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Updated: Jan 21, 2026

Isolation of Cardiomyocyte Nuclei from Post-mortem Tissue
Published on: July 10, 2012
Application of proteomic to investigate the post-mortem tenderization rate of different horse muscles
Antonella Della Malva1, Pasquale De Palo2, Josè Manuel Lorenzo3
1Department of Agricultural Food and Environmental Sciences, University of Foggia, Via Napoli, 25- 71121 Foggia, Italy.
Abstract:
The aim of this study was to evaluate the effect of post-mortem aging on tenderness development and proteolysis of myofibrillar proteins in 3 different horse muscles. Warner-Bratzler shear force decreased during aging in all muscles, showing the lowest values in longissimus lumborum (LL) in all sampling points. Myofibril fragmentation index significantly increased in LL and semimembranosus (SM) muscles throughout aging time whereas in semitendinosus (ST) it increased after 14 days of aging. Proteomics analysis revealed the major content of intact myofibrillar proteins with high molecular weight in ST muscle in the first phase of aging, while, after 14 days a higher accumulation of TnT-derived polypeptides and spots isoforms ascribed to MLC2 and MLC1 proteins were found. Data highlight that aging affects the meat tenderness and proteolysis with different intensities in each muscle and suggest that a more extensive post-mortem proteolysis occurred in ST muscle.
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