Tenderness is an important determinant of meat quality. Inconsistency and variability in tenderness have been identified as major problems for the meat industry (Morgan et al., 1991). It is well documented that tenderness improves during postmortem storage of meat but the mechanisms involved remain controversial. The general consensus is that proteolysis of structural muscle proteins causes tenderisation but alternative theories suggest that changes in the actin-myosin interaction (Goll et al., 1997) or a non-enzymatic effect of calcium on muscle proteins (Takahasi, 1999) or a rise in ionic strength (Ouali, 1990) may be involved. However, discussion of these theories is not within the scope of this review. With regard to postmortem proteolysis, the calpain system is thought to play a major role. Calpains are calcium-activated proteases with an optimum activity at neutral pH. In skeletal muscle, the calpain system consists three proteases, m-calpain, m-calpain and skeletal muscle-specific calpain, p94, and an inhibitor of m- and m-calpain, calpastatin. The involvement of calpains in postmortem tenderisation has been the subject of several reviews (Goll et al., 1991; Koohmaraie, 1988, 1992a, 1994, 1996; Ouali, 1990). Since these reviews, new information has become available which has provided answers to some of the questions on the role of calpains in postmortem tenderisation. The purpose of this review is to discuss some of these issues in the context of recent results. For further information on postmortem proteolysis and meat tenderness, or characteristics of the calpain system, the reader is referred to a number of excellent reviews (Penny, 1980; Greaser, 1986; Croall and DeMartino, 1991; Ouali, 1992; Sorimachi et al., 1994; Ono et al., 1998).

GH, Geesink, MA Ilian, JD Morton, and R Bickerstaffe

Proceedings of the New Zealand Society of Animal Production, Volume 60, Hamilton, 99-102, 2000
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