Please use this identifier to cite or link to this item: http://hdl.handle.net/11452/23532
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dc.date.accessioned2021-12-23T13:12:40Z-
dc.date.available2021-12-23T13:12:40Z-
dc.date.issued2011-10-
dc.identifier.citationAybastıer, O. vd. (2011). "Determination of total phenolic content in Prunella L. by horseradish peroxidase immobilized onto chitosan beads". Analytical Methods, 3(10), 2289-2297.en_US
dc.identifier.issn1759-9660-
dc.identifier.issn1759-9679-
dc.identifier.urihttps://doi.org/10.1039/c1ay05218g-
dc.identifier.urihttps://pubs.rsc.org/en/content/articlelanding/2011/ay/c1ay05218g-
dc.identifier.urihttp://hdl.handle.net/11452/23532-
dc.description.abstractHorseradish Peroxidase (HRP) was immobilized by covalent binding onto glutaraldehyde cross-linked chitosan beads and these beads were used for determination of total phenolic content in Prunella L. species. Central composite design (CCD) was employed to optimize the conditions for the maximum HRP activity and to understand the significance and interaction of the factors affecting the activity of immobilized HRP. The results indicated that enzyme concentration and immobilization time were significant factors for the immobilization of HRP. The optimum conditions were determined as enzyme concentration 0.25 mg mL(-1), pH 8.0 and immobilization time 20h. The recovered activity was obtained as 81% after immobilization under optimal conditions. Total phenol content was determined in four Prunella L. species (Prunella vulgaris L., Prunella laciniata (L.) L., Prunella orientalis Bornm., Prunella grandiflora L.) extracted using methanol, water and methanol/water (4 : 1, v/v). The enzymatic method is based on the spectrophometric measurement of the final quinone-imine colored product, absorbing at 510 nm, by HRP oxidation in presence of hydrogen peroxide. The results were compared with those obtained by applying the Folin method. The highest total phenol content was obtained with the methanol/water (4 : 1, v/v) extract of Prunella vulgaris L. by immobilized HRP method (63.75 mg gallic acid equivalent (GAE) per g dried plant). Operational stability was determined with immobilized HRP and it indicated that a small enzyme deactivation (15%) occurred after 10 consecutive uses.en_US
dc.language.isoenen_US
dc.publisherRoyal Soc Chemistryen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectChemistryen_US
dc.subjectFood science & technologyen_US
dc.subjectSpectroscopyen_US
dc.subjectAntioxidan capatyen_US
dc.subjectRosmarin aciden_US
dc.subjectStabilityen_US
dc.subjectVulgarisen_US
dc.subjectOptimizasyonen_US
dc.subjectOxideen_US
dc.subjectLipaseen_US
dc.subjectFreshen_US
dc.subjectAldehydesen_US
dc.subjectBiological water treatmenten_US
dc.subjectChitosanen_US
dc.subjectHydrogen peroxideen_US
dc.subjectMethanolen_US
dc.subjectOptimizationen_US
dc.subjectOxidationen_US
dc.subjectPhenolsen_US
dc.subjectSolvent extractionen_US
dc.subjectCentral composite designsen_US
dc.subjectChitosan beadsen_US
dc.subjectColored productsen_US
dc.subjectCovalent bindingen_US
dc.subjectCross linked chitosanen_US
dc.subjectEnzymatic methodsen_US
dc.subjectEnzyme concentrationsen_US
dc.subjectEnzyme deactivationen_US
dc.subjectGallic acidsen_US
dc.subjectGlutaraldehydesen_US
dc.subjectHorseradish peroxidaseen_US
dc.subjectOperational stabilityen_US
dc.subjectOptimal conditionsen_US
dc.subjectOptimum conditionsen_US
dc.subjectTotal phenolic contenten_US
dc.subjectTotal phenolsen_US
dc.subjectVulgarisen_US
dc.subjectEnzyme immobilizationen_US
dc.titleDetermination of total phenolic content in Prunella L. by horseradish peroxidase immobilized onto chitosan beadsen_US
dc.typeArticleen_US
dc.identifier.wos000295617000014tr_TR
dc.identifier.scopus2-s2.0-80053938190tr_TR
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergitr_TR
dc.contributor.departmentUludağ Üniversitesi/Fen-Edebiyat Fakültesi/Kimya Anabilim Dalı.tr_TR
dc.relation.bap2009/38tr_TR
dc.contributor.orcid0000-0003-1508-0181tr_TR
dc.contributor.orcid0000-0002-0380-1992tr_TR
dc.contributor.orcid0000-0002-4101-8448tr_TR
dc.contributor.orcid0000-0002-9381-0410tr_TR
dc.identifier.startpage2289tr_TR
dc.identifier.endpage2297tr_TR
dc.identifier.volume3tr_TR
dc.identifier.issue10tr_TR
dc.relation.journalAnalytical Methodsen_US
dc.contributor.buuauthorAybastıer, Önder-
dc.contributor.buuauthorŞahin, Saliha-
dc.contributor.buuauthorIşık, Esra-
dc.contributor.buuauthorDemir, Cevdet-
dc.contributor.researcheridAAH-2892-2021tr_TR
dc.contributor.researcheridABA-2005-2020tr_TR
dc.contributor.researcheridX-4621-2018tr_TR
dc.subject.wosChemistry, analyticalen_US
dc.subject.wosFood science & technologyen_US
dc.subject.wosSpectroscopyen_US
dc.indexed.wosSCIEen_US
dc.indexed.scopusScopusen_US
dc.wos.quartileQ3en_US
dc.wos.quartileQ2 (Food science & technology)en_US
dc.contributor.scopusid35344478800tr_TR
dc.contributor.scopusid15027401600tr_TR
dc.contributor.scopusid50761143600tr_TR
dc.contributor.scopusid7003565902tr_TR
dc.subject.scopusImmobilized Enzymes; Candida Rugosa; Penicillin Amidaseen_US
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