Effect of hydroxyl-radical on the biochemical properties and structure of myofibrillar protein from Alaska pollock (Theragra chalcogramma)

The aim of the study was to investigate the effect of hydroxyl-radical on myofibrillar protein properties. Myofibrillar protein isolated from Alaska pollock muscles were incubated with oxidant agents containing different H2O2 concentrations of 0, 0.1, 1, 5, 10 and 20 mmoL/L for 1, 3 and 5 h respectively. Incubation at higher concentrations of H2O2 induced a significant decrease of protein total sulfhydryl group and an increase in protein carbonyl content in the myofibrillar fraction. Moderate H2O2 concentration (1 mmoL/L) enhanced water-holding capacity and textural properties of a gel, while lower (0.1 mmoL/L) and higher (5, 10 & 20 mmoL/L) H2O2 concentrations significantly reduced the water-holding capacity. At higher H2O2 concentration, oxidized gel revealed some resistance toward the change in gel properties. Additionally, the results from SDS-PAGE and microstructure confirmed the structural changes through aggregation and denaturation of myofibrillar components that induced changes on gelation of myofibrillar protein. The whiteness of the myofibrillar protein gel decreased significantly (p < 0.05) with increasing the concentration of H2O2. Oxidation of myofibrillar protein revealed the slight improvement of textural properties of the heat set gel at a moderate concentration of oxidant agent.