COVALENT BONDING IN PRESSURE-INDUCED FISH-PROTEIN GELS

Surimi pastes were gelled by pressure, incubation at 25 degrees C, coo king, or their combination. Differential scanning calorimetry and solu bility measurements indicated that myosin denaturation and disulfide b ond formation occurred during pressure-induced gelation. Time of press ure treatment had little effect on gel fracture properties. Nondisulfi de covalent polymerization of myosin did not appreciably occur during pressure-induced gelation, but was prevalent in gels incubated at 25 d egrees C, even when such incubation followed pressure treatment. That combination treatment increased the stress value of cooked gels more t han six times, indicating synergy of pressure with the endogenous enzy me transglutaminase, thought to be responsible for gelation of surimi pastes at 25 degrees C.