Physico-chemical and functional properties of myofibrillar proteins from different species of molluscs

The physico-chemical and functional properties of myofibrillar proteins from scallop (Zygochlamys patagonica), bivalve molluscs (Aulacomya ater ater), and squid (Illex argentinus) were investigated. Actomyosins were studied by SDS-PAGE, Mg2+-(Ca2+-dependent) ATPase activity, reduced viscosity, and surface hydrophobicity determinations. The emulsion capacity (EC) of both soluble protein extracts and actomyosins was also determined. Densitometric analysis of the SDS-PAGE 10% gels showed that in comparison with the actomyosin from striated muscle of scallop, the actomyosins of Aulacomya, squid, and smooth plus striated muscle of scallop have a significant higher relative percentage of paramyosin and a lower relative percentage of myosin. The reduced viscosity of actomyosin from both striated and smooth plus striated adductor muscle of scallop was significantly lower than that of squid and Aulacomya. No significant differences were observed in the enzymatic activity of the actomyosins analysed. Surface hydrophobicity and EC of actomyosin from striated muscle of Aulacomya were lower than those corresponding to actomyosin of the other species. The highest values of EC were observed in extracts of squid mantle. In addition, the EC of the extracts was significantly higher than the EC of their respective actomyosins.