Title of article :
Postmortem proteolysis in three muscles from growing and mature beef cattle
Author/Authors :
Cruzen، نويسنده , , Shannon M. and Paulino، نويسنده , , Pedro V.R. and Lonergan، نويسنده , , Steven M. and Huff-Lonergan، نويسنده , , Elisabeth، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2014
Pages :
8
From page :
854
To page :
861
Abstract :
The objective of this study was to determine calpain system activity and postmortem protein degradation in three muscles from growing (n = 6, 7.3 ± 0.5 months) and mature (n = 6, 106.7 ± 43.1 months) beef cattle. The ratio of μ-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 μ-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.
Keywords :
calpain , Postmortem proteolysis , beef , Calpastatin
Journal title :
Meat Science
Serial Year :
2014
Journal title :
Meat Science
Record number :
1491463
Link To Document :
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