Antimicrobial and anticholinesterase activities of the essential oils isolated from Salvia dicroantha Stapf., Salvia verticillata L. subsp amasiaca (Freyn and Bornm.) Bornm. and Salvia wiedemannii Boiss.


KUNDUHOĞLU B., KÜRKÇÜOĞLU M., DURU M. E., BAŞER K. H. C.

JOURNAL OF MEDICINAL PLANTS RESEARCH, cilt.5, sa.29, ss.6484-6490, 2011 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 5 Sayı: 29
  • Basım Tarihi: 2011
  • Doi Numarası: 10.5897/jmpr11.220
  • Dergi Adı: JOURNAL OF MEDICINAL PLANTS RESEARCH
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.6484-6490
  • Anahtar Kelimeler: Salvia dicroantha, Salvia verticillata subsp amasiaca, Salvia wiedemannii, essential oil, antimicrobial activity, anticholinesterase activity, minimum inhibitory concentrations (MICs), DEMENTIA
  • Anadolu Üniversitesi Adresli: Evet

Özet

In this study, the essential oil compositions and antimicrobial and anticholinesterase activities of three Turkish endemic Salvia species were investigated. The gas chromatography (GC) and gas chromatography - mass spectrometry (GC-MS) analysis of the essential oils obtained from Salvia dicroantha, Salvia verticillata subsp. amasiaca, and Salvia wiedemannii showed that the major constituents were caryophyllene oxide (22.4%), Germacrene D (36.6%), and a-pinene (36.2%), respectively. All essential oils exhibited antimicrobial activity against tested Gram-positive and Gram-negative bacteria, and test yeast strains. The minimum inhibitory concentrations (MICs) of oils ranged from 12.5 to 50.0 mu l/ml. Additionally, essential oils were more active than standard antifungals, inhibiting test strains of yeasts such as Candida albicans, Candida glabrata, and Saccharomyces cerevisiae. At 400 mu M concentration, the essential oil of S. wiedemannii had moderate acetylcholinesterase (55.95+/-2.01%), and butyrylcholinesterase (50.97+/-3.12%) inhibitory activity, while other two species no activity against both enzymes.