Enzyme-catalyzed Cross-linking and Degradation of Myosin Heavy Chain in Walleye Pollack Surimi Paste during Setting.

Walleye pollack surimi paste was incubated (set) at 25, 35, 45, and 55•Ž in the presence of either transglutaminase (TGase) inhibitor or protease inhibitor. In the absence of inhibitors, cross-linking of myosin heavy chains and formation of 150 kDa component occurred at the same time during the incuba tion at 25•Ž. Inhibition of endogenous TGase resulted in complete suppression of myosin cross-linking, while it did not suppress the formation of 150 kDa component. The cross-linking was also depressed above 45 •Ž due to the inactivation of TGase. On the other hand, the addition of E-64, a cysteine protease inhibi tor, suppressed completely and partially the formation of 150 kDa component at 25 and 55?C, respec tively. Together with these results, the 150 kDa component might be a proteolytic fragment of myofibril lar proteins. possibly myosin. The proteolysis as well as the cross-linking of myosin during the setting affected the textural proper ties of final cooked gels.

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