Understanding Antidiabetic Potential of Oligosaccharides from Red Alga Dulse Devaleraea inkyuleei Xylan by Investigating α-Amylase and α-Glucosidase Inhibition.

Publisher: MDPI Country of Publication: Switzerland NLM ID: 100964009 Publication Model: Electronic Cited Medium: Internet ISSN: 1420-3049 (Electronic) Linking ISSN: 14203049 NLM ISO Abbreviation: Molecules Subsets: MEDLINE

Original Publication: Basel, Switzerland : MDPI, c1995-

alpha-Amylases* ; Hyperglycemia* ; Edible Seaweeds* ; Rhodophyta* ; Glucuronates*; Humans ; alpha-Glucosidases ; Hypoglycemic Agents/pharmacology ; Xylans/pharmacology ; Molecular Docking Simulation ; Oligosaccharides/pharmacology

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 n ≥ 4 xylose units (DXM). The different fractions exhibited moderate MGAM (IC 50 = 11.41-23.44 mg/mL) and α-amylase (IC 50 = 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.

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Keywords: dulse; enzyme kinetics; maltase-glucoamylase; molecular docking; oligosaccharides; xylan; α-amylase inhibition; α-glucosidase inhibition

EC 3.2.1.1 (alpha-Amylases)
EC 3.2.1.20 (alpha-Glucosidases)
0 (Hypoglycemic Agents)
0 (Xylans)
0 (xylooligosaccharide)
0 (Oligosaccharides)
0 (Glucuronates)

Palmaria palmata

Date Created: 20240413 Date Completed: 20240415 Latest Revision: 20240425

20240425

PMC11013419

10.3390/molecules29071536

38611816