Preparation and Characterization of Soy Isoflavones Nanoparticles Using Polymerized Goat Milk Whey Protein as Wall Material

Abstract

Soy isoflavones (SIF) are a group of polyphenolic compounds with health benefits. However, application of SIF in functional foods is limited due to its poor aqueous solubility. SIF nanoparticles with different concentrations were prepared using polymerized goat milk whey protein (PGWP) as wall material. The goat milk whey protein was prepared from raw milk by membrane processing technology. The encapsulation efficiencies of all the nanoparticles were found to be greater than 70%. The nanoparticles showed larger particle size and lower zeta potential compared with the PGWP. Fourier Transform Infrared Spectroscopy indicated that the secondary structure of goat milk whey protein was changed after interacting with SIF, with transformation of α-helix and β-sheet to disordered structures. Fluorescence data indicated that interactions between SIF and PGWP decreased the fluorescence intensity. All nanoparticles had spherical microstructure revealed by Transmission Electron Microscope. Data indicated that PGWP may be a good carrier material for the delivery of SIF to improve its applications in functional foods.

Physicochemical, Digestive, and Sensory Properties of Panax Notoginseng Saponins Encapsulated by Polymerized Whey Protein

“…Results indicated that a part of the PNS was not encapsulated by PWP. Similar findings were reported by Tian et al [ 29 ], who found that encapsulation efficiency of soy isoflavones (SIF) in polymerized goat milk whey protein (PGWP) nanoparticles decreased with increasing SIF concentration. Researchers found that the curcumin showed higher encapsulation efficiency (93.1%) and oxidation stability using whey protein as the wall material [ 30 ].…”

Interaction between laccase and diethylstilbestrol based on multispectral and chromatography analyses

“…Additionally, similar binding constants in the order of 10 4 or 10 3 M −1 were described for numerous ligand‐protein complexes via fluorescence spectroscopic technique 30 . The increase of the binding constant with temperature increases indicated that the protein‐bound per unit of the fluorescent group increased 33 …”

“…30 The increase of the binding constant with temperature increases indicated that the protein-bound per unit of the fluorescent group increased. 33…”

Formation and Characterization of Self-Assembled Rice Protein Hydrolysate Nanoparticles as Soy Isoflavone Delivery Systems

“…However, the O–H bands changed to 3286 cm −1 , 3390 cm −1 , 3310 cm −1 , and 3298 cm −1 in the RPH(F)-SIF, RPH(A)-SIF, RPH(N)-SIF, and RPH(T)-SIF spectra, respectively. And the phenolic hydroxyl groups were involved in the non-covalent interaction between RPH and SIF [ 35 ]. After the formation of nanoparticles, the various shifts of O–H band observed may be related to the secondary structure of the RPHs [ 36 ].…”

“…The influences of RPHs may be due to their different structure obtained by the hydrolysis of different enzymes, which was further affected the interaction between RPH and SIF. Because the absorption site of SIF is in the intestinal epithelial cells [ 35 ], the RPH-SIF needed to ensure sufficient release of SIF in the intestine. These results also suggested that a large amount of SIF from the RPH(F)-SIF delivery system will reach the colon, where it can exert a beneficial effect [ 45 ].…”