark at 45 °C for up to 8 days, as determined by measuring lipid hydroperoxides and 2-thiobarbituric acid-reactive substances (TBARS). Conversely, the whe...

Impact of Interfacial Composition on Lipid and Protein Co-Oxidation in Oil-in-Water Emulsions Containing Mixed Emulisifers.

Vegetable proteins are increasingly used to stabilize oil-in-water (O/W) emulsions. However, emulsions are thermodynamically unstable. Recently, high-intensity ultrasound (US) has been used to enhance the stability of emulsions. For these reasons, and considering almond (Prunus dulcis L.) as a good source of high-quality proteins, the aim of this work was to investigate the effect of US treatment on the stability of pre-emulsification O/W emulsions coated with almond protein isolate (API).; Results: The influence of API concentration (0.25-2.0 g L-1 ), ion strength (0-500 mmol L-1 NaCl), and pH (3.0-7.0) on the stability of US-treated emulsions was evaluated. US treatment (200-600 W, 25 kHz, 15 min) led to a significant reduction in the particles size of droplets in emulsions, increased critical osmotic pressure and additional protein interfacial adsorption, and thus the formation of more stable emulsions. The more unfolded and random coil structures of the proteins were detected at higher US power, facilitating protein interfacial adsorption. Increasing API concentrations resulted in higher stability of US-treated emulsions against untreated counterparts. The US-treated emulsions were more resistant to salt than untreated samples. In the range from pH 3.0 to7.0, US treatment also enhanced the physical stability of emulsions compared with untreated emulsions.; Conclusion: US technology could be applied to produce more stable O/W food emulsions stabilized by proteins. © 2018 Society of Chemical Industry.; © 2018 Society of Chemical Industry.

Ultrasound improving the physical stability of oil-in-water emulsions stabilized by almond proteins.

The invention relates to a method for improving functional characteristics of sweet almond isolated protein. A sweet almond isolated protein solution is ultrasonically treated, and the structure of a protein molecule is changed by utilizing the fluctuation and energy attribute of the ultrasonic waves. The sample solution is treated by utilizing different ultrasonic power and ultrasonic time, a mechanical shearing force and a series of chain reactions generated by the high-frequency oscillation in a short time are used for generating a cavitation effect acting on the sweet almond isolated protein solution, the space structure change of the sweet almond isolated protein is promoted, so that the functional characteristics of the protein such as solubility, emulsion property, emulsification stability, foaming property, foaming stability, antioxidant sulfhydryl groups of the proteins can be improved to various degrees. The method is low in cost, free from pollution, and capable of satisfying the environment-friendly, resource-saving and sustainable development principles. By adopting the method, while the functional characteristics of the sweet almond protein is improved, the processing additional value and comprehensive utilization rate of the almond protein is increased.

Method for improving functional characteristics of sweet almond isolated proteins

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Impact of Interfacial Composition on Lipid and Protein Co-Oxidation in Oil-in-Water Emulsions Containing Mixed Emulisifers.

Ultrasound improving the physical stability of oil-in-water emulsions stabilized by almond proteins.

Method for improving functional characteristics of sweet almond isolated proteins