Abstract
The salted fish meat paste prepared from frozen surimi of Alaska pollack with 3% NaCl was submitted to setting (suwari) at 20°C. Fish gels formed during the setting for up to 6h were completely dissolved in SDS solution containing urea and mercaptoethanol. The SDS-soluble protein was applied to analyze the protein subunits composition by SDS-gel filtration technique using Bio-Gel A 50m column, followed by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). It was shown that myosin heavy chain (denoted as HC) decreased as the setting proceeded, and a group of oligomers of myosin heavy chain (correspond to (HC)n, n=2-6) was formed at an early stage of the setting. At a later stage of the setting, polymers of myosin heavy chain (correspond to (HC) n, n>10) were found by SDS-PAGE using 1.8% acrylamide gels. The SDS-gel filtration patterns of the other myofibrillar proteins were scarcely changed.
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