Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, PR China.
Food Chem. 2013 Nov 15;141(2):675-9. doi: 10.1016/j.foodchem.2013.04.034. Epub 2013 Apr 19.
The objectives of this study, were to examine the relationship between duck meat tenderness, actomyosin dissociation and endogenous enzyme activities when heating the duck breast muscle, to the internal temperature of 30, 40, 50, 60, 70, 80, 90°C. The shear force increased in the temperature range of 30-50°C and 70-90°C and decreased from 50 to 70°C, which was negatively related with liberated actin (P<0.05). The activity of cathepsin B and L was stable while heating the meat to a temperature below 50°C, then it decreased rapidly with temperature increase. The calpain activity kept decreasing with the temperature increase. There was no significant change in the cathepsin D activity below 70°C but it declined rapidly thereafter, and its activity was strongly correlated with actomyosin dissociation (P<0.05). The results suggest that actomyosin dissociation and cathepsin D, could contribute to the tenderness of duck meat during the cooking process.
本研究旨在探讨鸭肉嫩度、肌球蛋白解离和内源性酶活性与鸭胸肌肉加热至 30、40、50、60、70、80、90°C 内部温度之间的关系。剪切力在 30-50°C 和 70-90°C 的温度范围内增加，在 50-70°C 之间降低，与游离肌动蛋白呈负相关（P<0.05）。组织蛋白酶 B 和 L 的活性在低于 50°C 加热肉时保持稳定，然后随着温度的升高迅速下降。钙蛋白酶活性随着温度的升高而持续下降。在 70°C 以下，组织蛋白酶 D 的活性没有明显变化，但此后迅速下降，其活性与肌球蛋白解离呈强相关（P<0.05）。结果表明，肌球蛋白解离和组织蛋白酶 D 可能有助于鸭肉在烹饪过程中的嫩度。
