Abstract
ABSTRACTGelation behavior and potential cross‐linking of Pacific whiting (Merluccius productus) surimi were affected by setting temperatures and an enzyme inhibitor. Gels of Pacific whiting surimi with salt and beef plasma protein were compared with those containing guanidine hydrochloride, sodium dodecyl sulfate, and β‐mercaptoethanol. The strongest gels were formed at 25°C setting followed by 90°C heating. Hydrogen and hydrophobic bonds appeared to strongly influence gel formation, while the influence of disulfide bonds was moderate. Viscosity scanning during setting at different temperatures was also useful to estimate effects of enzymes and inhibitors.
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