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Specific effects on strength and heat stability of intramuscular connective tissue during long time low temperature cooking

Latorre, María E., Palacio, María I., Velázquez, Diego E., Purslow, Peter P.
Meat science 2019 v.153 pp. 109-116
collagen, cooked foods, cooking, denaturation, differential scanning calorimetry, endothermy, energy, enzymatic hydrolysis, heat stability, meat, meat tenderness, temperature, trypsin
Long-time low-temperature (LTLT) cooking of meat is known to produce a tender product. The current work tested the hypothesis that LTLT cooking for periods of up to 24 h at 60 °C reduces the contribution of intramuscular connective tissue to cooked meat toughness. Tensile tests on perimysium excised after cooking showed that its strength diminished with cooking time, although not as markedly as the Warner-Bratzler peak force measure of toughness. A gradually increasing susceptibility to trypsin digestion with increasing heating time demonstrated that there was a slow and gradual increase in the proportion of denatured collagen in the perimysium. Differential scanning calorimetry on perimysium excised after cooking showed an endothermic peak representing the denaturation of the collagen not already denatured on cooking. With increasing cooking time, the energy per milligram of collagen necessary to denature this remaining fraction increased. These results support the hypothesis that there is both an easily destabilized and more resistant fractions of the collagen in intramuscular connective tissue.