Relationship between pyridinoline concentration and thermal stability of bovine intramuscular collagen
1991
Smith, S.H. | Judge, M.D.
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 < .01) and Ts, increased (P < .01), whereas Hs showed no change (P > .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 < .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 < .001) and Ts (r = .34; P < .05) support this contention.
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