Abstract
The effect of degrees of dehydration on protein denaturation during vacuum freezing and subsequent freeze-drying of carp myofibrils with 5% sucrose + 0.2% polyphosphates or without additives has been examined. At suitable intervals of freeze-drying, the aliquots of samples were taken out and examined as to protein denaturation, using as indexes the solubility in 0.6M KCI, the relative viscosity and the ATPase activity of the 0.6M KCI extractable protein, and the total ATPase activity. The myofibrils with sucrose and polyphosphates could be freeze-dried thoroughly without causing protein denaturation; but freeze-drying the myofibrils without additives caused the protein denaturation. In the latter case, the protein deaturation was not suddenly caused at a critical moisture range, but was slowly caused during freeze-drying.
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