Publication:
Immobilization of glucoamylase onto lewis metal ion chelated magnetic affinity sorbent: Kinetic, isotherm and thermodynamic studies

dc.contributor.buuauthorOsman, Bilgen
dc.contributor.buuauthorKara, Ali
dc.contributor.buuauthorBeşirli, Necati
dc.contributor.departmentFen Edebiyat Fakültesi
dc.contributor.departmentKimya Ana Bilim Dalı
dc.contributor.researcheridAAG-6271-2019
dc.contributor.researcheridABF-4791-2020
dc.contributor.scopusid15221651200
dc.contributor.scopusid7102824859
dc.contributor.scopusid6507924888
dc.date.accessioned2021-12-23T07:07:33Z
dc.date.available2021-12-23T07:07:33Z
dc.date.issued2011
dc.description.abstractIn this study, magnetic metal-chelate beads, m-poly(ethylene glycol dimethacrylate-vinyl imidazole) [m-poly(EGDMA-VIM)] with an average diameter 150-200 m was synthesized by copolymerizing ethylene glycol dimethacrylate (EGDMA) with vinyl imidazole (VIM). The spesific surface area of the m-poly(EGDMA-VIM) beads was found 63.1 m2/g. Cu2+ ions were chelated on the m-poly(EGDMA-VIM) beads and used in immobilization of Aspergillus niger glucoamylase in a batch system. The maximum glucoamylase adsorption capacity of the m-poly(EGDMA-VIM)-Cu2+ beads was observed as 120 mg/g at pH 6.5. The optimum pH for free and m-poly(EGDMA-VIM)-Cu2+ immobilized glucoamylase were found 4.0 and 4.5, respectively. The optimum temperature of glucoamylase was not changed after immobilization and determined as 60oC for free and immobilized enzyme preparations. The glucoamylase adsorption capacity and adsorbed enzyme activity slightly decreased after 10 batch successive reactions, demonstrating the usefulness of the enzyme-loaded beads in biocatalytic applications. Storage stability was found to increase with immobilization. The effect of various experimental parameters such as pH, glucoamylase concentration, contact time and temperature in aqueous solution were also investigated. Adsorption isotherm obtained for m-poly(EGDMA-VIM)-Cu2+ was consistent with Langmuir model. Kinetic studies showed that the adsorption process agreed with both the pseudo-second-order kinetic model and the modified Ritchie's-second-order kinetic model. Various thermodynamic parameters, free energy (G0), enthalpy (H0) and entropy (S0), were also calculated and the results showed that the adsorption process strongly depended on temperature of medium.
dc.identifier.citationOsman, B. vd. (2011). "Immobilization of glucoamylase onto lewis metal ion chelated magnetic affinity sorbent: Kinetic, isotherm and thermodynamic studies". Journal of Macromolecular Science, Part A-Pure and Applied Chemistry, 48(5), 387-399.
dc.identifier.endpage399
dc.identifier.issn1060-1325
dc.identifier.issn1520-5738
dc.identifier.issue5
dc.identifier.scopus2-s2.0-79954537873
dc.identifier.startpage387
dc.identifier.urihttps://doi.org/10.1080/10601325.2011.562734
dc.identifier.urihttps://www.tandfonline.com/doi/full/10.1080/10601325.2011.562734
dc.identifier.urihttp://hdl.handle.net/11452/23478
dc.identifier.volume48
dc.identifier.wos000289574800009
dc.indexed.wosSCIE
dc.language.isoen
dc.publisherTaylor & Francis
dc.relation.bapUAP(F)-2008/55
dc.relation.bapUAP(F)-2010/26
dc.relation.journalJournal of Macromolecular Science, Part A-Pure and Applied Chemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectPolymer science
dc.subjectImmobilization
dc.subjectAdsorption isotherms
dc.subjectAdsorption kinetics
dc.subjectGlucoamylase
dc.subjectIMAC
dc.subjectMagnetic support
dc.subjectReversible use
dc.subjectHuman serum
dc.subjectPh value
dc.subjectEnzyme activity
dc.subjectBeads
dc.subjectAdsorption
dc.subjectRemoval
dc.subjectCatalase
dc.subjectCu(II)
dc.subjectBinding
dc.subjectAdsorption isotherms
dc.subjectChelation
dc.subjectDyes
dc.subjectEnzyme activity
dc.subjectEnzyme immobilization
dc.subjectEnzymes
dc.subjectEthylene
dc.subjectEthylene glycol
dc.subjectKinetic theory
dc.subjectMetal ions
dc.subjectpH effects
dc.subjectTemperature
dc.subjectAdsorption kinetics
dc.subjectGlucoamylase
dc.subjectIMAC
dc.subjectImmobilization
dc.subjectMagnetic support
dc.subjectAdsorption
dc.subject.scopusCibacron Blue F 3Ga; Cryogels; Muramidase
dc.subject.wosPolymer science
dc.titleImmobilization of glucoamylase onto lewis metal ion chelated magnetic affinity sorbent: Kinetic, isotherm and thermodynamic studies
dc.typeArticle
dc.wos.quartileQ3
dspace.entity.typePublication
local.contributor.departmentFen Edebiyat Fakültesi/Kimya Ana Bilim Dalı
local.indexed.atScopus
local.indexed.atWOS

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