INTERACTION BETWEEN TRIOLEIN AND NATURAL HAKE ACTOMYOSIN DURING FROZEN STORAGE AT -18C

The interaction of hake muscle actomyosin with triolein in 0.6 M KCl, pH 7, during frozen storage has been investigated. ATPase activity, protein solubility and relative viscosity measurements were performed. No effect of triolein on these functional properties was observed during the storage period studied. Incorporation of l-14C triolein to the protein was found over the storage period, indicating that despite the lack of effect on functionality, lipid-protein interaction occurs. No differences were found in the electrophoretic patterns between control and neutral lipid added samples.