The thermal stabilities of the proteins of a range of fish muscles of
different habitat temperatures were determined by differential scanning
calorimetry before and after frozen storage at 20°C.
In whole muscle a clear relationship was seen between habitat
temperature and the thermal denaturation of myosin, which persisted when
isolated myosins were analysed under conditions close to physiological
pH and ionic strength. the ionic environment of the myosin molecules in
the whole tissue will, however, not be exactly the same as in the myosin
No significant correlations were seen between habitat temperature,
ultimate pH and other analytical parameters.
After frozen storage, the myosin transitions in red snapper, a warm
water species, was markedly changed in whole muscle but not in isolated
myosin, suggesting the post mortem development of an interaction with
other muscle proteins. In contrast, in cod, a cold water species,
changes in myosin transitions were very similar, both in whole muscle
and isolated myosin.
The implications of species differences in the ‘melting’ of myosin
domains and changes in textural quality during frozen storage are
Davies, J.; Ledward, D.A.; Bardsley, R.G.; Poulter, R.G. Species dependence of fish myosin stability to heat and frozen storage. International Journal of Food Science and Technology (1994) 29 (3) 287-301. [DOI: 10.1111/j.1365-2621.1994.tb02070.x]
Species dependence of fish myosin stability to heat and frozen storage