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This study explores the isolation and characterization of two acidic polysaccharides from baobab (Adansonia digitata) fruits, named ADPs40-F3 and ADPs60-F3; the two types of acidic polysaccharides exhibited high sugar content and chemical structural features characterized by O–H, C–H, carbonyl C=O, and COOH carboxyl functional groups. The two fractions showed molecular weights of 1.66 × 105 and 9.59 × 104 Da. ADPs40-F3 residues consist of arabinose (2.80%), galactose (0.91%), glucose (3.60%), xylose (34.70%), and galacturonic acid (58.10%). On the other hand, ADPs60-F3 is composed of rhamnose (1.50%), arabinose (5.50%), galactose (2.50%), glucose (3.10%), xylose (26.00%), and galacturonic acid (61.40%). Furthermore, NMR analysis showed that the main acidic structures of ADPs40-F3 and ADPs60-F3 are formed by 4,6)-α-D-GalpA-(1→, →4)-β-D-Xylf-(1→, →4,6)-β-D-Glcp- (1→, →5)-α-L-Araf-(1→, →4,6)-α-D-Galp-(1→ residues and 4)-α-D-GalpA-(1→, →4)-β-D-Xylf-(1→, →6)-β-D-Glcp-(1→, →5)-α-L-Araf-(1→ 4,6)-α-D-Galp-(4,6→, →2)-α-Rhap- residues, respectively, based on the observed signals. Antioxidant assays against DPPH, ABTS+ , and FRAP revealed significant antioxidant activities for ADPs40-F3 and ADPs60-F3, comparable to ascorbic acid (VC). Additionally, both polysaccharides exhibited a dose-dependent inhibition of α-glucosidase and αamylase activities, suggesting potential anti-diabetic properties. In vivo evaluation demonstrated that ADPs60-F3 significantly reduced blood glucose levels, indicating promising therapeutic effects. These findings underscore the potential utility of baobab fruit polysaccharides as natural antioxidants and anti-diabetic agents. [ABSTRACT FROM AUTHOR]

Bioactive peptides have received significant attention due to their natural origin, low toxicity, and targeting specificity in the past decade. This study identified highly active ACE/XO inhibitors using molecular simulation and online databases and validated their in vitro antioxidant activity and the mechanisms of molecular interactions. According to computer predictions, Asp-Gly-Gly (DGG) and Asp-Gly-Met (DGGM) were identified as potential hydrolysates of common gastrointestinal peptidases with well water-soluble, non-toxic, and non-allergenic. Fourier transform infrared spectroscopy showed that the two peptides altered the enzyme's secondary structure, decreasing α-helix content by about 13 %, along with increasing β-sheet, randam coli, and β-turns content. Molecular docking and molecular dynamics simulations showed that hydrogen bonding and electrostatic interactions caused DGG and DGGM to form stable and dense complexes with the two enzymes. This study provides a new way for economical and efficient screening of new ACE and XO inhibitory peptides from natural proteins., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)