Denaturation kinetics of myofibrillar proteins in bovine muscle

WAGNER, J.R; AÑON, MARÍA CRISTINA

JOURNAL OF FOOD SCIENCE

WILEY-BLACKWELL PUBLISHING, INC

Lugar: Londres; Año: 1985 vol. 50 p. 1547 - 1550

0022-1147

Differential 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.