Abstract
Oxidation is a leading cause for quality deterioration during processing and storage of food. The objective of the present study was to examine the sensitivity of common carp (Cyprinus carpio) myofibrillar protein (MP) to oxidising radicals produced by a hydroxyl radical-generating system. Both structural and functional changes of common carp MP were evaluated. With increasing H2O2 concentrations and oxidation time, the protein carbonyl content, surface hydrophobicity and turbidity of MP increased (P<0.05), while total sulfhydryl groups decreased (P<0.05). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis revealed protein polymerisation in oxidised MP. The oxidative process destroyed (P<0.05) the texture (springiness and hardness) of MP gels and decreased their water-binding capacity and whiteness. The thermal gelation profile analysis indicated that oxidation led to a great reduction in the elasticity of samples. Taken together, proteins are susceptible to free radical attack, and oxidative stress had a detrimental effect on protein structure and the general functionality of MP.
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