α-GLUCOSIDASE AND TYROSINASE INHIBITORY GUIDED ISOLATION, IDENTIFICATION OF MAJOR COMPOUND AND IN SILICO STUDY FROM EDIBLE MUSHROOM COPRINUS COMATUS
Crude Thermostable Cellulase from Geobacillus Kaustophilus as an Animal Feed Additive
DOI:
https://doi.org/10.55766/sujst-2024-04-e03986Keywords:
Diabetes mellitus, Hyperpigment, Molecular docking, Tyrosinase, α-glucosidaseAbstract
Coprinus comatus is an edible and medicinal mushroom. The crude hexane, EtOAc and methanol extracts were extracted successively from C. Comatus. All the crude extracts were evaluated for anti-a-glucosidase and tyrosinase. The results showed that %inhibition valued for the crude hexane, EtOAc and methanol extracts of anti-a-glucosidase were 98.58 ± 0.09, 98.90 ± 0.21, and 6.68 ± 0.79, respectively. The anti-tyrosinase for the crude hexane, EtOAc and methanol extracts were 97.31 ± 2.77, 97.31 ± 3.34 and 64.94 ± 3.34, respectively. Notably, the bioassay-guided showed that the crude hexane and EtOAc were the highest for anti-a-glucosidase and tyrosinase activities, which led to the interest in purifying the major compound. The isolation and purification were successively done using chromatographic techniques. The pure compounds were determined by spectroscopic analysis (UV, FTIR, and NMR) and comparison with previously reported. The isolation led to three compounds (1-3), ergosterol (1), indole-3-carbaldehyde (2), and 4-hydroxybenzoic acid (3). The molecular docking of compounds 1-3, reported as α-glucosidase and tyrosinase inhibitors, was done by the AutoDockTools 1.5.6 (ADT) software. The results revealed that ergosterol (1) provides the highest binding free energy (-9.91 kcal/mol) to the active site of a-glucosidase, indicating that it is quite specific to this enzyme. Moreover, ergosterol (1) has strong binding energy (-9.64 kcal/mol) to tyrosinase but not significant tyrosinase specificity. This evidence supports that C. Comatus would be applicable for a functional food for controlling glucose blood levels.
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