Production of self-assembling acylated ovalbumin nanogels as stable delivery vehicles for curcumin

Study on the emulsification and oxidative stability of ovalbumin-pectin-pumpkin seed oil emulsions using ovalbumin solution prepared by ultrasound

“…The fluorescence intensity of the PEC solution was close to zero, as PEC contains no fluorescence emitting groups. The maximum fluorescence emission of suOVA solutions was obtained at 335 nm, and was mainly due to tryptophan [34] . Moreover, the fluorescence intensity of the OVA-PEC solution was significantly lower than the OVA solution (red line) and the lowest fluorescence intensity of suOVA-PEC solutions was obtained at 300 W ( Fig.…”

Optimization of Encapsulation Using Milk Polar Lipid Liposomes with S-Layer Protein and Transport Study of the ACE-Inhibitory Peptide RLSFNP

“…A peak at 1744 cm –1 was due to the carbonyl (CO) bond in the phospholipid. The observed spectrum results are very similar to those of the naked liposomes studied previously. , Compared with naked MPL liposomes, SLP-LIP showed an absorption band corresponding to the N–H stretching vibration at wavenumbers of 3200–3600 cm –1 , which was the characteristic peak of the S-layer protein. These characteristic absorption peaks still appeared in SLP-LIP, suggesting the existence of the S-layer protein on the surface of SLP-LIP.…”

Egg-Curry: Insights into the Interaction Between Curcumin and Ovalbumin Using Spectroscopic Analyses and Protein-Ligand Docking Simulations

“…In both studies, fluorescence quenching results indicated that the binding constant value was on the order of 10 4 M −1 [7,8]. Some studies have also reported the complex formation between CU and OVA by the desolvation [9], by the coacervation with cellulose [10] and by loading CU into the nanogel of OVA [11][12][13]. In these studies, the complex sizes were, however, larger than 100 nm, and the information about binding or loading mechanism was not fully addressed in the aqueous solution.…”