Meat tenderness: distribution of molecular species of collagen in bovine muscle

The collagen of bovine striated muscle has been shown to be comprised of three genetically distinct types of collagen, the proportions of which vary from the tendon to the endomysium. Despite the variation in genetic type all three collagens are stabilised by lysine‐derived cross‐links. It is proposed that the change in the tenderness of meat at temperatures above 65°C is caused by the tension generated during thermal contraction of all three types of collagen and that the extent is determined by the thermal stability of the intermolecular cross‐links. The relative contributions of each type of collagen remain to be elucidated.