The relationship between animal age and the thermal stability and cross-link content of collagen from five goat muscles
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Updated: May 27, 2026

Exploring the Longissimus Muscle: Unraveling its Correlation with Meat Quality in Bos indicus and Crossbred Bulls
Published on: July 12, 2024
D J Horgan1, P N Jones, N L King
1CSIRO Division of Food Research, Meat Research Laboratory, P.O. Box 12, Cannon Hill, Queensland 4170, Australia.
Abstract:
The thermal stability of intramuscular collagen, as determined using differential scanning calorimetry, was measured in five muscles from 75 goats with known birth dates ranging in age from one day to 13 years. The collagen cross-link pyridinoline, and the collagen-associated, and putative cross-link, Ehrlich Chromogen were also measured. Five different muscles were examined and the effects of age compared to those found in the tendon of the longissimus dorsi muscle. The differences between intramuscular collagen and tendon collagen were found to be much greater than those between the intramuscular collagens of different muscles. Intramuscular collagen is more thermally stable than tendon collagen due to higher levels of heat-stable cross-links. However the increase in thermal stability of intramuscular collagen with age could not be explained simply in terms of the cross-links measured.
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