Evidence against the non-enzymatic calcium theory of tenderization.

The objective of the present study was to determine whether variation in the tenderization of lamb longissimus could be attributed to variations in the rise in free calcium postmortem and sarcomere lengthening post rigor. The longissimus muscle of 10 crossbred lambs (Romney×Coopworth) was sampled at 1 and 7 days postmortem for determination of MIRINZ shear force, myofibrillar fragmentation index (MFI), sarcomere length, free calcium, and proteolysis of troponin-T. Despite considerable variation in tenderness and tenderization of the muscles, sarcomere lengthening was not observed. The concentration of free calcium at 7 days postmortem correlated significantly with the MFI (r=0.640; P<0.05) and tended to correlate with the shear force (r=-0.596; P<0.1) and degradation of troponin-T (r=0.625; P<0.1). Degradation of troponin-T was significantly correlated with tenderization (r=0.664; P<0.05). Troponin-T is a calpain substrate, but reportedly is not degraded through a direct effect from calcium. The present results, therefore, suggest that the variation in free calcium in postmortem muscle affects tenderization through an effect on the calpain system and not through a direct effect of calcium on myofibrillar proteins. Consequently, the results of this study do not support the (calcium) theory that calcium directly affects tenderization.