Changes in chemical, structural and technofunctional attributes of animal-based proteins upon emerging non-thermal...

Animal-based proteins are key to the nutritional and functional properties of many foods, yet conventional processing often impairs their structure and quality. This review evaluates how emerging non-thermal processing (NTP) methods i.e., high-pressure processing, ultrasound, pulsed electric field, cold plasma, pulsed light, and ozonation, modulate their molecular structure, technofunctional properties and nutritional attributes. These treatments induce changes in protein secondary and tertiary structures, such as unfolding, aggregation, or cross-linking, which in turn influence particle size, morphology, rheological attributes, foaming and emulsion stability, gelling properties, swelling power, solubility, enzymatic activity, and nutritional attributes. While NTPs offer promising improvements in protein techno-functionality, their effects are highly technique- and protein-specific. Overexposure may lead to unwanted oxidation or loss of solubility. Overall, this review highlights NTPs as powerful tools for tailoring animal protein functionality with minimal processing. Future work should address process optimization, scalability, and impacts on sensory and nutritional quality.