CAUSES OF INFERIOR GEL-FARMING ABILITY OF SALMON SURIMI PASTE

Salmon surimi has not been preferred commercially due to its poor gel formability resulting from the absence of setting response. The causes were investigated. It was found that the activity of transglutaminase extracted from the salmon surimi was too low to produce cross-inked myosin polymers and to set gels. In addition, the contents of myosin and Ca2+ were also lower than those in walleye pollack surimi. The inhibition of protease activity did not enhance the polymerization of myosin at all. Salmon actomyosin could be cross-linked in great extent by carp transglutaminase and resulted in the gelation. Although the enzyme-induced set gel was formed from salmon actomyosin paste, carp transglutaminase supplied to salmon surimi paste did not induce the myosin cross-linking nor did the gelation. This result suggests the presence of factors inhibiting the enzyme activity in the salmon surimi paste.