Freezing and frozen storage of actomyosin from different species

A comparative study was made of the influence of freezing (–24°C) and frozen storage (–12°C) on the functional properties (viscosity, solubility) and physico-chemical characteristics (aliphatic and aromatic hydrophobicity, ATPase activity) of actomyosin (AM) from myosystems (chicken and hake) of differing freezing and frozen stability. The difference in functional behaviour between chicken and hake AM as a consequence of freezing and frozen storage suggests that, for hake AM, denaturation and aggregation occur essentially through direct aggregation of AM molecules to produce AM aggregates, whereas in chicken proteins, AM first dissociates into myosin and actin to produce myosin and myosin-actin aggregates.