LAUSR

Intramuscular collagen may affect the value of meat by limiting its tenderness and cooking convenience. Production factors such as age of animal at slaughter, the use of steroids and beta-adrenergic agonists as growth promotants, and cattle breed may affect the contribution of collagen to beef quality. Recent research has indicated that concentrations of the mature collagen cross-link pyridinoline (PYR) are positively correlated with Warner-Bratzler shear force (WBSF) and animal age at slaughter, while contribution of the concentration of a second mature collagen cross-link Ehrlich's Chromogen (EC) to beef toughness declines with cattle age. Cattle breed influences total collagen content of muscle due to differing rates of maturation among breeds. Growth promoting technologies do not appear to affect collagen solubility, but do influence PYR and EC densities and concentrations in some beef muscles. Concentrations of PYR and EC do not account for all the variation in collagen heat solubility in beef muscles, nor do advanced glycation end products given the relative immaturity of cattle at slaughter. In light of this, other collagen cross-links such as heat-stable divalent cross-links may warrant reconsideration with regard to their contribution to cooked beef toughness.