Self-assembly potential of bioactive peptides from Norwegian sea cucumber Parastichopus tremulus for development of functional hydrogels. (August 2021)

• Record Type: Journal Article
• Authors: Mildenberger, J.; Remm, M.; Atanassova, M.
• Is Part Of: Lebensmittel-Wissenschaft + Technologie =. Volume 148(2021)
• Publication Date: 2021-08
• Subjects: Parastichopus tremulus -- Sea cucumber -- Antioxidant -- Self-assembling peptides -- Hydrogels; Food industry and trade -- Periodicals; Food -- Composition -- Periodicals; Microbiology -- Periodicals; Nutrition -- Periodicals; 664.005
• DOI: 10.1016/j.lwt.2021.111678
• Languages: English
• ISSNs: 0023-6438

Abstract

Abstract: Hydrogels based on marine natural biopolymers have extensive possibilities for application in regenerative medicine, being best fit from safety and toxicity point of view, inexpensive and commercially available materials for 3D tissue scaffold development. In this study a peptide fraction from the temperate sea cucumber species Parastichopus tremulus has been characterized by de novo sequencing. ORAC antioxidant activity of 0, 35 ± 0, 05 TE/μg protein; IC50 of 22% and capacity to self-assemble into transparent hydrogel under physiological conditions have been experimentally determined. 926 MALDI-TOF peptide sequences were identified to belong to four protein types on basis of homology with Apostichopus japonicus and sea urchin proteins – major yolk protein, non-skeletal actin, collagen, and cluster BSL78-belonging. The surface hydrophobicity, gelation, and cytotoxicity of the P. tremulus peptides were studied and 13 peptide sequences from the collagen group were predicted in silico to have auto-assembly capacity. Graphical abstract: In vitro activity guided, size exclusion- based isolation of antioxidant peptides from sea cucumber protein hydrolysate and their physicochemical and bioinformatic characterization. Image 1 Highlights: A peptide fraction from sea cucumber Parastichopus tremulus was sequenced de novo . 926 sequences were identified by homology with A. japonicus and sea urchin proteins. FR5 had ORAC antioxidant activity 0, 35 ± 0, 05 TE/μg protein and IC50 of 22%. FR5 self-assembled into transparent hydrogel under physiological conditions. 13 collagen peptides were predicted in silico to have auto-assembly capacity.