Denaturation of Cod Myosin during Freezing after Modification with Formaldehyde

Formaldehyde at concentrations occurring in frozen fish increased the extent of denaturation as measured by loss in solubility, decrease in ATPase activity and increase in surface hydrophobicity, of partially purified cod myosin stored at ‐25°C or ‐80°C. Most denaturation occurred during the freezing/thawing process. Formaldehyde caused some crosslinking of myosin, but crosslinking and insolubilization appeared to be relatively independent. The presence of diamines led to some increase in crosslinking but had little effect on protein solubility.