Fucoidan from Ecklonia maxima is a powerful inhibitor of the diabetes-related enzyme, α-glucosidase.
Chemical Fractionation
Enzyme Activation
/ drug effects
Glycoside Hydrolase Inhibitors
/ chemistry
Hypoglycemic Agents
/ chemistry
Molecular Weight
Phaeophyceae
/ chemistry
Polymerization
Polysaccharides
/ chemistry
Seaweed
/ chemistry
Spectrum Analysis
Starch
/ chemistry
alpha-Glucosidases
/ chemistry
Ecklonia maxima
Fucoidan
α-Glucosidase
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
15 May 2020
15 May 2020
Historique:
received:
02
12
2019
revised:
11
02
2020
accepted:
15
02
2020
pubmed:
20
2
2020
medline:
4
2
2021
entrez:
20
2
2020
Statut:
ppublish
Résumé
Ecklonia maxima, an endemic South African seaweed, is a potential source of beneficial bioactive compounds. Among these compounds, fucoidan, a sulphated polysaccharide has a wide range of bioactivities including anti-diabetic activity. In this study, fucoidan was extracted from E. maxima by the hot water extraction method and then characterised by colorimetric assays for sugar composition. The extraction from E. maxima yielded 6.89% fucoidan which was found to contain 4.45 ± 0.25% L-fucose and 6.01 ± 0.53% sulphate. The water extracted E. maxima fucoidan had a low molecular weight of approximately 10 kDa. Structural studies (FT-IR, NMR and XRD) confirmed the structure and integrity of the fucoidan to be similar to previously studied fucoidans in literature. Finally, the activities of starch digestive enzymes; α-amylase and α-glucosidase, were investigated in the presence of the E. maxima fucoidan extract. Fucoidan from E. maxima was observed to be a potent mixed-type inhibitor of α-glucosidase with an IC
Identifiants
pubmed: 32070744
pii: S0141-8130(19)39663-1
doi: 10.1016/j.ijbiomac.2020.02.161
pii:
doi:
Substances chimiques
Glycoside Hydrolase Inhibitors
0
Hypoglycemic Agents
0
Polysaccharides
0
Starch
9005-25-8
fucoidan
9072-19-9
alpha-Glucosidases
EC 3.2.1.20
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
412-420Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.