Abstract
ABSTRACTDifferential scanning calorimetry was used to monitor the thermal denaturation kinetics of myofibrillar proteins in bovine muscle at pH 5.6. The activation energy, pre‐exponential factor, rate constant and mean life time for each transition were calculated by means of a dynamic method. The kinetic values and the proposed reaction order (n= 1) were confirmed applying an isothermal method as a test. The position of the endothermal peaks proved to be pH dependent. Evidences suggest that peak III is a result of actin denaturation and possibly other thin filament proteins. Peaks I and II would represent the thermal transition of thick filaments. The number of bonds involved in each transition were estimated.
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