Takahashi K, Hattori A, Kuroyanagi H
Meat Science Laboratory, Department of Animal Science, Faculty of Agriculture, Hokkaido University, Sapporo, Japan.
Meat Sci. 1995;40(3):413-23. doi: 10.1016/0309-1740(95)00038-m.
The weakening effect of paratropomyosin on rigor linkages formed between actin and myosin was determined by measuring the restoration of rigor-shortened sarcomeres of chicken, pork and beef. We observed the rate of the post-mortem translocation of paratropomyosin from the A-I junction region of sarcomeres onto the thin filaments in the A-band, where rigor linkages had been formed; this agreed well with the rate of increase in length of rigor-shortened sarcomeres. The sarcomere lengths were found to be maximum at 1, 7 and 10 days post-mortem in chicken, pork and beef, respectively. Thus, translocated paratropomyosin weakens rigor linkages and brings about the recovery in the length of rigor-shortened sarcomeres. Paratropomyosin stimulates the resolution of rigor mortis, and is a key factor in meat tenderization during post-rigor ageing. These results powerfully support the 'Calcium theory of meat tenderization' which we have proposed.
通过测量鸡、猪和牛肉僵直缩短肌节的恢复情况，确定了原肌球蛋白对肌动蛋白和肌球蛋白之间形成的僵直连接的减弱作用。我们观察到原肌球蛋白在死后从肌节的A-I连接区域转移到A带中的细肌丝上的速率，在该区域已形成僵直连接；这与僵直缩短肌节长度增加的速率非常吻合。发现鸡、猪和牛肉的肌节长度分别在死后1天、7天和10天时达到最大值。因此，转移的原肌球蛋白会减弱僵直连接，并使僵直缩短的肌节长度恢复。原肌球蛋白刺激尸僵的缓解，是僵直后熟化过程中肉嫩化的关键因素。这些结果有力地支持了我们提出的“肉嫩化的钙理论”。
