AI Article Synopsis
- The study investigated how ultrasound treatment affects myofibrillar proteins (MPs) in low salt solutions, focusing on their solubility, hydrophobicity, and structural changes.
- Results showed that ultrasonic treatment increased solubility, sulfhydryl and carbonyl content, and α-helix structure while decreasing turbidity, β-sheet content, and improving fluorescence intensity.
- Emulsions stabilized with MPs treated at 800 W displayed smaller particle sizes, better uniformity, and greater stability, indicating improved emulsifying properties.
Article Abstract
The physiochemical properties, structure characteristics, oxidation, and emulsifying properties of myofibrillar proteins (MPs) in low salt solution after treated by the ultrasound were investigated. The solubility, mean diameters, sulfhydryl content, and carbonyl contents of MPs after ultrasonic treatment increased, while the turbidity decreased. The surface hydrophobicity of MPs with 200 W-600 W treatment increased, but decreased at 800 W treatment. The circular dichroism analysis revealed that α-helix content increased, while β-sheet and random coil content decreased after ultrasonic treatment. Fluorescence spectroscopy indicated the fluorescence intensities of MPs were increased after ultrasonic treatment. SDS-PAGE results showed more protein polymers due to myosin heavy chain (MHC) aggregation via disulfide bonds. Based on LC-MS/MS result, the myosin heavy chain was susceptible to oxidation, with monooxidation being the main oxidative modification. Finally, the emulsions stabilized by ultrasonically treated MPs, especially those treated at 800 W, exhibited decreased particle size, improved uniformity, and enhanced stability.
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| http://dx.doi.org/10.1016/j.foodchem.2023.137564 | DOI Listing |
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