Understanding Antidiabetic Potential of Oligosaccharides from Red Alga Dulse <i>Devaleraea inkyuleei</i> Xylan by Investigating α-Amylase and α-Glucosidase Inhibition
In this study, the α-glucosidase (maltase-glucoamylase: MGAM) and α-amylase inhibitory properties elicited by xylooligosaccharides (XOSs) prepared from dulse xylan were analysed as a potential mechanism to control postprandial hyperglycaemia for type-2 diabetes prevention and treatment. Xylan was pu...
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MDPI AG
2024-03-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/29/7/1536 |
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| author | Martin Alain Mune Mune Tadashi Hatanaka Hideki Kishimura Yuya Kumagai |
| author_facet | Martin Alain Mune Mune Tadashi Hatanaka Hideki Kishimura Yuya Kumagai |
| author_sort | Martin Alain Mune Mune |
| collection | DOAJ |
| description | In this study, the α-glucosidase (maltase-glucoamylase: MGAM) and α-amylase inhibitory properties elicited by xylooligosaccharides (XOSs) prepared from dulse xylan were analysed as a potential mechanism to control postprandial hyperglycaemia for type-2 diabetes prevention and treatment. Xylan was purified from red alga dulse powder and used for enzymatic hydrolysis using Sucrase X to produce XOSs. Fractionation of XOSs produced xylobiose (X2), β-(1→3)-xylosyl xylobiose (DX3), xylotriose (X3), β-(1→3)-xylosyl-xylotriose (DX4), and a dulse XOS mixture with <i>n</i> ≥ 4 xylose units (DXM). The different fractions exhibited moderate MGAM (IC<sub>50</sub> = 11.41–23.44 mg/mL) and α-amylase (IC<sub>50</sub> = 18.07–53.04 mg/mL) inhibitory activity, which was lower than that of acarbose. Kinetics studies revealed that XOSs bound to the active site of carbohydrate digestive enzymes, limiting access to the substrate by competitive inhibition. A molecular docking analysis of XOSs with MGAM and α-amylase clearly showed moderate strength of interactions, both hydrogen bonds and non-bonded contacts, at the active site of the enzymes. Overall, XOSs from dulse could prevent postprandial hyperglycaemia as functional food by a usual and continuous consumption. |
| first_indexed | 2024-04-24T10:39:05Z |
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| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-04-24T10:39:05Z |
| publishDate | 2024-03-01 |
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| series | Molecules |
| spelling | doaj.art-6259a308120c453c93c31524a8a4f4432024-04-12T13:23:20ZengMDPI AGMolecules1420-30492024-03-01297153610.3390/molecules29071536Understanding Antidiabetic Potential of Oligosaccharides from Red Alga Dulse <i>Devaleraea inkyuleei</i> Xylan by Investigating α-Amylase and α-Glucosidase InhibitionMartin Alain Mune Mune0Tadashi Hatanaka1Hideki Kishimura2Yuya Kumagai3Faculty of Science, University of Maroua, Maroua P.O. Box 814, CameroonOkayama Prefectural Technology Center for Agriculture, Forestry and Fisheries, Research Institute for Biological Sciences (RIBS), Okayama, 7549-1 Kibichuo-cho, Kaga-gun, Okayama 716-1241, JapanLaboratory of Marine Chemical Resource Development, Faculty of Fisheries Sciences, Hokkaido University, Hakodate 041-8611, JapanLaboratory of Marine Chemical Resource Development, Faculty of Fisheries Sciences, Hokkaido University, Hakodate 041-8611, JapanIn this study, the α-glucosidase (maltase-glucoamylase: MGAM) and α-amylase inhibitory properties elicited by xylooligosaccharides (XOSs) prepared from dulse xylan were analysed as a potential mechanism to control postprandial hyperglycaemia for type-2 diabetes prevention and treatment. Xylan was purified from red alga dulse powder and used for enzymatic hydrolysis using Sucrase X to produce XOSs. Fractionation of XOSs produced xylobiose (X2), β-(1→3)-xylosyl xylobiose (DX3), xylotriose (X3), β-(1→3)-xylosyl-xylotriose (DX4), and a dulse XOS mixture with <i>n</i> ≥ 4 xylose units (DXM). The different fractions exhibited moderate MGAM (IC<sub>50</sub> = 11.41–23.44 mg/mL) and α-amylase (IC<sub>50</sub> = 18.07–53.04 mg/mL) inhibitory activity, which was lower than that of acarbose. Kinetics studies revealed that XOSs bound to the active site of carbohydrate digestive enzymes, limiting access to the substrate by competitive inhibition. A molecular docking analysis of XOSs with MGAM and α-amylase clearly showed moderate strength of interactions, both hydrogen bonds and non-bonded contacts, at the active site of the enzymes. Overall, XOSs from dulse could prevent postprandial hyperglycaemia as functional food by a usual and continuous consumption.https://www.mdpi.com/1420-3049/29/7/1536dulsexylanoligosaccharidesα-glucosidase inhibitionmaltase-glucoamylaseα-amylase inhibition |
| spellingShingle | Martin Alain Mune Mune Tadashi Hatanaka Hideki Kishimura Yuya Kumagai Understanding Antidiabetic Potential of Oligosaccharides from Red Alga Dulse <i>Devaleraea inkyuleei</i> Xylan by Investigating α-Amylase and α-Glucosidase Inhibition Molecules dulse xylan oligosaccharides α-glucosidase inhibition maltase-glucoamylase α-amylase inhibition |
| title | Understanding Antidiabetic Potential of Oligosaccharides from Red Alga Dulse <i>Devaleraea inkyuleei</i> Xylan by Investigating α-Amylase and α-Glucosidase Inhibition |
| title_full | Understanding Antidiabetic Potential of Oligosaccharides from Red Alga Dulse <i>Devaleraea inkyuleei</i> Xylan by Investigating α-Amylase and α-Glucosidase Inhibition |
| title_fullStr | Understanding Antidiabetic Potential of Oligosaccharides from Red Alga Dulse <i>Devaleraea inkyuleei</i> Xylan by Investigating α-Amylase and α-Glucosidase Inhibition |
| title_full_unstemmed | Understanding Antidiabetic Potential of Oligosaccharides from Red Alga Dulse <i>Devaleraea inkyuleei</i> Xylan by Investigating α-Amylase and α-Glucosidase Inhibition |
| title_short | Understanding Antidiabetic Potential of Oligosaccharides from Red Alga Dulse <i>Devaleraea inkyuleei</i> Xylan by Investigating α-Amylase and α-Glucosidase Inhibition |
| title_sort | understanding antidiabetic potential of oligosaccharides from red alga dulse i devaleraea inkyuleei i xylan by investigating α amylase and α glucosidase inhibition |
| topic | dulse xylan oligosaccharides α-glucosidase inhibition maltase-glucoamylase α-amylase inhibition |
| url | https://www.mdpi.com/1420-3049/29/7/1536 |
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