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Emulsion systems are extensively used in the food processing sector and the use of natural emulsifiers like proteins for stabilizing emulsion has been in demand from consumers due to increased awareness about the consumption of healthy food. Numerous methods are available for the preparation of emulsion, but ultrasound got more attention among common methods owing to its economical and environment-friendly characteristics. The physical effects caused by to bursting of the cavity bubble, result in reduced droplet size, thus forming an emulsion with appreciable stability. Ultrasound ameliorates the emulsifying characteristics of natural emulsifiers like protein and improves the storage stability of the emulsion by positively boosting the rheological, emulsifying characteristics, improving zeta potential, and reducing average droplet size. The stability of protein-based emulsion is affected by environmental stresses hence conjugate of protein with polysaccharide showed good emulsifying characteristics. However, the data on the effect of ultrasound parameters on emulsifier properties is lacking and there is a need to develop a sonication device that can carry out large-scale emulsification operation. The review covers the principles and mechanisms of ultrasound-assisted formation of protein-based and protein-based conjugate emulsions. Further, the effect of ultrasound on various characteristics of protein-based emulsion is also explored. This review will provide concise data to the researchers to extend their experiments in the area of ultrasound emulsification which will help in commercializing the technology at the industrial scale.

The optimized conditions of ultrasound-assisted enzyme modification and the effects of modification on the emulsification properties of Chlorella protein were investigated in this paper. The ultrasonic time, ultrasonic power, enzyme addition and enzyme reaction time were selected as the investigating factors. The analytic hierarchy process (AHP) was used to weight the emulsification activity, emulsification stability and creaming index, and the comprehensive weighted score was used as the response value. A four-factor, three-level response surface method was used to investigate the optimal modification conditions for the emulsification properties of ultrasound-assisted enzyme-modified Chlorella protein. The results showed that the optimal modification conditions were as follows: Ultrasonic time 31 min, ultrasonic power 209 W, enzyme addition 3.1% and enzyme reaction time 3 h. Under the optimized conditions, the best score of emulsification performance was 98.99, which was close to the predicted value. Compared with the original protein, the solubility and foaming ability of modified Chlorella protein increased by 68.30% and 49.44%, respectively. However, the modification of water-holding and oil-holding properties showed no significant effect. In summary, this study could provide certain theoretical basis for the application of Chlorella protein in food emulsification systems.

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In order to explore the key components affecting the emulsification characteristics in hydrolyzed rice protein. rice protein was hydrolyzed by acidprotease, papain and trypsin, respectively. The relationships between the structural and functional properties of different hydrolyzed rice proteins were studied by surface hydrophobicity, Fourier transform infrared spectroscopy (FTIR), emulsifying activity index and emulsifying stability index. 10 kDa were separated from the rice protein with degree of 2% treated with trypsin (trypsin 2%) by ultrafiltration. The interfacial tension, quartz crystal microbalance with dissipation (QCM-D), mean diameter particle, confocal laser scanning microscope (CLSM) and storage stability were measured to explore the influence of molecular weight on the interfacial characterization and emulsion stability. The results demonstrated that hydrolysates treated with trypsin exhibited the highest yield. Compared with the rice protein, the surface hydrophobicity of the enzymatic hydrolysis products declined significantly except for the rice protein with degree of 6% treated with trypsin (trypsin 6%). The secondary structure content revealed that the β-sheet contents of hydrolyzed rice protein significantly decreased, showing that the structure of hydrolyzed rice protein was more unfolded. The trypsin 2% exhibited the better emulsifying capacity. The mean diameter particle of 10 kDa had lower interfacial tension and thicker interfacial film than the others. The emulsion prepared by >10 kDa exhibited better emulsion stability. The results indicated that the emulsion stabilized by high molecular peptides was more stable than the smaller ones.

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)