FOOD SCIENCE ›› 0, Vol. ›› Issue (): 0-0.

• Basic Research •     Next Articles

Effects of Hydroxyl Radical Oxidation on Myofibrillar Proteins from Coregonus peled

LEI Yongdong 2, 2, 2,   

  • Received:2018-09-10 Revised:2019-06-26 Online:2019-08-15 Published:2019-08-26

Abstract: Abstract: The effect of the hydroxyl radical (?OH) oxidation on myofibrillar protein of the dorsal muscle from Coregonus peled were investigated by in vitro simulant oxidation experiments. The different oxidation levels of the fillets were generated with four distinct oxidation concentration of the hydroxyl radical. The optimal oxidation concentration was obtained by determining the carbonyl content of the fillets with 5 mmol/L H2O2 and 0.4 mmol/L FeCl3 for 60 min. Then the oxidized fillets were stored at 4 ℃ for 0, 1, 7, and 14 d, and the unoxidized were taken as a control at the same time. The indexes including degradation of myosin heavy chain (MHC), actin, desmin and troponin-T of myofibrillar protein were analyzed. The degradation of MHC was observed via SDS-PAGE, and the actin, desmin, and troponin-T via Western Blotting. The results showed that compared with the native MHC, degradation of oxidized MHC was enhanced. The results revealed that protein oxidation accelerated the degradation of MHC. The degradation and changes of actin demonstrated that no significant changes were observed between oxidized group and non-oxidized group at the same storage time, which revealed that it was natural degradation of actin that constituted a dominant position during storage. According to western blotting analysis of degradation of desmin subjected to hydroxyl radical oxidation, the results of protein stability of non-oxidized desmin showed positive on degradation, indicating that the stability of oxidized desmin were strengthened by hydroxyl radical to a certain extent. The results about degradation trend of troponin-T subjected to hydroxyl radical oxidation were consistent with the degradation of desmin. These results show that the hydroxyl radical oxidation system can change the degradation rate of myofibrillar proteins in Coregonus peled, leading to increase the degradation for thick filament of myofibrillar protein, less influence on the degradation in thin filament, decrease the degradation both of cytoskeletal protein and junction protein.

Key words: Coregonus peled, hydroxyl radical (?OH), oxidation, myofibrillar protein, degradation

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