Effects of thermal and non-thermal processing on the structure and function of food proteins: A review

Food proteins play important roles in determining the nutritional quality and functional properties of food systems. However, many native proteins exhibit limited solubility, digestibility, and bioactivity, restricting their industrial applications and nutritional utilization. Although numerous studies have investigated the effects of thermal and non-thermal processing on protein modification, current understanding remains fragmented, and systematic comparisons of the underlying structure-function relationships across different processing technologies are still limited. This review provides a comparative and mechanistic perspective on how thermal treatments (e.g., traditional heating methods, ohmic heating, microwave and radio frequency) and non-thermal technologies (e.g., high hydrostatic processing, cold plasma, pulsed electric fields, ultrasound and irradiation) regulate the structural evolution and functional properties of food proteins. Particular emphasis is placed on the relationships between processing-induced changes in secondary and tertiary structures and the consequent alterations in protein solubility, digestibility, and bioactivity, thereby providing insights for the rational design of protein modification strategies.