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Formation of pea protein amyloid-like nanofibrils-derived hydrogels mediated by epigallocatechin gallate

  • Hailing Zhang
  • , Ling Kang
  • , Rizwan Ahmed Bhutto
  • , Yuting Fan
  • , Jiang Yi*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

This study investigated the interaction between pea protein amyloid-like nanofibril and epigallocatechin gallate, constructed and characterized the novel pea protein nanofibrils-derived hydrogel mediated by epigallocatechin gallate, and researched the functionalities of the hydrogel. Epigallocatechin gallate remodeled the structure of pea protein nanofibrils, and a stable and strong hydrogel was formed at a relatively low protein concentration (4.5%). Additionally, the hydrogels exhibited various surface structures and hydrogel properties dependent on the mass ratio. Strongest gel strength (51 g) was attained at 0.25 epigallocatechin gallate/pea protein nanofibrils mass ratio. Whereas, the hydrogels exhibited the highest water holding capacity (87%) at 0.05 mass ratio. The primary driving forces in the formation and maintaining of the hydrogels were hydrophobic interactions and ionic bonds. Progressive rise of β-sheet content of pea protein nanofibrils occurred increasing epigallocatechin gallate concentration. This hydrogel holds great potential for applications in food processing, targeted delivery of nutraceuticals and biomedicine.

Original languageEnglish
Article number140381
JournalFood Chemistry
Volume459
DOIs
StatePublished - 30 Nov 2024
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2024 Elsevier Ltd

Keywords

  • Amyloid-like fibril
  • EGCG
  • Hydrogel
  • Molecular interaction
  • Pea protein

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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