Related Experiment Video
Updated: Jul 28, 2025
Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
Published on: September 11, 2015
Pulsed electric field improves the EGCG binding ability of pea protein isolate unraveled by multi-spectroscopy and
Ze-Ling Chen1, Ying Li2, Jin-Hua Wang3
1School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; Guangdong Provincial Key Laboratory of Food Intelligent Manufacturing, Foshan University, Foshan 528225, China; China-Singapore International Joint Research Institute, Guangzhou 510700, China; Research Institute of Yangjiang, South China University of Technology, Yangjiang 529500, China.
Abstract:
Understanding molecular mechanisms during protein modification is critical for expanding the application of plant proteins. This study investigated the conformational change and molecular mechanism of pea protein isolate (PPI) under pulsed electric field (PEF)-assisted (-)-Epigallocatechin-Gallate (EGCG) modification. The flexibility of PPI was significantly enhanced after PEF treatment (10 kV/cm) with decrease (23.25 %) in α-helix and increase (117.25 %) in random coil. The binding constant and sites of PEF-treated PPI with EGCG were increased by 2.35 times and 10.00 % (308 K), respectively. Molecular docking verified that PEF-treated PPI had more binding sites with EGCG (from 4 to 10). The number of amino acid residues involved in hydrophobic interactions in PEF-treated PPI-EGCG increased from 5 to 13. PEF-treated PPI-EGCG showed a significantly increased antioxidant activity compared to non-PEF-treated group. This work revealed the molecular level of PEF-assisted EGCG modification of PPI, which will be significant for the application of PPI in food industry.
