Adsorption equilibrium, kinetics and thermodynamics of alpha-amylase on poly(DVB-VIM)-Cu+2 magnetic metal-chelate affinity sorbent

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dc.contributor.buuauthorOsman, Bilgen
dc.contributor.buuauthorKara, Ali
dc.contributor.buuauthorDemirbel, Emel
dc.contributor.buuauthorKök, Şenay
dc.contributor.buuauthorBeşirli, Necati
dc.contributor.departmentUludağ Üniversitesi/Fen-Edebiyat Fakültesi/Kimya Bölümü.tr_TR
dc.contributor.researcheridAAG-6271-2019tr_TR
dc.contributor.researcheridABF-4791-2020tr_TR
dc.contributor.scopusid15221651200tr_TR
dc.contributor.scopusid7102824859tr_TR
dc.contributor.scopusid54681740300tr_TR
dc.contributor.scopusid37054138900tr_TR
dc.contributor.scopusid6507924888tr_TR
dc.date.accessioned2022-05-13T12:38:30Z
dc.date.available2022-05-13T12:38:30Z
dc.date.issued2012-09
dc.description.abstractDesigning an immobilised metal ion affinity process on large-scale demands that a thorough understanding be developed regarding the adsorption behaviour of proteins on metal-loaded gels and the characteristic adsorption parameters to be evaluated. In view of this requirement, interaction of alpha-amylase as a model protein with newly synthesised magnetic-poly(divinylbenzene-1-vinylimidazole) [m-poly(DVB-VIM)] microbeads (average diameter, 53-212 mu m) was investigated. The m-poly(DVB-VIM) microbeads were prepared by copolymerising of divinylbenzene (DVB) with 1-vinylimidazole (VIM). The m-poly(DVB-VIM) microbeads were characterised by N-2 adsorption/desorption isotherms, electron spin resonance, elemental analysis, scanning electron microscope and swelling studies. Cu2+ ions were chelated on the m-poly(DVB-VIM) beads and used in adsorption of alpha-amylase in a batch system. The maximum alpha-amylase adsorption capacity of the m-poly(DVB-VIM)-Cu2+ beads was determined as 10.84 mg/g at pH 6.0, 25 A degrees C. The adsorption data were analyzed using three isotherm models, which are the Langmuir, Freundlich and Dubinin-Radushkevich isotherm models. The pseudo-first-order, pseudo-second-order, modified Ritchie's-second-order and intraparticle diffusion models were used to test dynamic experimental data. The study of temperature effect was quantified by calculating various thermodynamic parameters such as Gibbs free energy, enthalpy and entropy changes.en_US
dc.identifier.citationOsman, B. vd. (2012). "Adsorption equilibrium, kinetics and thermodynamics of alpha-amylase on poly(DVB-VIM)-Cu+2 magnetic metal-chelate affinity sorbent". Applied Biochemistry and Biotechnology, 168(2), 279-294.en_US
dc.identifier.endpage294tr_TR
dc.identifier.issn0273-2289
dc.identifier.issn1559-0291
dc.identifier.issue2tr_TR
dc.identifier.pubmed22736275tr_TR
dc.identifier.scopus2-s2.0-84866729881tr_TR
dc.identifier.startpage279tr_TR
dc.identifier.urihttps://doi.org/10.1007/s12010-012-9771-z
dc.identifier.urihttps://link.springer.com/article/10.1007%2Fs12010-012-9771-z
dc.identifier.urihttp://hdl.handle.net/11452/26460
dc.identifier.volume168tr_TR
dc.identifier.wos000309224300006tr_TR
dc.indexed.pubmedPubMeden_US
dc.indexed.scopusScopusen_US
dc.indexed.wosSCIEen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.journalApplied Biochemistry and Biotechnologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergitr_TR
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBiochemistry & molecular biologyen_US
dc.subjectBiotechnology & applied microbiologyen_US
dc.subjectImmobilised metal ion affinityen_US
dc.subjectImaen_US
dc.subjectProtein adsorptionen_US
dc.subjectAlpha-amylaseen_US
dc.subjectMagnetic beadsen_US
dc.subjectAqueous-solutionen_US
dc.subjectIonsen_US
dc.subjectImmobilizationen_US
dc.subjectBeadsen_US
dc.subjectProteinsen_US
dc.subjectRemovalen_US
dc.subjectZn(II)en_US
dc.subjectMatrixen_US
dc.subjectWateren_US
dc.subjectAdsorption isothermsen_US
dc.subjectAmylasesen_US
dc.subjectChelationen_US
dc.subjectDyesen_US
dc.subjectFree energyen_US
dc.subjectGibbs free energyen_US
dc.subjectMagnetic momentsen_US
dc.subjectMetal ionsen_US
dc.subjectMetalsen_US
dc.subjectScanning electron microscopyen_US
dc.subjectAdsorption capacitiesen_US
dc.subjectAdsorption equilibriaen_US
dc.subjectIntraparticle diffusion modelsen_US
dc.subjectKinetics and thermodynamicsen_US
dc.subjectMagnetic beadsen_US
dc.subjectMetal ion affinitiesen_US
dc.subjectThermodynamic parameteren_US
dc.subjectAdsorptionen_US
dc.subject.emtree1 vinylimidazole derivativeen_US
dc.subject.emtreeAmylaseen_US
dc.subject.emtreeCopperen_US
dc.subject.emtreeDivinylbenzeneen_US
dc.subject.emtreeMetal chelateen_US
dc.subject.emtreeSorbenten_US
dc.subject.emtreeAdsorptionen_US
dc.subject.emtreeAdsorption equilibriumen_US
dc.subject.emtreeArticleen_US
dc.subject.emtreeChemical analysisen_US
dc.subject.emtreeDesorptionen_US
dc.subject.emtreeDiffusionen_US
dc.subject.emtreeElectron spin resonanceen_US
dc.subject.emtreeEntropyen_US
dc.subject.emtreeIsothermen_US
dc.subject.emtreeKineticsen_US
dc.subject.emtreeModelen_US
dc.subject.emtreePolymerizationen_US
dc.subject.emtreeScanning electron microscopyen_US
dc.subject.emtreeTemperatureen_US
dc.subject.emtreeThermodynamicsen_US
dc.subject.scopusImmobilized Enzymes; Amylases; Storage Stabilityen_US
dc.subject.wosBiochemistry & molecular biologyen_US
dc.subject.wosBiotechnology & applied microbiologyen_US
dc.titleAdsorption equilibrium, kinetics and thermodynamics of alpha-amylase on poly(DVB-VIM)-Cu+2 magnetic metal-chelate affinity sorbenten_US
dc.typeArticle
dc.wos.quartileQ4 (Biochemistry & Molecular Biology)en_US
dc.wos.quartileQ3 (Biotechnology & applied microbiology)en_US

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