Nondisulfide covalent cross-linking of myosin heavy chain in "setting" of Alaska pollock and Atlantic croaker surimi
1992
Kamath, G.G. | Lanier, T.C. | Foegeding, E.A. | Hamann, D.D.
Myosin heavy chain (MHC) content of cooked gels of pollock and croaker surimi decreased during preincubation ("setting") at temperatures ranging from 4-50 degrees C. Decreases in MHC content were attributed to either nondisulfide covalent cross-linking or proteolysis. Depending upon which process dominated at a given temperature, formation of stronger or weaker gels occurred, respectively. Maximum production of cross-linked polymers occurred at the optimum setting temperatures, i.e., at 25 degrees C for pollock surimi and 40 degrees C for croaker surimi. Subsequent cooking of these set gels at 90 degrees C decreased the amount of cross-linked polymers formed at the optimum setting temperature. Addition of free lysine-HCl inhibited formation of cross-linked polymers of MHC during setting and the increase in cooked gel strength for both species. This supports published evidence that cross-linking of MHC during setting may be of the epsilon-amino-(gamma-glutamyl) lysine type, mediated by a transglutaminase enzyme.
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