Ultrasound-assisted modification of gelation properties of proteins: A review

Protein gels have diverse applications in the food, pharmaceutical, and cosmetic sectors due to their affordability, biodegradability, and edibility. However, the inherent properties of some native proteins have a few drawbacks that have to be tailored to meet the needs of specific functions as the food ingredients. The protein gelation properties mainly depend on the protein molecular structure, primarily the folding and unfolding of secondary structural elements (α-helix and β-sheets) with distinctive functions. In the past, a great amount of work (thermal, chemical, and enzymatic methods) has been carried out to enhance the gelation and functional properties of proteins. Recently, the traditional methods have been replaced with non-thermal physical methods that enhance the properties for better applications. One such approach is the use of ultrasonic technology as a low-cost green technology to modify the molecular orientation attributed to the native chemistry and functionality of that proteins. Ultrasonic technology is important in food systems and can be effectively used as an alternative method to improve the protein gelling characteristics to form high-quality gels. This article is aimed to comprehensively collate some of the vital information published on the mechanism of protein gelation by ultrasonication and review the effects of ultrasound-assisted extraction and treatments on gelation properties of different proteins. The enhanced gelation properties by the ultrasound application open a new stage of technology that enables the proteins for better utilization in the food processing sector.