Abstract: In recent years, ultrasound has been widely used in the food industry as a promising non-thermal, green technology, but the exact effect of ultrasound on the physicochemical properties of myofibrillar proteins from Procambarus clarkii is not clear yet. This study investigated the effect of high-intensity ultrasound treatment at 300 W power and 20 kHz frequency for 0, 4, 8, 12 and 16 min during homogenization on the structure and physicochemical properties of myofibrillar proteins from Procambarus clarkii. The results showed that ultrasound treatment decreased the turbidity and mean particle size of myofibrillar proteins significantly (P < 0.05), but initially increased and then decreased the solubility and absolute value of ζ-potential, demonstrating altered degree of protein aggregation. The surface hydrophobicity and endogenous fluorescence intensity initially increased and then decreased with increasing treatment time; the total sulfhydryl group content significantly decreased (P < 0.05) while the carbonyl group content significantly increased (P < 0.05), demonstrating changes in the tertiary structure and a certain degree of protein denaturation. In addition, the relative contents of α-helix and random coil increased first and then decreased, whereas the opposite trend was observed for the proportion of β-sheet, indicating changes in the secondary structure. These results showed that high-intensity ultrasound treatment could affect the physicochemical properties, structure and aggregation degree of myofibrillar proteins from crayfish meat, which could provide a reference for the application of ultrasound as an auxiliary approach in the processing and storage of crayfish.

Key words: Procambarus clarkii; myofibrillar proteins; structure; degree of aggregation; high-intensity ultrasound