This study examined the thermal galation characteristics of myofibrillar protein (MP) and salt-ground horse mackerel surimi that had been mixed with hydroxypropylmethylcellulose (HPMC). Analysis, using thermal scanning rigidity monitor and differential scanning calorimetry, demonstrated that thermal gelation begins in the thermo-reversible HPMC gel used in this study at approximately 60°C. In the rescanning test, first scanning diagrams showed similar pattern, but second scanning diagrams were rather diverse between MP and MP/HPMC mixture. The addition of HPMC increased rigidity of salt-ground surimi and modified the thermal gelation during the heating process, suggesting that certain enhancing effect of gelation occurred when the mixture of MP and HPMC was heated. In the annealing test, the addition of HPMC lowered the breaking force, but increased the gel strength of surimi due to a substantial increase in deformation. Although the strong cross-linking between the two components might not occur during the gelling process, HPMC gel formed at high temperature occupies some space in thermal gel by interacting with proteins and resulted in a combinative gel with a higher rigidity and gel strength at higher temperature.
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