Molecular Biotechnology Group, Animal and Food Sciences Division, P.O. Box 84, Lincoln University, Canterbury, New Zealand.
Meat Sci. 2004 Jul;67(3):433-45. doi: 10.1016/j.meatsci.2003.11.016.
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.
本研究旨在利用 Ca(2+)和 Zn(2+)处理肉类，以批判性地探讨钙蛋白酶 3 在肉质嫩化中的可能作用。同时还检测了钙蛋白酶 1 和 2，用于比较目的。控制动物加上用 CaCl(2)、ZnCl(2)或 H(2)O 输注的动物（每组 6 只羔羊）用于确定死后储存过程中 Longissimus thoracis et lumborum（LTL）中肌肉钙蛋白酶 3 蛋白的时间变化。同时，还测定了（1）剪切力、（2）肌节长度、（3）titin 和 nebulin 的蛋白水解和（4）钙蛋白酶 1 和 2 蛋白的时间变化。与水输注和对照动物相比，LTL 中输注 Ca(2+)或 Zn(2+)分别导致 LTL 嫩度的显著上调和下调。此外，钙蛋白酶 3 的分解率、titin 和 nebulin 的蛋白水解率以及各种处理中 LTL 死后储存期间的肉嫩度变化率高度相关。这些研究表明，钙蛋白酶 3 与钙蛋白酶 1 一样，可能通过对 titin 和 nebulin 等特定肌肉结构蛋白的有限蛋白水解参与肉的嫩化。
