Polyphenols Weaken Pea Protein Gel by Formation of Large Aggregates with Diminished Noncovalent Interactions

• Published in: Biomacromolecules 2021-02, Vol.22 (2), p.1001-1014
• Main Authors: Chen, Da, Zhu, Xiao, Ilavsky, Jan, Whitmer, Tanya, Hatzakis, Emmanuel, Jones, Owen G, Campanella, Osvaldo H
• Format: Article
• Language: English
• Subjects: Animals; BASIC BIOLOGICAL SCIENCES; Gels; molecular dynamics; molecular dynamics simulation; Pea Proteins; Plant Proteins; polyphenol; Polyphenols; simulation; solid-state NMR; Tea; Viscosity
• ISSN: 1525-7797; 1526-4602
• DOI: 10.1021/acs.biomac.0c01753

Polyphenols are well-known native cross-linkers and gel strengthening agents for many animal proteins. However, their role in modifying plant protein gels remains unclear. In this study, multiple techniques were applied to unravel the influence of green tea polyphenols (GTP) on pea protein gels and the underlying mechanisms. We found that the elasticity and viscosity of pea protein gels decreased with increased GTP. The protein backbone became less rigid when GTP was present based on shortened T1ρ H in relaxation solid-state NMR measurements. Electron microscopy and small-angle X-ray scattering showed that gels weakened by GTP possessed disrupted networks with the presence of large protein aggregates. Solvent extraction and molecular dynamic simulation revealed a reduction in hydrophobic interactions and hydrogen bonds among proteins in gels containing GTP. The current findings may be applicable to other plant proteins for greater control of gel structures in the presence of polyphenols, expanding their utilization in food and biomedical applications.