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Journal of Animal Science





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This study was conducted to determine degradation of the giant myofibrillar proteins titin and nebulin in postmortem aged beef, with known tenderness values, from animals differing in sex (steers vs bulls) and age (cows vs steers and bulls). Ten bulls and 10 steers (both groups were approximately 14 mo old) and 10 cows (44 to 108 mo old) were slaughtered. Longissimus muscle samples were removed for determination of Warner-Bratzler shear force, sensory panel tenderness evaluation, and SDS-PAGE analysis at 3, 7, 14, and 28 d postmortem. The SDS-PAGE analysis of titin and nebulin revealed that titin often migrated as three closely-spaced bands (T1, T1-2, T2, in increasing order of migration) in 3-d postmortem samples. With increasing time post-mortem, intact titin (T1) decreased and degraded titin (T2) increased in all samples. Within a class (i.e., steers, bulls, or cows) the rate of conversion of T1 to T2 was slower in the less-tender samples. The T1 to T2 conversion postmortem was slower in the intact males (bulls) than in the castrated males (steers). The T1 to T2 conversion postmortem also was slower in the older animals (cows) in comparison to the younger steers, but not in comparison to the younger bulls. Nebulin was degraded by 3 d postmortem in tender samples from steers, but some nebulin remained in the less-tender 3-d samples from steers and in all of the 3-d samples from bulls and older animals (cows). Intact nebulin was absent in all 7-d samples, regardless of the class of animal. Our results suggest that titin and nebulin are degraded at faster rates in more tender beef samples within each of the three classes of animals examined. The rate of degradation seems to differ when sex and age classifications are compared.


This article is from Journal of Animal Science 73 (1995): 1064–1073. Posted with permission.

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American Society of Animal Science



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