Abstract
In this study, the effect of L-arginine (L-Arg) on the oxidative aggregation of myofibrillar proteins (MPs) in Antarctic krill was evaluated. The results showed that the oxidized aggregation of MPs was significantly inhibited after the addition of 20 mM L-Arg compared to the oxidized group, the solubility of MPs significantly increased by 25.74 %, the turbidity reduced from 0.56 to 0.18. These effects were primarily attributed to the addition of L-Arg, which prevented the unfolding of the spatial structure of MPs after oxidation, inhibited the formation of disulfide bonds and dityrosine, and improved the stability of MPs structure. Analysis of carbonyl content and hydroxyl radical (•OH) inhibitory capacity showed that carbonyl formation and hydroxyl radicals were effectively reduced by the pH and guanidinium group of L-Arg. The pH of L-Arg exhibited a significantly higher effect than the guanidinium group in inhibiting the oxidative aggregation of MPs.
Published Version
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