Inhibitory effects of chickpea and Tribulus terrestris on lipase, α-amylase and α-glucosidase

Food Chem. 2016 Aug 15;205:163-9. doi: 10.1016/j.foodchem.2016.03.012. Epub 2016 Mar 4.


The total saponin content and its in vitro bioaccessibilities in Tribulus terrestris and chickpea were determined by a static in vitro digestion method (COST FA1005 Action INFOGEST). Also, in vitro inhibitory effects of the chosen food samples on lipid and starch digestive enzymes were determined by evaluating the lipase, α-amylase and α-glucosidase activities. The tested T. terrestris and chickpea showed inhibitory activity against α-glucosidase (IC50 6967 ± 343 and 2885 ± 85.4 μg/ml, respectively) and α-amylase (IC50 343 ± 26.2 and 167 ± 6.12 μg/ml, respectively). The inhibitory activities of T. terrestris and chickpea against lipase were 15.3 ± 2.03 and 9.74 ± 1.09 μg/ml, respectively. The present study provides the first evidence that these food samples (T. terrestris, chickpea) are potent inhibitors of key enzymes in digestion of carbohydrates and lipids in vitro.

Keywords: 4-Nitrophenyl α-d-glucopyranoside (PNPG) (PubChem CID: 92969); Chickpea; Diosgenin (PubChem CID: 99474); In vitro bioaccessibility; Inhibitors; Lipase; Methanol (PubChem CID: 887); Pefabloc® SC (PubChem CID: 186136); Saponins; Tribulus terrestris; n-Butanol (PubChem CID: 263); α-Amylase; α-Glucosidase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cicer / chemistry*
  • Glycoside Hydrolase Inhibitors / therapeutic use*
  • Lipase / chemistry*
  • Plant Extracts / pharmacology*
  • Saponins / chemistry*
  • Tribulus / chemistry*
  • alpha-Amylases / chemistry*
  • alpha-Glucosidases / chemistry*


  • Glycoside Hydrolase Inhibitors
  • Plant Extracts
  • Saponins
  • Lipase
  • alpha-Amylases
  • alpha-Glucosidases