α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors

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dc.authoridONAL ACET, Burcu/0000-0003-2408-8660
dc.authoridODABASI, Mehmet/0000-0002-3288-132X
dc.authoridAcet, Omur/0000-0003-1864-5694
dc.authoridDIKICI, EMRAH/0000-0002-3086-8156
dc.contributor.authorAcet, Omur
dc.contributor.authorInanan, Tulden
dc.contributor.authorAcet, Burcu Onal
dc.contributor.authorDikici, Emrah
dc.contributor.authorOdabasi, Mehmet
dc.date.accessioned2025-03-17T12:27:30Z
dc.date.available2025-03-17T12:27:30Z
dc.date.issued2021
dc.departmentTarsus Üniversitesi
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.endpage2496
dc.identifier.issn0273-2289
dc.identifier.issn1559-0291
dc.identifier.issue8
dc.identifier.pmid33779933
dc.identifier.scopus2-s2.0-85103373835
dc.identifier.scopusqualityQ2
dc.identifier.startpage2483
dc.identifier.urihttps://doi.org/10.1007/s12010-021-03559-z
dc.identifier.urihttps://hdl.handle.net/20.500.13099/2294
dc.identifier.volume193
dc.identifier.wosWOS:000634664600001
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
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/openAccess
dc.snmzKA_WOS_20250316
dc.subjectProtein adsorption
dc.subjectIMAC
dc.subjectalpha-Amylase
dc.subjectComposite cryogel
dc.subjectBead embedding
dc.titleα-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors
dc.typeArticle

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