1. Non-covalent interactions between large yellow croaker (Pseudosciaena crocea) roe protein isolates and curcumin: Implications for enhanced curcumin delivery.
- Author
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Du, Yi-Nan, Jia, Jiao, Yan, Jia-Nan, Xu, Shi-Qi, Wang, Yu-Qiao, and Wu, Hai-Tao
- Subjects
LARIMICHTHYS ,VAN der Waals forces ,CURCUMIN ,FOURIER transform infrared spectroscopy ,HEAT treatment ,FLUORESCENCE spectroscopy - Abstract
This study investigated the influence of heat treatment on the interaction of large yellow croaker (Pseudosciaena crocea) roe protein isolate (pcRPI) with curcumin (Cur), and heated pcRPI (HpcRPI)-Cur and pcRPI-Cur complexes were also prepared. Fourier transform infrared spectroscopy, fluorescence spectroscopy, and surface hydrophobicity analysis indicated that pcRPI and HpcRPI bind to Cur mainly by hydrogen bonds, van der Waals forces, and hydrophobic interactions, and compared with pcRPI, HpcRPI showed better binding effects with Cur. Molecular docking analysis also evaluated the binding site and the forces between vitellogenin, vitellogenin B and C in pcRPI and Cur. Furthermore, HpcRPI-Cur could form gels induced by glucono-δ-lactone (GDL), while pcRPI-Cur-GDL exhibited a fluid state. The HpcRPI-Cur-GDL gels showed great protective effects on Cur in the resistant gastrointestinal environment. These results indicated that heat treatment will improve the application of pcRPI as a functional material in the food field. [Display omitted] • The pcRPI can bind to curcumin via noncovalent interactions and form complexes. • The heat treatment promoted the noncovalent interactions of pcRPI with curcumin. • The heat treatment enhanced the formation of pcRPI cold-set gels. • The heated-pcRPI gel significantly improved the delivery effect of curcumin. [ABSTRACT FROM AUTHOR]
- Published
- 2024
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