4.7 Article

Postmortem proteolysis in three muscles from growing and mature beef cattle

Journal

MEAT SCIENCE
Volume 96, Issue 2, Pages 854-861

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2013.09.021

Keywords

Beef; Postmortem proteolysis; Calpain; Calpastatin

Funding

  1. Wise Burroughs Memorial Endowment in Animal Sciences research grant

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The objective of this study was to determine calpain system activity and postmortem protein degradation in three muscles from growing (n = 6,73 +/- 0.5 months) and mature (n = 6,106.7 +/- 43.1 months) beef cattle. The ratio of p-calpain:total calpastatin activity tended to be lower in mature animals (P = 0.08), suggesting reduced potential for proteolysis. Additionally, muscles from the mature group had greater calpastatin activity compared to calves at 6 days postmortem and had less p-calpain autolysis and troponin-T and titin degradation during the aging period (P < 0.01). Between the longissimus, semimembranosus, and triceps brachii muscles, the triceps brachii had the least postmortem proteolysis, with greater calpastatin activity and less troponin-T and titin degradation compared to other muscles (P < 0.01). These data suggest that calpastatin activity in muscle from older animals is more persistent postmortem. This difference may contribute to the decreased protein degradation and increased toughness of beef from mature cattle, even after aging. (C) 2013 Elsevier Ltd. All rights reserved.

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