Biochemical changes of Coregonus peled myofibrillar proteins isolates as affected by HRGS oxidation system

The objective of the study was to research the effect of protein oxidation on the biochemical properties of Coregonus peled muscle proteins. Myofibrillar proteins (MP) prepared from C. peled back muscle was oxidized using a hydroxyl radical-generating system (HRGS: 0.1 mM FeCl3, 0.1 mM ascorbic acid (Asc) and 1-20 mM H2O2). In the HRGS oxidizing system, the carbonyls, dityrosine content, and the surface hydrophobicity of C. peled MP (p < 0.05) increased with the increasing of H2O2 concentration and oxidation time, while the total sulfhydryl, free amino groups and the Ca-ATPase activity decreased (p 0.05). The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) pattern reflected the formation of protein polymers and protein degradation. The results indicate that protein oxidation and the increasing levels of biochemical alterations of C. peled MP have influence on the quality of C. peled muscle protein.