Alpha-Amylase immobilized composite cryogels: some studies on kinetic and adsorption factors

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dc.contributor.authorAcet, Ömür
dc.contributor.authorİnanan, Tülden
dc.contributor.authorAcet, Burcu Önal
dc.contributor.authorDikici, Emrah
dc.contributor.authorOdabaşı, Mehmet
dc.date.accessioned2021-05-04T07:07:14Z
dc.date.available2021-05-04T07:07:14Z
dc.date.issued2021
dc.departmentTeknik Bilimler Meslek Yüksekokulu
dc.description*İnanan, Tülden ( Aksaray, Yazar )
dc.description.abstractStability of enzymes is a significant factor for their industrial feasibility. alpha-Amylase is an important enzyme for some industries, i.e., textile, food, paper, and pharmaceutics. Pumice particles (PPa) are non-toxic, natural, and low-cost alternative adsorbents with high adsorption capacity. In this study, Cu2+ ions were attached to pumice particles (Cu2+-APPa). Then, Cu2+-APPa embedded composite cryogel was synthesized (Cu2+-APPaC) via polymerization of gel-forming agents at minus temperatures. Characterization studies of the Cu2+-APPaC cryogel column were performed by X-ray fluorescence spectrometry (XRF), scanning electron microscopy (SEM), and Brunauer, Emmett, Teller (BET) method. The experiments were carried out in a continuous column system. alpha-Amylase was adsorbed onto Cu2+-APPaC cryogel with maximum amount of 858.7 mg/g particles at pH 4.0. Effects of pH and temperature on the activity profiles of the free and the immobilized alpha-amylase were investigated, and results indicate that immobilization did not alter the optimum pH and temperature values. k(cat) value of the immobilized alpha-amylase is higher than that of the free alpha-amylase while K-M value increases by immobilization. Storage and operational stabilities of the free and the immobilized alpha-amylase were determined for 35 days and for 20 runs, respectively.
dc.identifier.doi10.1007/s12010-021-03559-z
dc.identifier.endpage-en_US
dc.identifier.issue-en_US
dc.identifier.pmid33779933
dc.identifier.startpage-en_US
dc.identifier.urihttps:/dx.doi.org/ 10.1007/s12010-021-03559-z
dc.identifier.urihttps://hdl.handle.net/20.500.12451/7935
dc.identifier.volume-en_US
dc.identifier.wosWOS:000634664600001
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.language.isoen
dc.publisherSpringer
dc.relation.ispartofApplied Biochemistry and Biotechnology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectProtein Adsorption
dc.subjectIMAC
dc.subjectAlpha-Amylase
dc.subjectComposite Cryogel
dc.subjectBead Embedding
dc.titleAlpha-Amylase immobilized composite cryogels: some studies on kinetic and adsorption factors
dc.typeArticle

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