Mechanism for the Gelation of Unheated Surimi by Vinegar Curing

The mechanism for the formation of vinegar-cured, unheated surimi-gel, so called shime-kamaboko in Japan, from Alaska pollack frozen surimi was investigated. In the SDS-PAGE pattern, a band due to the myosin heavy chain disappeared after dialyzing a sol of the salted fish flesh, shio-surimi, against Walpole buffer (pH 0.5–6.5). The breaking force and deformation of shime-kamaboko were maximized at around pH 4.0, but remained constant in the pH range of 1.0–4.2 if the muscle proteins of the surimi were succinylated. These values were increased by adding salt, but decreased by adding urea or guanidine-HCl. The fluorescence intensity of shio-surimi measured in the presence of ANS-Na was scarcely affected by reducing the pH value.