ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1985.tb10530.x
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