Tracking protein aggregation behaviour and emulsifying properties induced by structural alterations in common carp (Cyprinus carpio) myofibrillar protein during long-term frozen storage.

The effect of ultrasound-assisted immersion freezing (UIF), air freezing (AF), and immersion freezing (IF) on the protein structure, aggregation, and emulsifying properties of common carp (Cyprinus carpio) myofibrillar protein during frozen storage were evaluated in the present study. The result showed that, compared with AF and IF samples, UIF sample had higher reactive/total sulfhydryl, protein solubility, and lower protein turbidity (P < 0.05), indicating that UIF was beneficial to inhibit protein oxidation and aggregation induced by frozen storage. UIF inhibited the alteration of secondary structure and tertiary structure during frozen storage. Meanwhile, UIF sample had higher emulsifying activity index, and smaller emulsion droplet diameter than AF and IF samples (P < 0.05), suggesting that UIF was beneficial for maintaining the emulsifying properties of protein during storage. In general, UIF is a potential and effective method to suppress the decrease in protein emulsifying properties during long-term frozen storage.