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Myosin B, myosin and actin were polymerized and gelled by Ca2+-independent transglutaminase (B.T.G.) derived from a microorganism (Streptoverticillium). The concentration of B.T.G. required for gelation of myosin B was lower than that for myosin and actin. On SDS-PAGE of myosin B treated with B.T.G., the monomeric myosin heavy chain decreased markedly with increasing amount of B.T.G. and a polymer fraction increased. Analysis of actin by SDS-PAGE indicated that actin was also polymerized. The small amount of B.T.G. increased the turbidity of myosin B induced by heating of linearly increasing rate of 2°C/min, suggesting that myosin B suspension with B.T.G. formed a finer network structure of heat-induced gel than that of myosin B alone. When the myosin B solution with B.T.G. was heated and then the heat induced gel centrifuged; tropomyosin and troponin-T were not freed from the sediment. These results suggest that the regulatory proteins play some role in the heat-induced gelation of this system. (Received Dec. 6, 1989)

nippon shokuhin kōgyō gakkaishi

Studies on application of transglutaminase to meat and meat products Part II. The effect of microbial transglutaminase on gelation of myosin B, myosin and actin.