Relationship between pyridinoline concentration and thermal stability of bovine intramuscular collagen.
Semimembranosus muscle samples were obtained from 49 Holstein beef animals representing different USDA maturities. Intramuscular collagen (IMC) was isolated in the frozen state and evaluated for heat-labile collagen solubility (% Sol), thermal shrinkage temperature (Ts), enthalpy (Hs) changes, and mature crosslink (pyridinoline) content. These measures were obtained to elucidate a relationship between pyridinoline content of IMC and beef maturity level and to relate IMC thermal stability (% Sol, Ts, and Hs) to pyridinoline content. With increasing maturity, % Sol decreased (P less than .01) and Ts increased (P less than .01), whereas Hs showed no change (P greater than .05). Thus, IMC melted at increasing temperatures, but the amount of energy required to induce this endothermic change remained constant throughout maturation. The pyridinoline content of IMC increased (P less than .01) linearly with maturity, indicating that this heat-stable, mature crosslink enhances thermal stability of IMC as beef muscle matures. Significant correlations between pyridinoline content and maturity (r = .56; P less than .001) and Ts (r = .34; P less than .05) support this contention.
Smith
S H
SH
Purdue University, West Lafayette, IN 47907.
Judge
M D
MD
D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D003094:Collagen / Q000737:chemistry* / Q000302:isolation & purification; D004355:Drug Stability; D006358:Hot Temperature; D008460:Meat / Q000592:standards; D009132:Muscles; D012995:Solubility
D000596:Amino Acids; C015484:pyridinoline; D003094:Collagen