Immobilized metal ion affinity nanospheres for ?-amylase immobilization

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dc.authoridAkgol, Sinan -- 0000-0002-8528-1854; Tuzmen, Nalan -- 0000-0001-9863-7023; AKGOL, Sinan -- 0000-0003-2836-7181
dc.contributor.authorKalburcu, Tülden
dc.contributor.authorTüzmen, Münire Nalan
dc.contributor.authorAkgöl, Sinan
dc.contributor.authorDenizli, Adil
dc.date.accessioned13.07.201910:50:10
dc.date.accessioned2019-07-16T09:15:00Z
dc.date.available13.07.201910:50:10
dc.date.available2019-07-16T09:15:00Z
dc.date.issued2014
dc.departmentSabire Yazıcı Fen Edebiyat Fakültesi
dc.description.abstractImmobilized metal chelate affinity chromatography (IMAC) support was practiced for alpha-amylase immobilization. Poly(hydroxyethylmethacrylate-methacryloylamidotryptophan)-Ni2+ [p(HEMA-MAT)-Ni2+] nanospheres, average diameter 100 nm, were produced by surfactant free emulsion polymerization. Characterizations of p(HEMA-MAT)-Ni2+ nanospheres were carried out by Fourier transform infrared (FTIR) spectroscopy and scanning electron microscope (SEM). In addition, average particle size, size distribution, and surface charge were specified. The amount of N-methacryloylamidotryptophan (MAT) incorporated to polymer was determined as 1.95 mmol/g polymers by using nitrogen stoichiometry. The specific surface areas of poly(hydroxyethylmethacrylate) [p(HEMA)] and p(HEMA-MAT) nanospheres were calculated as 1856 m(2)/g and 1914 m(2)/g, respectively. Protein adsorption increased with increasing initial protein concentration and maximum alpha-amylase adsorption on p(HEMA-MAT)-Ni2+ nanospheres was observed at pH 4.0. Both free and immobilized alpha-amylase showed pH optimum at pH 7.0. It was determined that the immobilized alpha-amylase had better thermostability than the free one. Immobilization of the enzyme did not significantly change the kinetic parameters. The storage stability of alpha-amylase increased upon immobilization. It was also observed that p(HEMA-MAT)-Ni2+ nanospheres can be repeatedly used for alpha-amylase immobilization.
dc.identifier.doi10.3906/kim-1301-87
dc.identifier.endpage40en_US
dc.identifier.issn1300-0527
dc.identifier.issue1en_US
dc.identifier.scopusqualityQ3
dc.identifier.startpage28en_US
dc.identifier.urihttps://doi.org/10.3906/kim-1301-87
dc.identifier.urihttps://hdl.handle.net/20.500.12451/4251
dc.identifier.volume38en_US
dc.identifier.wosWOS:000329090500002
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakTR-Dizin
dc.language.isoen
dc.publisherScientific Technical Research Council Turkey-Tubitak
dc.relation.ispartofTurkish Journal of Chemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectAlpha-Amylase
dc.subjectNanospheres
dc.subjectIMAC
dc.subjectEnzyme Immobilization
dc.subjectAdsorption
dc.titleImmobilized metal ion affinity nanospheres for ?-amylase immobilization
dc.typeArticle

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