In vitro and In silico Analysis of Pomegranate (Punica granatum L.) Fruit Powder as Pancreatic Lipase and α-Amylase Inhibitor

Journal of Physics: Conference Series
2020.0

Abstract

This study aims are to produce pomegranate powder, then to extracted with boiling water and to find out the phytochemical compounds, total phenolic compounds (TPC), total flavonoid compounds (TFC) and its inhibitory activity against pancreatic lipase by in vitro analysed. Besides of that, a compound that exist in pomegranate will also be in silico analysed by docking technique, for its binding with the α-amylase enzyme compared to acarbose. In vitro inhibition tests were conducted by titrimetric method, using olive oil as substrate, pancreatic lipase as enzymes, and orlistat as a standard inhibitor; meanwhile the in silico test was conducted by molecular docking techniques using human α -amylase as a receptor and acarbose and a compound in pomegranate (quercetin) as ligand. The result has shown that hot water extracts of pomegranate fruits powder (1.5 gr/150 ml) contained flavonoids, polyphenols, and alkaloids and TPC and TFC contents were 2.090 ppm and 2.058 ppm, respectively; had pancreatic lipase inhibition activity of 0.54 times compared to orlistat at the same mass (120 mg), and based on its molecular docking, quercetin, a compound in the pomegranate can bind to the α-amylase enzyme in a position that is relatively the same as acarbose, even with slightly larger affinity bindings. © Published under licence by IOP Publishing Ltd.

Knowledge Graph

Similar Paper

In vitro and In silico Analysis of Pomegranate (Punica granatum L.) Fruit Powder as Pancreatic Lipase and α-Amylase Inhibitor
Journal of Physics: Conference Series 2020.0
Molecular modelling and in vitro studies ofDaruharidraas a potent alpha-amylase inhibitor
Journal of Biomolecular Structure and Dynamics 2023.0
In silico docking studies of α-amylase inhibitors from the anti-diabetic plant Leucas ciliata Benth. and an endophyte, Streptomyces longisporoflavus
3 Biotech 2021.0
α-Glucosidase and α-amylase inhibitory activities of guava leaves
Food Chemistry 2010.0
Flavonoids for Controlling Starch Digestion: Structural Requirements for Inhibiting Human α-Amylase
Journal of Medicinal Chemistry 2008.0
Chemical and biochemical characterization of Ipomoea aquatica: genoprotective potential and inhibitory mechanism of its phytochemicals against α-amylase and α-glucosidase
Frontiers in Nutrition 2023.0
Medicinal uses, pharmacological activities, phytochemistry, and the molecular mechanisms of Punica granatum L. (pomegranate) plant extracts: A review
Biomedicine & Pharmacotherapy 2022.0
In vitro and in silico elucidation of antidiabetic and anti-inflammatory activities of bioactive compounds from Momordica charantia L.
Bioorganic & Medicinal Chemistry 2019.0
Potential pancreatic lipase inhibitory activity of phenolic constituents from the root bark of Morus alba L.
Bioorganic & Medicinal Chemistry Letters 2016.0
Inhibition of pancreatic lipase by berberine and dihydroberberine: an investigation by docking simulation and experimental validation
Medicinal Chemistry Research 2013.0