Abstract
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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