Recent advances in protein modification strategies to enhance their gel formation capability and stability: Principles, mechanisms, and techniques.

Proteins are becoming more and more popular as environmental and human health concerns grow, as is the demand for sustainable food sources. Among the many functional characteristics of proteins are their ability for emulsifying, gelling, and foaming. Depending on the protein content, pH, ion type, and strength, a dense three-dimensional gel network structure is produced by the denatured and aggregated proteins. The structure of proteins for gel formation can be tailored using a variety of modification strategies, including both conventional and emerging techniques. Additionally, applying different treatment conditions might change the gelation characteristics of proteins to varying degrees. At the moment, it is difficult to unlock the potential substitution of proteins since their structural properties and gelation mechanisms vary greatly from one another, and because the underlying mechanisms of proteins under different modification techniques are not fully understood. Information about the structure and processes of protein gels is provided in this review. We also explained how some processing techniques change the structure of proteins to improve gel formation and stability, as well as the chemistry behind them. Future research can examine efficient modification techniques for binary proteins to enhance their gelation ability.