Spectroscopy‐based analysis of the effect of Maillard reaction products on oxidative stability of carp myoglobin

Abstract As a pro‐oxidant, myoglobin (Mb) can induce lipid oxidation in meat. In this study, Fourier‐transform infrared spectroscopy (FTIR), circular dichroism (CD), fluorescence spectroscopy, UV–vis spectrophotometry, and fluorescence microscopy were used to evaluate the impact of Maillard reaction products (MRPs) formed from glucose and lysine on the oxidative stability of carp Mb. MRPs were found to inhibit the auto‐oxidation of Mb, reducing MetMb production by 8.45%. The static quenching of fluorescence indicated that MRPs interacted with Mb through hydrogen bonding and van der Waals forces, thereby enhancing the α‐helical content by 11.57% and reducing the random coil content by 2.72%. The enhanced stability of this advanced structure helps to minimize the exposure of amino acid in the side chain and prevent the formation of MetMb. Fluorescence microscopy showed that MRPs reduce porphyrin ring degradation, consequently decreasing heme iron release. It is evident that MRPs play a crucial role in maintaining Mb structure stability and inhibiting its oxidation.