The frozen surimi of Alaska pollack was ground with 3% salt. The salted paste was submitted to setting, so-called “SUWARI”, at a fixed temperature of 20°or 30°C. During the setting, a portion of the paste was taken out to assess the gel strength before and after heat treatment at 90°C for 40min. Another portion was used to solubilize protein of the paste with a medium containing SDS, urea and 2-mercaptoethanol, and to analyze the soluble protein by SDS-poly- acrylamide gel electrophoresis.
The solubility of the paste slightly decreased with the prolonged setting, whereas the disappearance of myosin heavy chain in it became evident when still in high solubility.
The increase in gel strength of both gels with and without heat treatment was accompanied by the decrease in myosin heavy chain and a concomitant produce of cross-linked myosin heavy chain with large molecular sizes. It was thus proposed that the cross-likning of myosin in salted fish paste is responsible for textural changes of the gels.