This work was sponsored, in part, by the University of North Carolina Sea Grant College Program by NA-90-AA-D-SG062, Project No. R/SST-15 from the National Oceanic and Atmospheric Administration, NOAA. The U.S. Government is authorized to produce and dis-tribute reprints for governmental purposes notwithstanding any copyright that may appear theron. Paper No. FSR-96-19 of the Journal Series of the Department of Food Science, North Carolina State University, Raleigh, NC 27695-7624. Use of trade names in this publication does not imply endorsement by North Carolina Agricultural Research Service, nor criticism of similar ones not mentioned.
Covalent Bonding in Pressure-Induced Fish Protein Gels
Article first published online: 20 JUL 2006
Journal of Food Science
Volume 62, Issue 4, pages 713–733, July 1997
How to Cite
GILLELAND, G.M., LANIER, T.C. and HAMANN, D.D. (1997), Covalent Bonding in Pressure-Induced Fish Protein Gels. Journal of Food Science, 62: 713–733. doi: 10.1111/j.1365-2621.1997.tb15442.x
We gratefully acknowledge support for G.M. Gilleland from the National Fisheries Institute, Arlington VA.
- Issue published online: 20 JUL 2006
- Article first published online: 20 JUL 2006
- Ms received 8/7/96; revised 1/07/97; accepted 1/25/97.
Surimi pastes were gelled by pressure, incubation at 25°C, cooking, or their combination. Differential scanning calorimetry and solubility measurements indicated that myosin denaturation and disulfide bond formation occurred during pressure-induced gelation. Time of pressure treatment had little effect on gel fracture properties. Nondisulfide covalent polymerization of myosin did not appreciably occur during pressure-induced gelation, but was prevalent in gels incubated at 25°C, even when such incubation followed pressure treatment. That combination treatment increased the stress value of cooked gels more than six times, indicating synergy of pressure with the endogenous enzyme transglutaminase, thought to be responsible for gelation of surimi pastes at 25°C.