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 language | English |
|---|---|
| Article number | 140381 |
| Journal | Food Chemistry |
| Volume | 459 |
| DOIs | |
| State | Published - 30 Nov 2024 |
| Externally published | Yes |
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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