Myofibril degradation and structural changes in myofibrillar proteins of porcine longissimus muscles during frozen storage

The effect of frozen time and the temperature on myofibril degradation and the structure of myofibrillar proteins of porcine longissimus muscles were investigated. With extended frozen time and increased temperature, the muscle fibres became broken; the muscle cells became irregularly arranged; and the fragmentation index value, number of ionic bonds, and number of hydrogen bonds of the samples significantly decreased. Meanwhile, the myofibril fragmentation index value, number of hydrophobic interactions, and number of disulphide bonds significantly increased (P < 0.05). After 12 months of storage, the intensities of I-760/I-1003, I-850/I-830, I-1450/I-1003, and I-2945/I-1003 in the samples frozen at -8 C-degrees were reduced by 4.36 %, 1.28 %, 1.86 %, and 0.74 %, respectively. A reduction in the maximum absorption peak and a red shift were observed in the ultraviolet spectrum. Therefore, frozen storage resulted in significant damage to the tissue microstructureand caused accelerated protein degradation, and the loss of protein structural integrity.