Thermally induced gelation of squid (Illex argentinus) actomyosin. Influence of sexual maturation stage.

The biochemical properties and the characteristics of heat-induced gelation of actomyosin from mature and immature squid were investigated. Both Mg(2+)-ATPase activity and reduced viscosity values of actomyosin showed no significant differences between mature and immature squids. A lower content of myosin heavy chain and a higher content of a 160 kDa component were observed in the SDS-PAGE 10% pattern of actomyosin from immature specimens. Gelation of both actomyosins at 10 mg mL(-)(1) protein concentration was optimal at 80 degrees C and pH 6.0. The highest rigidity was reached at 0.25 M KCl with actomyosin from both mature and immature squids. Irrespective of the heating temperature, ionic strength, and pH condition, the rigidity of mature squid actomyosin gel was greater than that of immature squid. Scanning electron micrographs of gels obtained with actomyosin from mature squids showed a better tridimensional structure than those of immature squids.