Inhibiting effect of polymerization and degradation of myosin heavy chain during preheating at 30°C and 50°C on the gel-forming ability of walleye pollack surimi

ABSTRACT: To confirm the contribution of polymerization and degradation of myosin heavy chain (MHC) during preheating to the gel-forming ability of fish meat paste, walleye pollack surimi paste was preheated at 30°C and 50°C prior to heating at 80°C in the presence of various inhibitors. At 30°C, ethyleneglycol bis(2-aminoethyl ether) -N,N,N ', N '-tetraacetic acid (EGTA) and ethylenediaminetetraacitic acid (EDTA) inhibited gel formation as well as the polymerization of MHC, whereas dithiothreitol (DTT) and leupeptin promoted gel formation, which was accompanied by the enhancement of MHC polymerization and decreased MHC degradation, respectively. At 50°C, leupeptin inhibited MHC degradation and improved gel strength, whereas EGTA, EDTA and DTT had no effect on MHC polymerization and degradation and did not affect gel formation. The results demonstrate that the gel strength of cooked gel (80°C) is not affected by preheating at 30°C and 50°C and does not inhibit polymerization and degradation. Results suggest that the gel strength of cooked gel is dependent on the polymerization and degradation of MHC during preheating.     

Effect of pH-shifting on the gel forming characteristics of salt-ground meat from walleye pollack

ABSTRACT:   In order to elucidate the mechanism of the changes in gel forming characteristics of fish meat by pH-lowering, the gelation-temperature curve and the gelation-moisture content curve were examined using the acidified walleye pollack surimi or neutralized one after acidification. In the gelation-temperature curve, the gel strength was highest at 30°C and lowest at approximately 50–60°C, irrespective of pH shifting. The gel strength at 30°C and 80°C decreased with the decrease in pH value. The neutralization of acidified surimi improved the gel strength, but it was considerably lower than the original gel strength. The gel strength at 50–60°C was not affected by pH lowering. The gel strength at 80°C could not be revived to the original by pH readjustment, either in the presence or in the absence of EDTA. These results suggest that irreversible changes of meat protein take place under the low pH, and the oxidation ability of sulfhydryl (SH) groups of protein molecule is not affected by pH-shifting.     

Changes in physical properties of heat-induced gel on addition of gluconate associated with suppression of myosin denaturation in walleye pollack salt-ground <Emphasis Type="Italic">surimi</Emphasis> during preheating

Changes in physical properties of two-step heated gels on addition of gluconate were investigated in terms of relationships between breaking strength and gel stiffness. Regression lines between the breaking strength and the gel stiffness were extended to the x-axis (gel stiffness), and the intercept was defined as S_BSO. The S_BSO of the two-step heated gels increased with gluconate contents in salt-ground surimis, suggesting that the harder but less elastic gels formed on addition of gluconate were dose-dependent. Conversely, the denaturation rate constants of myosin in salt-ground surimis during preheating estimated by means of Ca-ATPase inactivation, loss of salt solubility, and decrease of denaturant solubility were considerably reduced by gluconate. Thus, the progress of myosin denaturation was strongly suppressed. Increments of S_BSO (δS_BSO) of the two-step heated gels on addition of gluconate were inversely correlated with the denaturation rate constants of myosin in salt-ground surimis for every index. Thus, the changes in physical parameters of two-step heated gel caused by gluconate may be associated with the sluggish progress of myosin denaturation in salt-ground surimi during preheating.