In vitro digestion and cellular antioxidant activity of β-carotene-loaded emulsion stabilized by soy protein isolate-Pleurotus eryngii polysaccharide conjugates

2021 ◽  
Vol 112 ◽  
pp. 106340
Author(s):  
Qiuhui Hu ◽  
Yiliang Wu ◽  
Lei Zhong ◽  
Ning Ma ◽  
Liyan Zhao ◽  
...  
LWT ◽  
2020 ◽  
Vol 117 ◽  
pp. 108647 ◽  
Author(s):  
Anqi Zhang ◽  
Shuang Chen ◽  
Yuying Wang ◽  
Xibo Wang ◽  
Ning Xu ◽  
...  

Nanomaterials ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 167
Author(s):  
Yanlong Liu ◽  
Chang Liu ◽  
Shenyi Zhang ◽  
Jishu Li ◽  
Huanyu Zheng ◽  
...  

In this study, β-carotene-loaded nanoemulsions are emulsified using four biomacromolecular proteins—peanut protein isolate (PPI), soy protein isolate (SPI), rice bran protein isolate (RBPI), and whey protein isolate (WPI)—in order to explore their emulsion stability and in vitro digestion characteristics. All four nanoemulsions attained high encapsulation levels (over 90%). During the three-stage in vitro digestion model (including oral, gastric, and small intestine digestion phases), the PPI-emulsified nanoemulsion showed the highest lipolysis rates (117.39%) and bioaccessibility (37.39%) among the four nanoemulsions. Moreover, the PPI-emulsified nanoemulsion (with the smallest droplet size) also demonstrated the highest stability during storage and centrifugation, while those for the RBPI-emulsified nanoemulsion (with the largest droplet size) were the lowest. In addition, all four nanoemulsions showed superior oxidation stability when compared with the blank control of corn oil. The oxidation rates of the PPI- and WPI-stabilized groups were slower than the other two groups.


LWT ◽  
2021 ◽  
Vol 152 ◽  
pp. 112380
Author(s):  
Jingyuan Liu ◽  
Yangling Wan ◽  
Liuyang Ren ◽  
Mengdi Li ◽  
Ying Lv ◽  
...  

Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1721
Author(s):  
Yaru Wu ◽  
Zhucheng Yin ◽  
Xuejiao Qie ◽  
Yao Chen ◽  
Maomao Zeng ◽  
...  

The interaction of soy protein isolate (SPI) and its hydrolysates (SPIHs) with cyanidin-3-O-glucoside (C3G) at pH 7.0 were investigated to clarify the changes in the antioxidant capacity of their complexes. The results of intrinsic fluorescence revealed that C3G binds to SPI/SPIHs mainly through hydrophobic interaction, and the binding affinity of SPI was stronger than that of SPIHs. Circular dichroism and Fourier-transform infrared spectroscopy analyses revealed that the interaction with C3G did not significantly change the secondary structures of SPI/SPIHs, while the surface hydrophobicity and average particle size of proteins decreased. Furthermore, the SPI/SPIHs-C3G interaction induced an antagonistic effect on the antioxidant capacity (ABTS and DPPH) of the complex system, with the masking effect on the ABTS scavenging capacity of the SPIHs-C3G complexes being lower than that of the SPI-C3G complexes. This study contributes to the design and development of functional beverages that are rich in hydrolysates and anthocyanins.


Sign in / Sign up

Export Citation Format

Share Document