Microstructure of Sea Cucumber <i>Parastichopus </i><i>Tremulus</i> Peptide Hydrogels and Bioactivity in Caco-2 Cell Culture Model

• DOI: 10.20944/preprints202502.0387.v1
• Publication Date: 2025-02-07T02:38:16Z
• Authors: Miroslava R. Atan...; Jennifer Mildenbe...; Marianne D. Hansen; Tarmo Tamm

Wider availability of marine proteins for development of food and biomedical applications has high importance. Sea cucumber body wall proteins have specific functional properties which could be very promising for such product development. However, protein extraction from whole animals is costly and complex, whereas peptide hydrogel production by biotechnological methods can be considered an economically viable approach. Body-wall derived peptides from sea cucumber Parastichopus tremulus 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 calcium ion-containing buffer confirmed untargeted self-assembly with long, thick fibrillar formations at micro scale (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 in vitro through ORAC, ABTS and DPPH 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 highest IC 50 of 7.11 ± 0.84 mg/ml. This is the first report exploring microstructures of P. tremulus peptide hydrogels.