Desmin as molecular chaperone for myofibrillar degradation during freeze-thaw cycles

Abstract

This study investigated the relationship of secondary protein structures with textural attributes of chicken breast subjected to 6 freeze (-20 °C) thaw (4 °C for 12 h) cycles. 2DE identified 78 distinct protein spots. Moreover, WB indicated a remarkable increase in the degree of desmin degradation during multiple freeze-thaw (MFT). In addition, the TEM micrographs revealed that MFT remarkably increased the spacing between the muscle fibers, especially from cycles 3 to 5, slightly decreased H-zone, but a remarkable shrinkage of Z-lines, as well as degradation of myofibril structures (Z-line, I-bands, and M-lines). DSC showed shifts in first and second endothermic transition peaks during the 3rd and 5th cycles. Viscoelastic graphs revealed a cycle-dependent decrease in gel-forming ability (G') during MFT. Finally, the MFT chicken breast samples exhibited significantly decreased shear force in a cycle-dependent manner. This study highlighted the critical role of desmin in regulating myofibrillar degradation through various routes and mechanisms.

Keywords: 2D electrophoresis; Chicken-meat; Meat-quality; Muscle-ultra-structure; Protein degradation; Rheology; Shear-force.