Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2022 Sep;102(12):5411-5421.
doi: 10.1002/jsfa.11894. Epub 2022 Apr 13.

Characteristics and structure of a soy protein isolate-lutein nanocomplex produced via high-pressure homogenization

Affiliations

Characteristics and structure of a soy protein isolate-lutein nanocomplex produced via high-pressure homogenization

Haodong Yang et al. J Sci Food Agric. 2022 Sep.

Abstract

Background: In recent years, nanocarriers for transporting active substances have attracted attention. This study was to explore the soy protein isolate (SPI) after high-pressure homogenization (HPH) (0, 30, 60, 90 and 120 MPa) as potential lutein carriers.

Results: The load amount (LA) and encapsulation efficiency (EE) of the SPI-lutein nanocomplexes at a homogenization pressure of 60 MPa were the highest (2.32 mg mL-1 and 92.85%, respectively), and the average particle size and ζ-potential of the SPI-lutein nanocomplexes were 192.1 nm and -30.06 mV, respectively. The DPPH (2,2-diphenyl-1-picrylhydrazyl) and hydroxyl-antioxidant activities of the complex increased from 12.4% and 23.3% to 52.7% and 61.07%, respectively, after the protein was treated with HPH. The surface hydrophobicity of the SPI and the SPI-lutein nanocomplexes increased with increasing homogenization pressure treatment. Fourier transform-infrared spectrophotometry analyses suggested that the homogenization treatments resulted in partial unfolding of the protein molecules, and the addition of lutein can also lead to the change of protein secondary structure. The fluorescence emission of SPI was quenched by lutein through the static quenching mechanism. Fluorescence experiments revealed that SPI and lutein had the strongest binding ability through hydrophobic interaction at a homogenization pressure of 60 MPa.

Conclusion: After HPH, the combination of SPI and lutein was beneficial, and the stability of lutein also improved after the combination. This study is conducive to expanding the application of soybean protein in the food industry. © 2022 Society of Chemical Industry.

Keywords: high-pressure homogenization; lutein; nanocomplexes; soy protein isolate.

PubMed Disclaimer

Similar articles

Cited by

References

REFERENCES

    1. Krinsky NI, Landrum JT and Bone RA, Biologic mechanisms of the protective role of lutein and zeaxanthin in the eye. Annu Rev Nutr 23:171-201 (2003).
    1. Tan TB, Yussof NS, Abas F, Mirhosseini H, Nehdi IA and Tan CP, Forming a lutein nanodispersion via solvent displacement method: the effects of processing parameters and emulsifiers with different stabilizing mechanisms. Food Chem 194:416-423 (2016).
    1. Niizu PY and Rodriguez-Amaya DB, New data on the carotenoid composition of raw salad vegetables. J Food Compos Anal 18:739-749 (2005).
    1. Sobral D and Renata G, Can lutein replace annatto in the manufacture of Prato cheese? LWT Food Sci Technol 68:349-355 (2016).
    1. Liang R, Shoemaker CF, Yang X, Zhong F and Huang Q, Stability and bioaccessibilityof β-Carotenein nanoemulsions stabilized by modified starches. J Agric Food Chem 61:1249-1257 (2013).

LinkOut - more resources