Roles of protein disassembly-reassembly behavior in determining physicochemical characteristics during food processing.

Abstract

Proteins are amphiphilic macromolecules whose conformational dynamics critically determine the physicochemical and sensory attributes of protein-based foods. During food manufacturing, environmental stresses such as heating, pH shifting, freeze-thaw cycles, and emerging physical fields (e.g., pulsed electric fields, ultrasound, and ohmic heating) disrupt noncovalent interactions and induce dynamic disassembling-reassembling transitions. These structural rearrangements involve unfolding, aggregation, refolding, and network reconstruction, thereby modulating hydrophobic exposure, disulfide bond formation, and interfacial behavior, which ultimately govern solubility, emulsification, gelation, texture, and flavor stability. This review provides a comprehensive and updated overview of how novel processing technologies regulate protein folding architecture compared with conventional thermal treatments. By integrating multiscale structural evolution with functional outcomes, we propose a unified analytical framework linking protein conformational transitions to food quality and nutrition, offering theoretical guidance for rational design and precision control of next-generation protein-rich foods.