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It is known that bovine muscles stored before the rigor mortis in low temperature cause the cold shortening. This study was carried out in order to clarify the relation of weakening of myofibrillar structure during storage on meat tenderization of cold shortened bovine semimembranous muscle. The muscle was excised immediately after slaughter from the dressed carcass and divided into muscle blocks, and then stored antiseptically at 4°C. The muscle restrained for two days on the carcass was excised on day 3 postmortem and similarly treated. The value of breaking strength and elasticity of both muscles gradually decreased with the postmortem time. However, the values of both breaking strength and elasticity in the excised muscle decreased but less than the restrained muscle, showing that the cold shortening developed in the immediately excised muscle. Measurement on the weakening of the myofibrillar structures of the cold shortened muscle showed that the weakening of the Z-disks progressed linearly after 3 days postmortem, agreeing with decline of the stiffness of the muscle. The weakening of the interaction between actin and myosin that affects sarcomere length hardly occurred throughout the storage time. And, the degradation of α-connectin rapidly progressed after 4 days postmortem. These results suggest that the weakening of the Z-disks and the degradation of connectin filaments were related to the tenderization of uncooked cold shortened bovine muscle during postmortem storage.

Myofibrillar Structural Weakening and Tenderization of Uncooked Cold Shortened Bovine Muscle during Postmortem Storage