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This Article Full Text Full Text (PDF) All Versions of this Article: jas.2007-0549v1 86/4/960    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Underwood, K. R. Articles by Du, M. Search for Related Content PubMed PubMed Citation Articles by Underwood, K. R. Articles by Du, M.

Caspase 3 is not likely involved in the postmortem tenderization of beef muscle¹

Department of Animal Science, University of Wyoming, Laramie, WY 82071

² Corresponding author: mindu{at}uwyo.edu

Postmortem proteolysis is an important determinant of beef tenderness. Caspase 3 is a protease that functions in apoptosis and has been shown to degrade myofibrillar proteins. Our objective was to evaluate whether caspase 3 activity is related to beef tenderness and muscle growth, and whether caspase 3 is activated in postmortem beef muscle. In experiment 1, longissimus thoracis (LT) and sternomandibularis muscle samples were obtained at 0, 0.25, 1, 3, 24, 72, and 240 h postmortem from 5 steers. In experiment 2, a group of 40 beef cattle was slaughtered at the University of Wyoming Meat Lab with 10 steers of different tenderness and growth characteristics chosen for the analysis of caspase 3 activity in the LT. In experiment 3, 10 steers with different tenderness but matched growth characteristics were chosen for analyses. In experiment 1, no significant activation (P = 0.70) of caspase 3 activity was detected; only a decreased activity at 72 (P = 0.05) and 240 h (P = 0.02) postmortem was observed. Western blot analysis of both muscle samples showed only the pro-caspase 3 form and failed to detect the activated enzyme. In experiment 2, caspase 3 activity in the LT immediately postmortem was greater (P = 0.05) for the cattle with increased Warner-Bratzler shear force values. No difference in caspase 3 activity was detected for experiment 3. Our results demonstrate that caspase 3 activity is not activated, with its activity decreasing with time postmortem, and caspase 3 activity is not associated with Warner-Bratzler shear force at slaughter. Therefore, caspase 3 is not anticipated to be involved in postmortem tenderization of beef.

Key Words: beef • caspase 3 • postmortem • proteolysis • tenderness