NONDISULFIDE COVALENT CROSS-LINKING OF MYOSIN HEAVY CHAIN IN “SETTING” OF ALASKA POLLOCK AND ATLANTIC CROAKER SURIMI1

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  • 1

    This work was sponsored, in part, by Office of Sea Grant, NOAA, U.S. Dept. of Commerce under Grant No. NA-86-AA-D-SG046, Project No. R/SST-15 and the State of North Carolina through The University of North Carolina. The U.S. Government is authorized to produce and distribute reprints for governmental purposes notwithstanding any copyright that may appear thereon. Paper No. FS92–17 of the Journal Series of the Department of Food Science, North Carolina State University, Raleigh, NC 27695–7643. Use of trade names in this publication does not imply endorsement by North Carolina Agricultural Research Service, nor criticism of similar ones not mentioned.

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Abstract

ABSTRACTMyosin heavy chain (MHC) content of cooked gels of pollock and croaker surimi decreased during preincubation (“setting”) at temperatures ranging from 4–50C. 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 25C for pollock surimi and 40C for croaker surimi. Subsequent cooking of these set gels at 90C 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 ε-amino-(γ-glutamyl) lysine I type, mediated by a transglutaminase enzyme.

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