Effect of chilling rate on heat shock proteins abundance, myofibrils degradation and caspase‐3 activity in postmortem muscles. (7th August 2022)

• Record Type: Journal Article
• Authors: Huang, Caiyan; Ijaz, Muawuz; Chen, Li; Xiang, Can; Liang, Ce; Li, Xin; Blecker, Christophe; Wang, Zhenyu; Zhang, Dequan
• Is Part Of: International journal of food science & technology. Volume 57:Number 10(2022)
• Page Start: 6492
• Page End: 6502
• Publication Date: 2022-08-07
• Subjects: Apoptosis -- heat shock proteins -- lamb -- postmortem chilling -- structural proteins -- tenderness; Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.15985
• Languages: English
• ISSNs: 0950-5423

Abstract

Summary: The objective of this study was to investigate the effect of chilling rate on heat shock proteins (HSP) abundance, myofibrillar proteins degradation and caspase‐3 activity of lamb muscle in postmortem. Eighteen longissimus dorsi (LD) muscles from lamb were treated under three different chilling rates—very fast chilling I (VFC‐I, 22.2 °C h −1 ), very fast chilling II (VFC‐II, 32.4 °C h −1 ) and control (1.44 °C h −1 )—and stored at −1 °C, −1 °C and 4 °C for 120 h postmortem, respectively. The results showed that myofibril fragmentation index (MFI), the abundance of αβ‐crystallin and HSP20, as well as the degradation of HSP27, HSP70, troponin‐T and desmin under the VFC‐I and VFC‐II groups were higher than control. Notably, HSP90 abundance may not be affected by the chilling rate in the late postmortem aging. Additionally, with increasing of chilling rate for postmortem muscle could inhibit caspase‐3 activity. Overall, results indicated that chilling rate may affect the process of meat tenderization by changing the abundance levels of heat shock proteins, myofibrillar degradation and apoptotic pathway. Abstract : Very fast chilling treatment could increase the myofibril fragmentation index value, the abundance of αβ‐crystallin and HSP20, and the degradation of HSP27, HSP70, troponin‐T and desmin, as well as inhibit caspase‐3 activity in postmortem, and then improve meat tenderness.