Insight into the Interaction of Malondialdehyde with Rabbit Meat Myofibrillar Protein: Fluorescence Quenching and Protein Oxidation

This research explored the effects of oxidative modification caused by different malondialdehyde (MDA) concentrations on rabbit meat myofibrillar protein (MP) structural characteristics and the interactions between MDA and MP. The fluorescence intensity of MDA-MP adducts, and surface hydrophobicity increased, whereas the intrinsic fluorescence intensity and free-amine content of MPs decreased as MDA concentration and incubation time increased. The carbonyl content was 2.06 nmol/mg for native MPs, while the carbonyl contents increased to 5.17, 5.57, 7.01, 11.37, 13.78, and 23.24 nmol/mg for MP treated with 0.25 to 8 mM MDA, respectively. When the MP was treated with 0.25 mM MDA, the sulfhydryl content and the a-helix content decreased to 43.78 nmol/mg and 38.46%, while when MDA concentration increased to 8 mM, the contents for sulfhydryl and a-helix decreased to 25.70 nmol/mg and 15.32%. Furthermore, the denaturation temperature and ?H decreased with the increase in MDA concentration, and the peaks disappeared when the MDA concentration reached 8 mM. Those results indicate MDA modification resulted in structural destruction, thermal stability reduction, and protein aggregation. Besides, the first-order kinetics and Stern-Volmer equation fitting results imply that the quenching mechanism of MP by MDA may be mainly driven by dynamic quenching.

Automated summary

This study investigated the effects of oxidative modification caused by different concentrations of malondialdehyde (MDA) on the structural characteristics of rabbit meat myofibrillar protein (MP) and the interactions between MDA and MP. The results showed that as the MDA concentration and incubation time increased, the fluorescence intensity and surface hydrophobicity of MDA-MP adducts increased, while the intrinsic fluorescence intensity and free-amine content of MPs decreased. The MDA modification resulted in structural destruction, thermal stability reduction, and protein aggregation.