Chemical, Physical, and Gel-forming Properties of Oxidized Myofibrils and Whey- and Soy-protein Isolates
Article first published online: 20 JUL 2006
Journal of Food Science
Volume 65, Issue 5, pages 811–818, August 2000
How to Cite
Liu, G., Xiong, Y.L. and Butterfield, D.A. (2000), Chemical, Physical, and Gel-forming Properties of Oxidized Myofibrils and Whey- and Soy-protein Isolates. Journal of Food Science, 65: 811–818. doi: 10.1111/j.1365-2621.2000.tb13592.x
- Issue published online: 20 JUL 2006
- Article first published online: 20 JUL 2006
- MS 19991012 received 10/5/99; revised 2/29/00; accepted 4/10/00.
- protein oxidation
Myofibrils, oxidized with FeCl3/H2O2/ascorbate, exhibited an increase in carbonyls and amines, SHSS conversion, peptide scission, myosin polymerization, and a decrease in thermal stability and gel-formation ability. Amino-acid side chains of whey-protein isolates (WPI) and soy-protein isolates (SPI) were also modified during oxidation, but the thermal stability of WPI or SPI was not significantly altered. Oxidation increased elasticity of SPI gel but not that of WPI gel. Similarly, oxidation promoted interactions of myofibrils with SPI but not with WPI, resulting in > 30% increases in elasticity of the myofibril/SPI composite gel over its nonoxidized control. Hence, in processed meats where oxidation occurs, the presence of soy proteins may enhance the functionality of myofibrillar proteins.