Academic Bibliography

 Search 200 years of publications by Ghent University researchers.
Advanced search
1 file | 7.33 MB
Add to list
  1. Search results
  2. The mechanism of resveratrol stabiliz...

The mechanism of resveratrol stabilization and degradation by synergistic interactions between constituent proteins of whey protein

Xin Yin, [missing] Wusigale, Hao Cheng, Paul Van der Meeren (UGent) and Li Liang
(2024) FOOD RESEARCH INTERNATIONAL. 188.
Author
Organization
Abstract
Whey protein isolate (WPI) is mainly composed of beta-lactoglobulin (beta-LG), alpha-lactalbumin (alpha-LA) and bovine serum albumin (BSA). The aim of this study was to compare and analyze the influence of WPI and its three main constituent proteins, as well as proportionally reconstituted WPI (R-WPI) on resveratrol. It was found that the storage stability of resveratrol was protected by WPI, not affected by R-WPI, but reduced by individual whey proteins at 45 degrees C for 30 days. The rank of accelerated degradation of resveratrol by individual whey proteins was BSA > alpha-LA > beta-LG. The antioxidant activity, localization of resveratrol and oxidation of carrier proteins were determined by ABTS, H2O2 assay, synchronous fluorescence, carbonyl and circular dichroism. The non-covalent interactions and disulfide bonds between constituent proteins improved the antioxidant activity of the R-WPI-resveratrol complex, the oxidation stability of the carrier and the solvent shielding effect on resveratrol, which synergistically inhibited the degradation of resveratrol in R-WPI system. The results gave insight into elucidating the interaction mechanism of resveratrol with protein carriers.
Keywords
Whey protein, Constituent protein, Resveratrol, Stability, Interaction, LIGAND-BINDING PROTEINS, BOVINE SERUM-ALBUMIN, BETA-LACTOGLOBULIN, ANTIOXIDANT ACTIVITY, ALPHA-LACTALBUMIN, COMPLEX COACERVATION, HYDROGEN-PEROXIDE, ACID, POLYPHENOLS, SPECTROSCOPY

Downloads

  • Download
    (...).pdf
    • full text (Published version)
    • |
    • UGent only
    • |
    • PDF
    • |
    • 7.33 MB

Citation

Please use this url to cite or link to this publication:

MLA
Yin, Xin, et al. “The Mechanism of Resveratrol Stabilization and Degradation by Synergistic Interactions between Constituent Proteins of Whey Protein.” FOOD RESEARCH INTERNATIONAL, vol. 188, 2024, doi:10.1016/j.foodres.2024.114485.
APA
Yin, X., Wusigale, [missing], Cheng, H., Van der Meeren, P., & Liang, L. (2024). The mechanism of resveratrol stabilization and degradation by synergistic interactions between constituent proteins of whey protein. FOOD RESEARCH INTERNATIONAL, 188. https://doi.org/10.1016/j.foodres.2024.114485
Chicago author-date
Yin, Xin, [missing] Wusigale, Hao Cheng, Paul Van der Meeren, and Li Liang. 2024. “The Mechanism of Resveratrol Stabilization and Degradation by Synergistic Interactions between Constituent Proteins of Whey Protein.” FOOD RESEARCH INTERNATIONAL 188. https://doi.org/10.1016/j.foodres.2024.114485.
Chicago author-date (all authors)
Yin, Xin, [missing] Wusigale, Hao Cheng, Paul Van der Meeren, and Li Liang. 2024. “The Mechanism of Resveratrol Stabilization and Degradation by Synergistic Interactions between Constituent Proteins of Whey Protein.” FOOD RESEARCH INTERNATIONAL 188. doi:10.1016/j.foodres.2024.114485.
Vancouver
1.
Yin X, Wusigale [missing], Cheng H, Van der Meeren P, Liang L. The mechanism of resveratrol stabilization and degradation by synergistic interactions between constituent proteins of whey protein. FOOD RESEARCH INTERNATIONAL. 2024;188.
IEEE
[1]
X. Yin, [missing] Wusigale, H. Cheng, P. Van der Meeren, and L. Liang, “The mechanism of resveratrol stabilization and degradation by synergistic interactions between constituent proteins of whey protein,” FOOD RESEARCH INTERNATIONAL, vol. 188, 2024.
@article{01JP53Y2PRASYXX9BBM8AMBQ71,
  abstract     = {{Whey protein isolate (WPI) is mainly composed of beta-lactoglobulin (beta-LG), alpha-lactalbumin (alpha-LA) and bovine serum albumin (BSA). The aim of this study was to compare and analyze the influence of WPI and its three main constituent proteins, as well as proportionally reconstituted WPI (R-WPI) on resveratrol. It was found that the storage stability of resveratrol was protected by WPI, not affected by R-WPI, but reduced by individual whey proteins at 45 degrees C for 30 days. The rank of accelerated degradation of resveratrol by individual whey proteins was BSA > alpha-LA > beta-LG. The antioxidant activity, localization of resveratrol and oxidation of carrier proteins were determined by ABTS, H2O2 assay, synchronous fluorescence, carbonyl and circular dichroism. The non-covalent interactions and disulfide bonds between constituent proteins improved the antioxidant activity of the R-WPI-resveratrol complex, the oxidation stability of the carrier and the solvent shielding effect on resveratrol, which synergistically inhibited the degradation of resveratrol in R-WPI system. The results gave insight into elucidating the interaction mechanism of resveratrol with protein carriers.}},
  articleno    = {{114485}},
  author       = {{Yin, Xin and Wusigale, [missing] and Cheng, Hao and Van der Meeren, Paul and Liang, Li}},
  issn         = {{0963-9969}},
  journal      = {{FOOD RESEARCH INTERNATIONAL}},
  keywords     = {{Whey protein,Constituent protein,Resveratrol,Stability,Interaction,LIGAND-BINDING PROTEINS,BOVINE SERUM-ALBUMIN,BETA-LACTOGLOBULIN,ANTIOXIDANT ACTIVITY,ALPHA-LACTALBUMIN,COMPLEX COACERVATION,HYDROGEN-PEROXIDE,ACID,POLYPHENOLS,SPECTROSCOPY}},
  language     = {{eng}},
  pages        = {{9}},
  title        = {{The mechanism of resveratrol stabilization and degradation by synergistic interactions between constituent proteins of whey protein}},
  url          = {{http://doi.org/10.1016/j.foodres.2024.114485}},
  volume       = {{188}},
  year         = {{2024}},
}
Altmetric
View in Altmetric
Web of Science
Times cited: