Potential of Ginkgo biloba L. leaves in the management of hyperglycemia and hypertension using in vitro models

Bioresour Technol. 2009 Dec;100(24):6599-609. doi: 10.1016/j.biortech.2009.07.021. Epub 2009 Aug 8.

Abstract

Leaves from four different Ginkgo biloba L. trees (1 and 2--females; 3 and 4--males), grown at the same conditions, were collected during a period of 5 months (from June to October, 2007). Water and 12% ethanol extracts were analyzed for total phenolics content, antioxidant activity, phenolic profile, and the potential in vitro inhibitory effects on alpha-amylase, alpha-glucosidase, and Angiotensin I-Converting Enzyme (ACE) enzymes related to the management of diabetes and hypertension. The results indicated a significant difference among the trees in all functional benefits evaluated in the leaf extracts and also found important seasonal variation related to the same functional parameters. In general, the aqueous extracts had higher total phenolic content than the ethanolic extracts. Also, no correlation was found between total phenolics and antioxidant activity. In relation to the ACE inhibition, only ethanolic extracts had inhibitory activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / pharmacology
  • Animals
  • Antioxidants / analysis
  • Chromatography, High Pressure Liquid
  • Ginkgo biloba / chemistry*
  • Glycoside Hydrolase Inhibitors
  • Hyperglycemia / drug therapy*
  • Hypertension / drug therapy*
  • Kaempferols / pharmacology
  • Models, Biological*
  • Peptidyl-Dipeptidase A / metabolism
  • Phenols / analysis
  • Phytotherapy
  • Plant Extracts / pharmacology
  • Plant Extracts / therapeutic use*
  • Plant Leaves / chemistry*
  • Quercetin / pharmacology
  • Rabbits
  • Seasons
  • alpha-Amylases / antagonists & inhibitors

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Antioxidants
  • Glycoside Hydrolase Inhibitors
  • Kaempferols
  • Phenols
  • Plant Extracts
  • kaempferol
  • Quercetin
  • alpha-Amylases
  • Peptidyl-Dipeptidase A