Phytochemical content, antioxidant activity, and enzyme inhibition effect of Salvia eriophora Boiss. & Kotschy against acetylcholinesterase, α-amylase, butyrylcholinesterase, and α-glycosidase enzymes.
Acetylcholinesterase
/ chemistry
Antioxidants
/ chemistry
Butyrylcholinesterase
/ chemistry
Cholinesterase Inhibitors
/ chemistry
Glycoside Hydrolases
/ antagonists & inhibitors
Kinetics
Phytochemicals
/ chemistry
Plant Extracts
/ chemistry
Salvia
/ chemistry
alpha-Amylases
/ antagonists & inhibitors
antioxidant
cholinesterase
enzyme inhibition
α-amylase
α-glycosidase
Journal
Journal of food biochemistry
ISSN: 1745-4514
Titre abrégé: J Food Biochem
Pays: United States
ID NLM: 7706045
Informations de publication
Date de publication:
03 2019
03 2019
Historique:
received:
22
10
2018
revised:
27
11
2018
accepted:
03
01
2019
entrez:
30
7
2019
pubmed:
30
7
2019
medline:
23
6
2020
Statut:
ppublish
Résumé
Many taxa of Salvia genus have been used in herbal beverages, food flavoring, cosmetics, and pharmaceutical industry. In this paper, chemical compounds of Salvia eriophora (S. eriophora) leaves were determined by LC-MS/MS (Liquid Chromatography tandem Mass Spectrometry). Salvigenin (158.64 ± 10.8 mg/kg), fumaric acid (123.09 ± 8.54 mg/kg), and quercetagetin-3.6-dimethylether (37.85 ± 7.09 mg/kg) were detected as major compounds in the ethanol extract, whereas fumaric acid (555.96 ± 38.56 mg/kg), caffeic acid (103.62 ± 20.51 mg/kg), and epicatechin (83.19 ± 8.43 mg/kg) were detected as major compounds in the water extract. Furthermore, enzyme inhibition of S. eriophora against acetylcholinesterase (AChE), α-amylase (AM), butyrylcholinesterase (BChE), and α-glycosidase (AG) enzymes were detected. AChE, BChE, AG, and AM enzymes were very strongly inhibited by S. eriophora water extract (WES) and S. eriophora methanol extract (MES). Additionally, antioxidant potential of S. eriophora was determined by in vitro analytical methods. IC
Substances chimiques
Antioxidants
0
Cholinesterase Inhibitors
0
Phytochemicals
0
Plant Extracts
0
Acetylcholinesterase
EC 3.1.1.7
Butyrylcholinesterase
EC 3.1.1.8
Glycoside Hydrolases
EC 3.2.1.-
alpha-Amylases
EC 3.2.1.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e12776Informations de copyright
© 2019 Wiley Periodicals, Inc.