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Bio-Guided Fractionation Driven by In Vitro α-Amylase Inhibition Assays of Essential Oils Bearing Specialized Metabolites with Potential Hypoglycemic Activity

Authors
  • Capetti, Francesca
  • Cagliero, Cecilia
  • Marengo, Arianna
  • Bicchi, Carlo
  • Rubiolo, Patrizia
  • Sgorbini, Barbara
Type
Published Article
Journal
Plants
Publisher
MDPI AG
Publication Date
Sep 21, 2020
Volume
9
Issue
9
Identifiers
DOI: 10.3390/plants9091242
PMID: 32967115
PMCID: PMC7569863
Source
PubMed Central
Keywords
Disciplines
  • Article
License
Green

Abstract

Type 2 diabetes mellitus (T2DM) is a metabolic disorder characterized by unpaired blood glycaemia maintenance. T2DM can be treated by inhibiting carbohydrate hydrolyzing enzymes (α-amylases and α-glucosidases) to decrease postprandial hyperglycemia. Acarbose and voglibose are inhibitors used in clinical practice. However, these drugs are associated with unpleasant gastrointestinal side effects. This study explores new α-amylase inhibitors deriving from plant volatile specialized metabolites. Sixty-two essential oils (EOs) from different plant species and botanical families were subjected to α-amylase in vitro enzymatic assay and chemically characterized using gas chromatography coupled to mass spectrometry. Several EOs were found to be potential α-amylase inhibitors, and Eucalyptus radiata , Laurus nobilis , and Myristica fragrans EOs displayed inhibitory capacities comparable to that of the positive control (i.e., acarbose). A bio-guided fractionation approach was adopted to isolate and identify the active fractions/compounds of Eucalyptus radiata and Myristica fragrans EOs. The bio-guided fractionation revealed that EOs α-amylase inhibitory activity is often the result of antagonist, additive, or synergistic interactions among their bioactive constituents and led to the identification of 1,8-cineole, 4-terpineol, α-terpineol, α-pinene, and β-pinene as bioactive compounds, also confirmed when they were tested singularly. These results demonstrate that EO oils are a promising source of potential α-amylase inhibitors.

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