Characterisation of Sargassum elegans fucoidans extracted using different technologies : linking their structure to α-glucosidase inhibition

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dc.contributor.author Mabate, Blessing
dc.contributor.author Daub, Chantal Desiree
dc.contributor.author Malgas, Samkelo
dc.contributor.author Pletschke, Brett Ivan
dc.date.accessioned 2025-02-13T09:51:41Z
dc.date.available 2025-02-13T09:51:41Z
dc.date.issued 2025-01
dc.description DATA AVAILABILITY : Data will be made available on request. en_US
dc.description.abstract Fucoidan, a sulphated polysaccharide found in brown seaweeds, has gained attention for its potential as an α-glucosidase inhibitor (AGI), which is significant for managing type 2 diabetes mellitus (T2DM). Although the use of brown algae for fucoidan extraction is becoming more popular, a few challenges remain, such as low extraction yields and a lack of understanding of the structure-activity relationship of fucoidan as an AGI. This study compared fucoidan extraction yields from S. elegans using three novel extraction methods (citrate buffer, EDTA, and enzyme-assisted extraction) and two well-established extraction protocols (hot water and mineral acid extraction). The structure-activity relationships of the fucoidan extracts as potential AGIs were then investigated. The fucoidan extraction yields for enzyme-assisted, citrate buffer, EDTA, hot water extraction and mineral acid extraction were 28 %, 20 %, 15 %, and 2.5 % and 3 %, respectively. Distinct structural features were noted from the fucoidan extracted by different techniques, according to their chemical profiles confirmed by their carbohydrate content, FTIR and NMR, and physical characteristics. Each extract exhibited unique chemical and structural properties. With IC50 values of 25 and 88 μg/ml, respectively, the fucoidans extracted by water and citrate buffer demonstrated the highest potency as AGIs, whereas the fucoidans extracted with the assistance of enzymes and EDTA showed IC50 values of 186 and 273 μg/ml. In summary, the extraction technology affected the fucoidans' structural and chemical compositions, impacting their biological activity as AGIs. Fucoidan's potent activity as an AGI represents a promising strategy for mitigating the burden of diabetes by reducing or preventing hyperglycaemia. Leveraging fucoidan could contribute meaningfully to developing alternative, natural therapeutic interventions for managing T2DM. en_US
dc.description.department Biochemistry, Genetics and Microbiology (BGM) en_US
dc.description.librarian hj2024 en_US
dc.description.sdg SDG-03:Good heatlh and well-being en_US
dc.description.sdg SDG-14:Life below water en_US
dc.description.sponsorship The German Academic Exchange Service (In-region-DAAD), the Pearson-Young Memorial Fellowship and Rhodes University and the Industrial Biocatalysis Hub (IBH), funded by the Department of Science and Innovation and the Technology Innovation Agency. en_US
dc.description.uri https://www.elsevier.com/locate/algal en_US
dc.identifier.citation Mabate, B., Daub, C.D., Malgas, S. et al. 2025, 'Characterisation of Sargassum elegans fucoidans extracted using different technologies : linking their structure to α-glucosidase inhibition', Algal Research, vol. 85, art. 103885, pp. 1-12, doi : 10.1016/j.algal.2024.103885. en_US
dc.identifier.issn 2211-9264 (online)
dc.identifier.other 10.1016/j.algal.2024.103885
dc.identifier.uri http://hdl.handle.net/2263/100824
dc.language.iso en en_US
dc.publisher Elsevier en_US
dc.rights © 2024 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by- nc-nd/4.0/). en_US
dc.subject Fucoidan en_US
dc.subject Type 2 diabetes mellitus (T2DM) en_US
dc.subject Sargassum elegans en_US
dc.subject α-Glucosidase inhibitor (AGI) en_US
dc.subject Enzyme-assisted extraction en_US
dc.subject SDG-03: Good health and well-being en_US
dc.subject Brown seaweeds en_US
dc.subject SDG-14: Life below water en_US
dc.title Characterisation of Sargassum elegans fucoidans extracted using different technologies : linking their structure to α-glucosidase inhibition en_US
dc.type Article en_US


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