Interaction Modes of Curcumin with Cynanchum auriculatum Royle ex Wigh Protein and Soy Protein Isolate

Abstract

Abstract: In this work, the interaction between curcumin (Cur) and Cynanchum auriculatum Royle ex Wigh protein (CAP) or soy protein isolate (SPI) was characterized by a combination of steady-state fluorescence, circular dichroism (CD), differential scanning calorimetry (DSC), and dynamic light scattering (DLS) analyses, and the protective effects of two proteins on the chemical stability of Cur were further investigated. Results showed that Cur quenched the intrinsic fluorescence of proteins through a static manner. The complexation of Cur with CAP/SPI was a spontaneous and Gibbs free energy-decreasing reaction, which was mainly driven by entropy loss (hydrophobic interaction). FT-IR analysis suggested that hydrogen bonding might also involve in the formation of Cur-protein complexes. Cur binding resulted in the reduction in the α-helix fraction in CAP with a paralleled increase in the content of other three secondary structures, as well as reduced the thermal stability of CAP. Compared with SPI, Cur-SPI complex contained less α-helix and β-sheet secondary structures and presented a higher thermal stability. The complexation of Cur with CAP and SPI affords nanoparticles with a diameter of 159.98 and 244.34 nm, respectively. The thermal stability of Cur under 40 °C and 90 °C improved remarkably after bound with CAP or SPI, and the protective effect of SPI appeared to be more pronounced.

Key words: Radix Polygoni Multiflori protein, soybean protein isolate, curcumin, interaction, thermal stability

CLC Number:

TS201.2

References

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