Effects of chilling rate on progression of rigor mortis in postmortem lamb meat. (30th March 2022)

• Record Type: Journal Article
• Authors: Yan, Tongjing; Hou, Chengli; Wang, Zhenyu; Li, Xin; Chen, Li; Liang, Ce; Xu, Yujun; Zhang, Dequan
• Is Part Of: Food chemistry. Volume 373:Part B(2022)
• Publication Date: 2022-03-30
• Subjects: Very fast chilling -- Chilling rate -- Rigor mortis -- Actomyosin ATPase -- μ-calpain; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2021.131463
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Rigor mortis was inhibited at a chilling rate of 15.10 °C/h. The super-contracted state of sarcomere was formed at a chilling rate of 15.10 °C/h. The changes in the activity of actomyosin ATPase and μ-calpain were key drivers. 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.