尸僵
肌原纤维
肌节
死后变化
化学
卡尔帕因
ATP酶
生物化学
解剖
生物
酶
医学
内分泌学
病理
心肌细胞
作者
Tongjing Yan,Chengli Hou,Zhenyu Wang,Xin Li,Li Chen,Ce Liang,Yujun Xu,Dequan Zhang
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2021-10-26
卷期号:373 (Pt B): 131463-131463
被引量:44
标识
DOI:10.1016/j.foodchem.2021.131463
摘要
This work investigated the effects of chilling rate on the progression of rigor mortis and explored possible mechanisms. Silverside from 18 lamb carcasses was assigned to control group (1.94 °C/h), very fast chilling-I group (VFC-I, 12.19 °C/h) and VFC-II group (15.10 °C/h). The shear force, myofibril fragmentation index (MFI), actomyosin ATPase activity, protein degradation and actomyosin dissociation were determined. There was no increase in the shear force in VFC-II group. The activation of actomyosin ATPase at 2-4 h postmortem in VFC-II group resulted in super-contracted sarcomeres and an increase in MFI. The degradation of μ-calpain, troponin T and desmin in VFC-II group was higher than that in control group from 6 to 24 h postmortem. These results suggested that rigor mortis was influenced which resulted in decreased shear force at a chilling rate of 15.10 °C/h by activating actomyosin ATPase and μ-calpain at early postmortem and promoted actomyosin dissociation.
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