The objective of this study was to determine associations of small heat shock proteins (sHSPs) in tenderness development of loins from callipyge and normal genotype lambs. Loins (M. longissimus lumborum) from sixteen lambs across four genotypes were collected throughout 9 days of postmortem aging. The loins from callipyge lambs had more intact desmin and troponin T throughout aging periods, as well as less μ-calpain autolysis and more calpastatin compared to loins from other genotypes (P < 0.05). Delayed onset of apoptosis was found in the callipyge loins indicated by less cytochrome c and more inactive procaspase-3 compared to normal lamb loins (P < 0.05). Less degraded HSP27 was also consistently found in the callipyge loins compared with loins from normal lambs (P < 0.001). The results found up-regulation of anti-apoptotic activities coincided with toughness in callipyge loins, which suggest apoptosis is likely involved in postmortem proteolysis and subsequent meat tenderization.
Keywords: Apoptosis; Callipyge; Heat shock protein 27; Meat tenderization; Postmortem proteolysis.
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