Inhibitory effects of chickpea and Tribulus terrestris on lipase, α-amylase and α-glucosidase
Publication type: Journal Article
Publication date: 2016-08-01
scimago Q1
wos Q1
SJR: 1.952
CiteScore: 18.3
Impact factor: 9.8
ISSN: 03088146, 18737072
PubMed ID:
27006227
General Medicine
Analytical Chemistry
Food Science
Abstract
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.
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Ercan P., El S. N. Inhibitory effects of chickpea and Tribulus terrestris on lipase, α-amylase and α-glucosidase // Food Chemistry. 2016. Vol. 205. pp. 163-169.
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Ercan P., El S. N. Inhibitory effects of chickpea and Tribulus terrestris on lipase, α-amylase and α-glucosidase // Food Chemistry. 2016. Vol. 205. pp. 163-169.
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TY - JOUR
DO - 10.1016/j.foodchem.2016.03.012
UR - https://doi.org/10.1016/j.foodchem.2016.03.012
TI - Inhibitory effects of chickpea and Tribulus terrestris on lipase, α-amylase and α-glucosidase
T2 - Food Chemistry
AU - Ercan, Pınar
AU - El, Sedef Nehir
PY - 2016
DA - 2016/08/01
PB - Elsevier
SP - 163-169
VL - 205
PMID - 27006227
SN - 0308-8146
SN - 1873-7072
ER -
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BibTex (up to 50 authors)
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@article{2016_Ercan,
author = {Pınar Ercan and Sedef Nehir El},
title = {Inhibitory effects of chickpea and Tribulus terrestris on lipase, α-amylase and α-glucosidase},
journal = {Food Chemistry},
year = {2016},
volume = {205},
publisher = {Elsevier},
month = {aug},
url = {https://doi.org/10.1016/j.foodchem.2016.03.012},
pages = {163--169},
doi = {10.1016/j.foodchem.2016.03.012}
}