Abstract
In this study, the influence of extracted pangasius myosin on the thermal stability of lycopene and the mechanism of their interaction were examined. The addition of pangasius myosin positively affected the thermal stability of lycopene. After adding myosin, under heating conditions, the L* value of lycopene increased by 6.2–10.04%, a* value increased by 20–27%, and ΔE decreased by 42–51%. Lycopene inhibited the fluorescence of ovalbumin by static burst. Binding and thermodynamic parameters demonstrated that lycopene bound spontaneously to myosin through hydrophobic interaction with a complex stoichiometry ratio of 1:1. Circular dichroism and Fourier infrared transform spectroscopy were used to examine the secondary structure changes that occurred in myosin after it bound to lycopene. Particle size and electron microscopy analysis showed that the addition of low concentrations of lycopene resulted in smaller particle size and improve dispersion stability; however, high concentrations of lycopene promoted myosin aggregation. This study provides a theoretical foundation for improving the thermal stability of lycopene in minced fish products.
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