Collagen content in meat

The collagen content of meat and meat products is often of particular interest to food processors because it alters batter gelation properties and in Germany the levels of collagen in meat products are governed by food laws.

Textural differences can be related to connective tissue properties as well as aging potential. Buffalo breeds have high collagen content, low collagen solubility and a tough texture.

The collagen content was 10-13% of total protein. Connective tissue in the buffalo meat had a bigger contribution to toughness.

The total concentration of connective tissue components were not closely related to the scores for muscles fiber tenderness.

Tenderness is highest in meat from very young animals but subsequently declines with age and physical activity, along with an increase in the amount of collagen and its degree of complexity.

The collagen content increased significantly with advancing age of the male Murrah buffaloes. A hydroxyproline content of 0.12% was recorded in high protein diet fed young male buffaloes.

The muscles from young buffaloes of 1 to 2 years showed less collagen (0.91 to 1.71 g/100g) than from 12 old buffaloes (1.16 to 2.23 g/100g).

During the growth and development of meat animals, covalent cross-links increase in number and collagen fibers become progressively stronger. Therefore, meat from older animals, tends to be tougher than meat from the same region of younger animals.

The water solubility of collagen under the action of heat decreases gradually with increasing age, with the result that the meat progressively becomes less tender.
Collagen content in meat

Copper role in formation of collagen

All copper metalloenzymes involve molecular oxygen or oxygen species in their reactions.

Copper plays a key role in the biosynthesis of the extracellular matrix proteins, collagen and elastin, through its function as a cofactor for the enzyme lysyl oxidase.

Lysyl is a secreted enzyme and it catalyzes cross-linking of collagen, which is necessary for proper collagen formation and integrity of all connective tissue.

Copper ion is being located at its active site. Since lysyl oxidase is a copper-dependent enzyme, impaired cross-linking can occur as a result of copper deficiency.

Inhibition of lysyl oxidase has profound effects on the strength of bone and elastic tissue.

Thus, copper is essential for formation and maintenance connective tissue and skeletal mineralization.
Copper role in formation of collagen