Up- and down-regulation of longissimus tenderness parallels changes in the myofibril-bound calpain 3 protein.

The objective of this study was to utilize Ca(2+) and Zn(2+) treatments of meat to critically explore the possible role of calpain 3 in meat tenderisation. Calpains 1 and 2 were also examined for comparative purpose. Control animals plus animals infused with CaCl(2), ZnCl(2) or H(2)O were used (six lambs per treatment) to determine the temporal changes in muscle calpain 3 protein in the Longissimus thoracis et lumborum (LTL) during post-mortem storage. Concurrently, the temporal changes of; (1) shear force, (2) sarcomere length, (3) proteolysis of titin and nebulin and (4) calpains 1 and 2 proteins were also determined. Infusing LTL with Ca(2+) or Zn(2+) caused significant up- and down-regulation of LTL tenderisation, respectively, compared to water infusion and the control animals. Furthermore, the rate of breakdown of calpain 3, the rate of proteolysis of titin and nebulin and the rate of meat tenderisation during post-mortem storage of LTL in the various treatments were highly correlated. These studies suggest that calpain 3, like calpain 1, may be involved in the tenderisation of meat through limited proteolysis of specific muscle structural proteins such as titin and nebulin.

Particulate metmyoglobin reducing activity and its relationship with meat color.

There is controversy about the effect of storage time on metmyoglobin (MetMb) reducing activity in the sarcoplasmic fraction of meat and the role of this reducing activity in maintaining the color of red meat. The presence of metmyoglobin reducing activity in the myofibrillar fraction of muscle extracts was investigated as a possible reason for this controversy. NADH-dependent MetMb reducing activity was found in the particulate fraction of meat following sedimentation of a meat homogenate at 35 000g. There was 5.8 times more MetMb reducing activity in the particulate fraction compared with that of the sarcoplasmic (supernatant) fraction. The presence of metmyoglobin reducing activity in the myofibrils (MMRA), defined as the activity in the sediment after centrifugation of a meat homogenate at 2 000g, was confirmed. The myofibrillar fraction contained 63% of the total MetMb reducing activity available in the meat. The relationship between muscle MetMb reducing activities and meat color parameters was investigated in a beef patties system. The particulate MetMb reducing activity (PMRA) in beef patties was found to be a good indicator of the total metmyoglobin reducing activity in meat and was positively correlated with the color parameters of the patties, suggesting that PMRA may be associated with red meat color of meat patties.