Contribution of SS Bonds to the Elasticity of Actomyosin Gel in which Coexisting Transglutaminase was inactivated

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  • Contribution of SS Bonds to the Elastic

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The contribution of SS bonds to the elasticity of suwari gel from various actomyosins was investigated, in which the coexisting transglutaminase was inactivated. The actomyosins, whose SH groups were blocked (SH-blocked AM) and unblocked (SH-unblocked AM), were prepared, respectively, by shaking the starting actomyosins with and without N-ethylmaleimide in 8M urea. After removal of urea by dialysis, they were measured for transglutaminase activity, total SH content, and suwari gel forming ability. The transglutaminase activity of both the actomyosins became zero by the above treatment with urea. The suwari gel prepared by setting SH-unblocked AM paste at 40°C for 1 h was considerably higher in the breaking force than the gel from the paste of the SH-blocked one. By setting the AM paste, total SH content was somewhat decreased in the former, but scarcely changed in the latter.

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