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. 2023 Apr 4;12(7):1523.
doi: 10.3390/foods12071523.

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

Haoran Mo  1 , Xiuwen Chen  1 , Bo Cui  2 , Yangling Chen  1 , Maolong Chen  1 , Zhou Xu  1 , Li Wen  1 , Yunhui Cheng  1   2 , Ye Jiao  1
Affiliations

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

Haoran Mo et al. Foods. .

Abstract

In this study, soy isoflavones-loaded nanoparticles were prepared using rice proteins (RPs) hydrolyzed by four types of enzyme (alcalase, neutrase, trypsin, and flavorzyme). After optimizing the preparation conditions, the encapsulation efficiency (EE) of the nanoparticles ranged from 61.16% ± 0.92% to 90.65% ± 0.19%. The RPs that were hydrolyzed by flavorzyme with a molecular weight of <5 KDa showed better characters on the formation of nanoparticles, and the formed nanoparticles had the highest EE and loading capacity (9.06%), the smallest particle size (64.77 nm), the lowest polymer dispersity index (0.19), and the lowest zeta potential (-25.64 mV).The results of Fourier transform ion cyclotron resonance, X-ray diffraction, and fluorescence spectroscopy showed that the nanoparticles were successfully encapsulated. The study of interaction showed that the formation of nanoparticles may depend mainly on hydrogen bonds, but other interactions, such as hydrophobic interactions and electrostatic interactions, cannot be ignored. After encapsulation, the pH stability, temperature stability, ionic stability, and oxidation resistance of the nanoparticles were enhanced. Moreover, the in vitro release experiment showed that the encapsulated nanoparticles had a certain protective effect on soybean isoflavones. In summary, rice protein hydrolysates are promising carriers for soybean isoflavones.

Keywords: nanoparticles transport systems; rice protein; soy isoflavone.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
The encapsulation efficiency (EE) and loading capacity (LC) of rice protein hydrolysate soy isoflavone (RPH-SIF) nanoparticles at different degrees of hydrolysis (DH) of RPHs ((a): RPH(A), (b): RPH(T), (c): RPH(N), and (d): RPH(F)), the hydrophobicity (H0) of RPHs with different DHs. A–D Different superscript letters represent a significant difference (p < 0.01). a–d Different superscript letters represent a significant difference (p < 0.05).
Figure 2
Figure 2
The encapsulation efficiency (EE) and loading capacity (LC) of rice protein hydrolysate soy isoflavone (RPH-SIF) nanoparticles with different molecular weights of RPH ((a): RPH(A), (b): RPH(T), (c): RPH(N), and (d): RPH(F)), A–C Different superscript letters represent a significant difference (p < 0.01). a–c Different superscript letters represent a significant difference (p < 0.05).
Figure 3
Figure 3
The CLSM images of RPH(A)-SIF (a), RPH(T)-SIF (b), RPH(N)-SIF (c), and RPH(F)-SIF (d). Red and green represented RPHs and SIF, respectively.
Figure 4
Figure 4
Fourier transform infrared spectra (a) and X-ray diffraction (XRD) patterns (b) of SIF, RPH, and RPH-SIF complex nanoparticles.
Figure 5
Figure 5
The effects of temperature (a) on the retention of SIF in nanoparticles and the effects of ionic strength (b) and pH (c) on the particle size and PDI of SIF-loaded RPHs. A–D Different superscript letters represent a significant difference (p < 0.05).
Figure 6
Figure 6
DPPH (a) and ABTS scavenging activities (b) of free and encapsulated SIF. (c) Release percentage of SIF in RPHs during in vitro digestion. A–E Different superscript letters represent a significant difference (p < 0.05).
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