In order to clarify the participation of hydrophobic amino acid residues on the protein surface in the setting phenomenon(low temperature gelation of fish flesh sol), the thermal behaviors of muscle proteins arylated with arylsulfonates and arylsulfonyl chlorides were investigated. The arylated hen and pig myosins and actomyosins gelled readily at 40°C. An elastic modulus of the resulting gel increased with an increase in the binding amount of the arylating reagent, but this increase was suppressed by the addition of sucrose. Gelation was induced even at 4°C.
The viscosity of hen and pig actomyosin arylated with β-naphthoquinone-4, -7disulfonate increased rapidly on heating to 40°C, while that of the unmodified actomyosin did not.

This article cannot obtain the latest cited-by information.