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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers.

The objectives of this study were to examine the effects of castration on the calpain proteinase system (mu-calpain, m-calpain, and calpastatin) activities and meat tenderness. Six each, MARC III bulls and steers were slaughtered at approximately 12 mo of age. Longissimus muscle samples were obtained for determining myofibril fragmentation index, Warner-Bratzler shear force, and sensory panel evaluation at 1, 7, and 14 d postmortem, and mu- and m-calpain and calpastatin activities at 24 h postmortem. Bulls produced leaner carcasses with lower (P < .05) quality grades than did steers. Meat from bulls had higher (P < .05) shear force values than meat from steers; however, sensory panelists were unable (P > .05) to detect differences in tenderness or other sensory traits between bulls and steers. Activities of mu- and m-calpain were not affected (P > .05) by castration; however, calpastatin was higher (P < .05) in muscles from the bull carcasses. Lower (P < .05) myofibril fragmentation index values indicate that less proteolysis occurred in muscle from bulls than in muscle from steers during the first 7 d postmortem. Greater calpastatin 24-h activity may be associated with the increased shear force of meat from bulls.[1]

References

  1. Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers. Morgan, J.B., Wheeler, T.L., Koohmaraie, M., Savell, J.W., Crouse, J.D. J. Anim. Sci. (1993) [Pubmed]
 
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