Open Access
INHIBITORY EFFECT OF A STANDARDIZED HYDROETHANOLIC EXTRACT OF TERMINALIA ARJUNA BARK ON ALPHA-AMYLASE ENZYMEINHIBITORY EFFECT OF A STANDARDIZED HYDROETHANOLIC EXTRACT OF TERMINALIA ARJUNA BARK ON ALPHA-AMYLASE ENZYME
Author(s) -
Sushant Shengule,
Sanjay Mishra,
Shweta Bodhale
Publication year - 2018
Publication title -
asian journal of pharmaceutical and clinical research
Language(s) - English
Resource type - Journals
eISSN - 2455-3891
pISSN - 0974-2441
DOI - 10.22159/ajpcr.2018.v11i4.24019
Subject(s) - terminalia arjuna , ellagic acid , bark (sound) , traditional medicine , chemistry , gallic acid , alpha amylase , phytochemical , alpha glucosidase , polyphenol , high performance liquid chromatography , chromatography , amylase , terminalia , enzyme , biochemistry , antioxidant , biology , medicine , ecology
Objective: The present study was initiated to screen the hydroethanolic bark extract for α-amylase inhibitory activity and standardization of the Terminalia arjuna for polyphenolic phytochemicals using high-performance liquid chromatography-photo diode array (HPLC-PDA) method.Methods: The T. arjuna bark sample was extracted with ethanol: water (70:30 v/v) using Soxhlet extraction. A Dionex P680 HPLC system was used to acquire chromatograms. The screening of extract of T. arjuna bark has performed for in vitro α-amylase inhibitory assay. Each experiment was repeated 3 times. All values were expressed mean ± standard deviation.Results: The content of arjunetin, arjungenin, gallic acid, ellagic acid, and quercetin was 0.47, 8.22, 2.443, 7.901, and 3.20 mg/g, respectively, in a hydroethanolic extract of T. arjuna. The hydroethanolic extract of T. arjuna bark and acarbose has shown an inhibitory activity with an IC50 value 145.90 and 62.35 μg/mL, respectively.Conclusion: The hydroethanolic extract T. arjuna bark demonstrates α-amylase inhibitory activity due to a synergistic effect of the phytochemical constituents present in it. This study suggests that one of the mechanisms of this plant for antidiabetic activity is through the inhibition of α-amylase enzyme.