Abstract
The objective of this study was to determine the proteolytic changes of myofibrillar and small heat shock proteins (HSPs) in different muscles during aging and to evaluate their relevance to meat quality attributes. From 8 beef carcasses, longissimus lumborum (LL), semimembranosus (SM), and psoas major (PM) muscles were obtained, cut into sections and assigned to various aging periods up to 23d. PM exhibited limited aging potential in quality developments shown by lower extents of shear force, water-holding capacity (WHC), and proteolytic changes, including calpain 1 autolysis, troponin T, and HSP27 compared to LL and SM. Conversely, LL had an increase in tenderization and WHC, which was accompanied with more extended calpain 1 autolysis, proteolysis and HSP27 degradation, compared with other muscles. The results of this study suggest that postmortem proteolytic changes of myofibrillar proteins, small HSPs and apoptotic factors occur in a muscle-specific manner, which is likely attributed to different rate and extent of meat quality developments of each muscle during aging.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
