U.S. Department of Agriculture: Agricultural Research Service, Lincoln, Nebraska
Date of this Version
2004
Document Type
Article
Citation
Published in Meat Science 68 (2004) 635–640.
Abstract
The objective of this experiment was to determine age-related changes in collagen concentration, sarcomere length, calpain (μ- and m-) and calpastatin activities, postmortem proteolysis and Warner–Bratzler shear force (WBSF) in ovine longissimus thoracis et lumborum. Rambouillet lambs were slaughtered at 2, 4, 6, 8 and 10 months of age and samples of longissimus were collected at 0, 2 and 10 days postmortem. Collagen concentration and sarcomere lengths were determined from the cores used for WBSF measurements and reflected changes in the background toughness. Longissimus collagen concentration did not change (P > 0.05) due to lamb age. Sarcomere lengths also showed age-related changes, increasing (P < 0.05) from 1.35 μm at 6 months to 1.48 and 1.55 μm at 8 and 10 months, respectively. The extent of calpain mediated proteolysis determines the improvement in meat tenderness with postmortem storage. The most notable change in the calpain proteolytic system was the decline (P < 0.05) in calpastatin activity from 4.18 to 1.91 U/g muscle between 2 and 10 months. The activity of μ-calpain showed a 16% increase (P < 0.05) from 4 to 6 months, before it dropped again at 8 and 10 months. There was a gradual decline (P < 0.05) in m-calpain activity with age, and by 10 months μ-calpain activity had reduced to 80% of 2 months levels. The ratio of μ-calpain to calpastatin activities increased (P < 0.05) from 2 to 6 months (from 0.31 to 0.56) with no further changes (P > 0.05) at 8 or 10 months. There were no age-related changes (P > 0.05) in desmin degradation at day 2, however, examination of day 10 samples showed increased (P < 0.05) degradation from 2 to 6 months. Thus, the changes observed in the ratio of μ-calpain to calpastatin activities are reflected in the extent of postmortem proteolysis. Meat tenderness was measured using WBSF at 2 and 10 days postmortem. Because little proteolysis had taken place at 2 days postmortem, the decline in day 2 WBSF from 6 to 8 months could be explained by changes in sarcomere length. However, at 10 days postmortem, where WBSF was shown to decrease from 2 to 8 months, the improvement in tenderness could be explained by the amount of postmortem proteolysis. The data presented in this paper show evidence that sarcomere length is the main determinant of background toughness in ovine longissimus, and that postmortem proteolysis, resulting from μ-calpain activity regulated by calpastatin, is the main determinant of ovine longissimus tenderization during aging. Thus, lamb longissimus tenderness after refrigerated storage is determined by postmortem proteolysis and its interaction with sarcomere length.