Microstructure of Sea Cucumber <i>Parastichopus tremulus</i> Peptide Hydrogels and Bioactivity in Caco-2 Cell Culture Model
Wider availability of marine proteins for the development of food and biomedical applications has a high importance. Sea cucumber body wall proteins have specific functional properties that could be very promising for such product development. However, protein extraction from whole animals is costly...
Saved in:
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-04-01
|
| Series: | Gels |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2310-2861/11/4/280 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | Wider availability of marine proteins for the development of food and biomedical applications has a high importance. Sea cucumber body wall proteins have specific functional properties that could be very promising for such product development. However, protein extraction from whole animals is costly and complex, whereas peptide hydrogel production using biotechnological methods can be considered an economically viable approach. Body-wall derived peptides from sea cucumber <i>Parastichopus tremulus</i> have been suggested as a nontraditional source of potentially edible hydrocolloids. In the current work, four peptides were produced through custom synthesis. Scanning electron microscopy (SEM) of the combined mix of the four peptides (1:1 ratio; 15 mM concentration) in a calcium ion-containing buffer confirmed untargeted self-assembly with long, thick fibrillar formations at a microscale (measured mean cross-section 2.78 µm and length sizes of 26.95 µm). The antioxidant activity of the peptides separately, and in combination (1:1 molar ratio), was studied <i>in vitro</i> through ORAC (values in the range from 279 to 543 µmol TE/g peptide), ABTS (from 80.4 to 1215 µmol TE/g peptide), and DPPH (from 5.2 to 19.9 µmol TE/g) assays, and confirmed for protection against oxidation in a Caco-2 cell culture model. Angiotensin-I converting enzyme inhibitory activity was also confirmed for two of the four peptides, with the highest IC 50 of 7.11 ± 0.84 mg/mL. |
|---|---|
| ISSN: | 2310-2861 |