Freezing of bovine muscle has a denaturating effect on myofibrillar proteins, Differ-ential Scanning Calorimetry (DSC) studies of fresh and frozen muscle at different freezing rates show a decrease on denaturation enthalpies; the lower the freezing rate the greater the loss. When measuring the specific areas (ratio between each partial area in cm', and the dry weight of the sample, in mg) of the DSC thermograms, it can be observed that the area ascribed to myosin decreases with freezing, while the area corresponding to actin is not affected. These results are in agreement with the ATPase activity decreases as a consequence of freezing observing higher losses at lower freezing rates. The denaturation observed could be a result of a partial unfolding of the myosin head being more pronounced at low freezing rate.
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Wagner et al. (1985) studied this question.
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