Basit öğe kaydını göster

dc.contributor.authorBursal, Ercan
dc.contributor.authorAras, Abdulmelik
dc.contributor.authorKılıç, Ömer
dc.contributor.authorTaslimi, Parham
dc.contributor.authorGören, Ahmet C.
dc.contributor.authorGülçin, İlhami
dc.date.accessioned2019-04-29T08:12:14Z
dc.date.available2019-04-29T08:12:14Z
dc.date.issued2019-03
dc.identifier.urihttp://hdl.handle.net/11772/1126
dc.description.abstractMany 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), alpha-amylase (AM), butyrylcholinesterase (BChE), and alpha-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. IC50 values of WES and MES were performed for radicals.en_US
dc.language.isoengen_US
dc.publisherJournal Of Food Biochemistryen_US
dc.relation.isversionof10.1111/jfbc.12776en_US
dc.rightsinfo:eu-repo/semantics/restrictedAccessen_US
dc.subjectAntioxidanten_US
dc.subjectCholinesteraseen_US
dc.subjectEnzyme inhibitionen_US
dc.subjectAlpha-amylaseen_US
dc.subjectAlpha-glycosidaseen_US
dc.titlePhytochemical content, antioxidant activity, and enzyme inhibition effect of Salvia eriophora Boiss. & Kotschy against acetylcholinesterase, α‐amylase, butyrylcholinesterase, and α‐glycosidase enzymesen_US
dc.typearticleen_US
dc.relation.journalJournal Of Food Bıochemıstryen_US
dc.contributor.departmentBartın Üniversitesi, Fen Fakültesi, Biyoteknoloji Bölümüen_US
dc.identifier.volume43en_US
dc.identifier.issue3en_US
dc.identifier.startpagee12776en_US


Bu öğenin dosyaları:

DosyalarBoyutBiçimGöster

Bu öğe ile ilişkili dosya yok.

Bu öğe aşağıdaki koleksiyon(lar)da görünmektedir.

Basit öğe kaydını göster