Antioxidant and anticholinesterase evaluation of selected Turkish Salvia species Ilkay Orhan a, * , Murat Kartal b , Qamar Naz c , Asma Ejaz c , Gu ¨ lderen Yilmaz d , Yu ¨ksel Kan e , Belma Konuklugil b , Bilge S ß ener a , M. Iqbal Choudhary c a Department of Pharmacognosy, Faculty of Pharmacy, Gazi University, 06330 Ankara, Turkey b Department of Pharmacognosy, Faculty of Pharmacy, Ankara University, 06110 Ankara, Turkey c H.E.J. Research Institute of Chemistry, International Center for Chemical Sciences, University of Karachi, 75270 Karachi, Pakistan d Department of Pharmaceutical Botany, Faculty of Pharmacy, Ankara University, 06110 Ankara, Turkey e Department of Field Crops, Faculty of Agriculture, Selc ¸uk University, 42070 Konya, Turkey Received 24 November 2005; received in revised form 18 July 2006; accepted 13 October 2006 Abstract Since Salvia species (Lamiaceae) have been recorded to be used against memory loss in European folk medicine, we herein examined in vitro anticholinesterase and antioxidant activities of 56 extracts prepared with petroleum ether, chloroform, ethyl acetate and meth- anol obtained from 14 Salvia species (Salvia albimaculata Hedge and Hub, Salvia aucheri Bentham var. canescens Boiss and Heldr, Salvia candidissima Vahl. ssp. occidentalis, Salvia ceratophylla L., Salvia cryptantha Montbret and Bentham, Salvia cyanescens Boiss and Bal., Salvia frigida Boiss, Salvia forskahlei L., Salvia halophilaHedge, Salvia migrostegia Boiss and Bal., Salvia multicaulis Vahl., Salvia sclarea L., Salvia syriaca L., Salvia verticillata L. ssp. amasiaca) growing in Turkey. The antioxidant activities were assessed by both chemical and enzymatic methods against 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging and xanthine/xanthine oxidase (XO) system generated superoxide anion radical inhibition. Anticholinesterase effect of the extracts was tested against both acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) at concentrations of 0.2 and 1 mg/ml using a microplate-reader assay based on the Ellman method. Most of the extracts did not show any activity against AChE at 0.2 mg/ml, while the chloroform extracts had noticeable inhi- bition against BChE between 47.7% and 74.7%. The most active extracts at 1 mg/ml for AChE inhibition were observed to be petroleum ether extract of Salvia albimaculata (89.4%) and chloroform extract of Salvia cyanescens (80.2%), whereas ethyl acetate extracts of Salvia frigida and Salvia migrostegia, chloroform extracts of Salvia candidissima ssp. occidentalis and Salvia ceratophylla, as well as petroleum ether extract of Salvia cyanescens were found to inhibit potently BChE (92.2%, 89.6%, 91.1%, 91.3%, and 91.8%, respectively). Partic- ularly, the ethyl acetate and methanol extracts were observed to be highly active against both DPPH and XO. Our data indicates that nonpolar extracts of Salvia species for anticholinesterase activity and the polar extracts for antioxidant activity are worth further phy- tochemical evaluation for identifying their active components. Ó 2006 Elsevier Ltd. All rights reserved. Keywords: Salvia; Lamiaceae; Acetylcholinesterase; Butyrylcholinesterase; Alzheimer’s disease; Antioxidant; DPPH; Free radical; Xanthine oxidase 1. Introduction Alzheimer’s disease (AD) is a degenerative neurological disorder characterized by senile plaques containing amy- loid b protein and loss of cholinergic neuromediators in the brain (Lawrence & Shakian, 1998; Whitehouse et al., 1982). The most remarkable biochemical change in AD patients is a reduction of acetylcholine (ACh) levels in the hippocampus and cortex of the brain (Jaen, Gregor, Lee, Davis, & Emmerling, 1996). Therefore, inhibition of acetylcholinesterase (AChE), the enzyme responsible for hydrolysis of ACh at the cholinergic synapse, is currently 0308-8146/$ - see front matter Ó 2006 Elsevier Ltd. All rights reserved. doi:10.1016/j.foodchem.2006.10.030 * Corresponding author. Tel.: +90 312 2023186; fax: +90 312 2235018. E-mail address: iorhan@gazi.edu.tr (I. Orhan). www.elsevier.com/locate/foodchem Food Chemistry 103 (2007) 1247–1254 Food Chemistry