文献类型: 外文期刊
作者: Yan T.; Hou C.; Wang Z.; Li X.; Chen L.; Liang C.; Xu Y.; Zhang D.
作者机构:
关键词: Chemical activation; Actomyosin atpase; ATPases; Calpains; Chilling rate; Control groups; Myofibrils; Rigor morti; Shear force; Very fast chilling; Μ-calpain; Dissociation; calpain 1; desmin; myosin adenosine triphosphatase; structural protein; troponin T; animal tissue; Article; carcass; cell ultrastructure; cold stress; controlled study; core temperature; dissociation; electrostimulation; enzyme activity; force; induced hypothermia; lamb; lamb meat; low temperature; muscle fibril; nonhuman; pH; protein degradation; rigor mortis; sarcomere; sarcomere length; sarcoplasmic reticulum; storage; animal; meat; postmortem change; red meat; sheep; skeletal muscle; Animals; Hydrogen-Ion Concentration; Meat; Muscle; Skeletal; Postmortem Changes; Red Meat; Rigor Mortis; Sheep
期刊名称: Food Chemistry
ISSN: 0308-8146
年卷期: 2022 年 373 卷
页码:
收录情况: SCIE(2022版) ; EI(2022版)
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. © 2021 Elsevier Ltd
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