Abstract
This study evaluated the effect of multi-frequency sonication (20 kHz, 25 kHz, 28 kHz, 40 kHz, 50 kHz) on structural characteristics of beef myofibrillar proteins (MPs) with different degrees of doneness (Rare 52~55 °C, Medium Rare 55~60 °C, Medium 60~65 °C, Medium Well 65~69 °C, Well Down 70~80 °C, and Overcooked 90 °C). The results showed that surface hydrophobicity and sulfhydryl content increased with the increase in degree of doneness. At the same degree of doneness, the sulfhydryl group contents reached the maximum at a frequency of 28 kHz. In addition, the absolute value of ζ-potential was significantly decreased after ultrasonic treatment (p < 0.05). SDS gel electrophoresis showed that the bands of beef MPs were not significantly affected by various ultrasonic frequencies, but the bands became thinner when the degree of doneness reached overcooked. Fourier transform infrared spectrum showed that with the increase of ultrasonic frequency, α-helix content decreased, and random coil content significantly increased (p < 0.05). The results of atomic force microscopy indicated that the surface structure of beef MPs was damaged, and the roughness decreased by sonication, while the roughness significantly increased when the degree of doneness changed from medium to overripe (p < 0.05). In conclusion, multi-ultrasound combined with degree of doneness treatment alters the structural characteristics of beef MPs.