Gelation of proteins from washed muscle of threadfin bream (Nemipterus japonicus) under mild acidic conditions

Gelation of proteins of washed mince of threadfin bream was induced by the organic acids: acetic, lactic, tartaric, and citric. Washing of mince was essential for gelation. The strength of acetic acid-induced gel was affected by setting conditions and heat treatment. Gelation was associated with degradation of myosin heavy chain and appearance of a new protein band of about 160 kDa. Solubility studies of the gel in various solvents suggested structural changes. Gelation was also associated with oxidation of sulfhydryl groups. Salts negatively influenced gelation.