Ilian Mohammad A, Bekhit Alaa El-Din, Bickerstaffe Roy
Molecular Biotechnology Group, Animal and Food Sciences Division, PO Box 84, Lincoln University, Canterbury, New Zealand.
Meat Sci. 2004 Feb;66(2):387-97. doi: 10.1016/S0309-1740(03)00125-6.
The objective was to study the potential role of calpain 3 in postmortem myofibril breakdown and meat tenderization. We determined the temporal changes in calpain 3 protein in the ovine m. longissimus thoracis et lumborum (LTL, n=4) during post-mortem storage. Concurrently, we also determined the kinetics of tenderization level, changes in MFI, degradation of nebulin and desmin, and autolysis of calpain 1. The autolysis of calpains 1 and 3 were strongly correlated with the kinetics of tenderization and changes in MFI. The best correlation was between the appearance of the autolyzed calpains 1 and 3 and nebulin degradation. Taken together, the results indicated that calpains 1 and/ or 3 might be playing a key role in post-mortem tenderization of LTL via the proteolysis of specific muscle structural proteins such as nebulin. This is the first report that relates calpain 3 to myofibrillar protein degradation in post-mortem skeletal muscle.
目的是研究钙蛋白酶3在宰后肌原纤维分解和肉嫩化过程中的潜在作用。我们测定了宰后储存期间绵羊胸腰最长肌（LTL，n = 4）中钙蛋白酶3蛋白的时间变化。同时，我们还测定了嫩化水平的动力学、肌原纤维小片化指数（MFI）的变化、伴肌动蛋白和结蛋白的降解以及钙蛋白酶1的自溶。钙蛋白酶1和3的自溶与嫩化动力学和MFI的变化密切相关。自溶的钙蛋白酶1和3的出现与伴肌动蛋白降解之间的相关性最佳。综上所述，结果表明钙蛋白酶1和/或3可能通过对特定肌肉结构蛋白（如伴肌动蛋白）的蛋白水解作用在LTL宰后嫩化过程中起关键作用。这是第一份将钙蛋白酶3与宰后骨骼肌中肌原纤维蛋白降解相关联的报告。
