Contraction state of beef muscle at onset of rigor influences tenderness of cooked meat. Loss in tenderness during cooking has been related, through use of differential scanning calorimetry (DSC), to thermal denaturation of myofibrallar proteins.
Differential scanning calorimetry (DSC) was used to follow the changes in the endothermic transitions of beef muscle during conditioning. Sternomandibularis muscle held at 5ºC from 2-8 days post-mortem resulted in a significant (P < 0.05) drop in total heat of transition (ΔH) from 3.8 to 3.0 J/g. The myosin transition decreased from 57.8º to 55.2ºC while the actin transition increased
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Semi-purified chicken pepsin was prepared from proventriculae at a yield of 33% of the original pepsin activity using a procedure based on the method described by Bohak (1970). Cheddar cheese was produced using the chicken pepsin preparation, and with calf rennet as a control, in two trials. The enzymes were standardized to the same milk-clotting strength on Berridge’s substrate at
Warner-Bratzler shear, Instron compression and extension were screened for sensitivity to the textural changes caused by heating scallop (Placopecten magellanicus) adductor muscle. Instron compression, expressed as hardness, was selected since it gave the greatest slope with respect to temperature. Previously frozen commercial scallop were heated to internal temperatures of 25 to 80 ºC. A linear increase in hardness of 0.033