Succinylated whey protein isolate-chitosan core-shell composite particles as a novel carrier: Self-assembly mechanism and stability studies.

Single protein [whey protein isolate (WPI) or succinylated whey protein isolate (SWPI)] and composite particles of proteins with chitosan (CS) were tested for their ability to encapsulate and protect curcumin (CUR). Combining protein and CS resulted in changes in zeta-potential and surface hydrophobicity, particularly in the SWPI-H (high degree of succinylation, 90 %) and CS composite particle (H-CS). Furthermore, the secondary and tertiary structures were dramatically altered using Fourier transform infrared (FTIR), circular dichroism (CD), and X-ray diffraction (XRD). Scanning electron microscopy (SEM) and atomic force microscope (AFM) analyses revealed that H-CS exhibited a soft core-rigid shell morphology due to electrostatic interactions, hydrophobic interactions, and H-bond interactions. Fluorescence quenching results demonstrated that H-CS had a higher binding constant (K, 1.69 ×10 M) and encapsulation effectiveness (EE, 88.3 %) of CUR. Because of increased binding sites and steric hindrance, CUR was stabilized more effectively in H-CS in photostability and thermostability tests,. These results show that SWPI-CS composite particles can be utilized to build a protection system for water-insoluble nutritional supplements.