Modulating the aggregation pattern of interface myofibrillar protein in emulsion gel to enhance Na+ inhomogeneous distribution during microwave heating: The effects of hydrophobic interactions and disulfide bonding

Nowadays, modulating microstructure of matrix to achieve salt reduction on diverse food have attract widespread attention. Our previous study found that the spatial site resistance effect of oil droplets attenuated the inhomogeneous distribution of Na + in microwave processing, which was detrimental to the enhancement of saltiness perception. This study promoted the extent of inhomogeneous Na + distribution by 39.79 % through regulating interfacial protein aggregation pattern. The protein aggregation pattern is mainly accomplished through the regulation of hydrophobic interaction and disulfide bonding of interfacial proteins by octenyl succinic anhydride and reduced glutathione, respectively. The results showed that droplet and interfacial tension of myofibrillar protein (MP) increased significantly, while the fluorescence intensity of hydrophobic groups decreased with the increase of hydrophobic interactions regulation. However, regulation of disulfide bonds conducive to the exposure of more hydrophobic amino acids and rapid adsorption of MPs at the oil-water interface to form more stable droplets. The unstable droplets regulated by hydrophobic interactions inhibited the inhomogeneous distribution of Na + in gel matrix, whereas the regulation of disulfide bonds promoted the inhomogeneous distribution of Na + . This work is expected to give some insights into the development of emulsified salt-reduced meat products by microwave processing.