Pressure-induced conversion of α-connectin to β-connectin.
Pressure-induced conversion of α-connectin to β-connectin.
复制标题
压力诱导的α-连接蛋白向β-连接蛋白的转化。
DOI：
10.1016/0309-1740(92)90110-p
复制
发表时间：
1992
期刊：
影响因子：
7.1
通讯作者：
A. Suzuki
中科院分区：
文献类型：
--
作者：
K. Kim;Y. Ikeuchi;A. Suzuki
压力诱导肉嫩化的机理尽管有其有益的效果，但尚未完全确定。为研究加压处理对肌原纤维大结构蛋白的影响，在低温（0-2°C）条件下，对家兔骨骼肌施加100-300 MPa的静水压10 min，观察到加压处理与对照组肌原纤维连接蛋白（也称肌联蛋白）电泳图谱的显著差异。α-连接蛋白（2800 kDa）向β-连接蛋白（2100 kDa）的转化随着施加于肌肉的压力的增加而加速，并且nebulin（800 kDa）通过压力处理而降解。如果说α-连接蛋白向β-连接蛋白的转化对肉的嫩化有一定的影响，那么压力诱导的α-连接蛋白向β-连接蛋白的转化可能是压力诱导肉嫩化的原因之一。
The mechanism of the pressure-induced tenderization of meat has not been fully established in spite of its beneficial effect. To detect the changes in the large structural proteins of the myofibrils induced by pressurization without heat treatment, high hydrostatic pressure (100–300 MPa) was applied to rabbit at-death skeletal muscle for 10 min at low temperature (0–2°C).Significant differences in the electrophoretic pattern of connectin (also called titin) in isolated myofibrils were observed between the control and pressurized muscle samples. The conversion of α-connectin (2800 kDa) to β-connectin (2100 kDa) was accelerated with increasing pressure applied to the muscle; also nebulin (800 kDa) was degraded by pressure treatment.From the results it is clear that the degradation of connectin is induced by pressurization alone without heat treatment. If the conversion of α-connectin to β-connectin during conditioning has some influence on meat tenderization, the pressure-induced conversion of α- to β-connectin is possibly one of the causes of pressure-induced tenderization of meat.