Composition of Collagen

The major component of connective tissue is the protein collagen, with minor components elastin, glycoproteins, and proteoglycans (61). Connective tissue comprises less than 2% of most skeletal muscles (2). Such a small amount of protein, however, has a major impact on the tenderness of the meat (when other factors such as cold shortening are avoided).

Extensive studies have shown that it is not only the amount of collagen but also the degree to which cross-links in collagen are solubilized during cooking that determine tenderness. Collagen has a high mechanical strength, brought about through the formation within the collagen fibers of intramolecular cross-links (2,61), which are co-valent in nature and result from a precise organization in the fiber. Two particular types of cross-links—an aldiminetype bond and a ketoimine-type bond—are replaced by more stable, nonreducible structures with increasing age. As the collagen molecules possess an extremely long biological half-life compared with most other proteins, changes in the numbers and type of cross-links tend to increase, causing the properties of the collagen to change with animal age. Thus, the fibers become progressively stronger and more rigid and less susceptible to enzymatic degradation and swelling by acids as the animals grow older. This maturation is achieved partly by further reactions to form multivalent cross-links that link several collagen molecules laterally, thus dramatically increasing the fiber stability.

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