Extraction and characterization of collagen and gelatin from body wall of sea cucumbers
Gelatin
Holothuria arenicola
Pepsin-solubilized collagen
Sea cucumber
Stichopus horrens
Journal
PeerJ
ISSN: 2167-8359
Titre abrégé: PeerJ
Pays: United States
ID NLM: 101603425
Informations de publication
Date de publication:
2024
2024
Historique:
received:
27
05
2024
accepted:
31
08
2024
medline:
14
10
2024
pubmed:
14
10
2024
entrez:
14
10
2024
Statut:
epublish
Résumé
Marine invertebrates, including sponges, molluscs, jellyfish, mussels, and sea cucumbers, are abundant sources of high-quality collagen and offer advantages such as availability, ease of processing, lower inflammatory response, and good metabolic compatibility. Approximately 70% of the total protein in the body wall of sea cucumbers is collagen. Gelatin is a water-soluble protein produced from heat-denatured collagen and has various industrial applications. Pepsin-solubilized collagen was extracted from the body wall of two sea cucumber Amino acid composition and SDS-PAGE analysis showed that the collagen from both species was type I, with one α1 chain and β chains, with molecular weights of 125 and 250 kDa, respectively. Glycine was the most abundant amino acid in the collagen from both sea cucumber species. The pepsin-soluble collagens from both species had high levels of glycine, proline, alanine, glutamic acid, and hydroxyproline. The gelatin from
Sections du résumé
Background
UNASSIGNED
Marine invertebrates, including sponges, molluscs, jellyfish, mussels, and sea cucumbers, are abundant sources of high-quality collagen and offer advantages such as availability, ease of processing, lower inflammatory response, and good metabolic compatibility. Approximately 70% of the total protein in the body wall of sea cucumbers is collagen. Gelatin is a water-soluble protein produced from heat-denatured collagen and has various industrial applications.
Methods
UNASSIGNED
Pepsin-solubilized collagen was extracted from the body wall of two sea cucumber
Results
UNASSIGNED
Amino acid composition and SDS-PAGE analysis showed that the collagen from both species was type I, with one α1 chain and β chains, with molecular weights of 125 and 250 kDa, respectively. Glycine was the most abundant amino acid in the collagen from both sea cucumber species. The pepsin-soluble collagens from both species had high levels of glycine, proline, alanine, glutamic acid, and hydroxyproline. The gelatin from
Identifiants
pubmed: 39399433
doi: 10.7717/peerj.18149
pii: 18149
pmc: PMC11471148
doi:
Substances chimiques
Gelatin
9000-70-8
Collagen
9007-34-5
Amino Acids
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e18149Informations de copyright
© 2024 Barzkar et al.
Déclaration de conflit d'intérêts
Balu Alagar Venmathi Maran is an Academic Editor for PeerJ.