Effect of Divalent Cations on Heat-induced Gelation of Chicken Gizzrd Myosin

Abstract

Smooth muscle myosin was prepared from chicken gizzards to study its heat-induced gelation. The gel strength of chicken gizzard myosin gel increased by the addition of FeCl₂. Scanning electron microscopic observations of the gels showed that the gels with FeCl₂ had a thinner and smoother network in their microstructure. Fluorescence intensity of gizzard myosin before heating increased in 0.4-0.5M and decreased in 0.1-0.2M KCl solutions by the addition of FeCl₂. Cross-linking experiments using. EDC indicated that myosin rods were cross-linked at 60-70°C and FeCl₂ accelerated the cross-linking of rods. These results suggested that FeCl₂ enhanced the gel strength of gizzard myosin due to the structural change of tail portion in high KCl solution, while in low KCl solution the addition of FeCl₂ accelerated head to head aggregation.