Immobilization of a thermostable α-amylase onto reactive membranes: kinetics characterization and application to continuous starch hydrolysis

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dc.contributor.authorBayramoğlu, G.
dc.contributor.authorYilmaz, M.
dc.contributor.authorArica, M.Y.
dc.date.accessioned2020-06-25T17:40:09Z
dc.date.available2020-06-25T17:40:09Z
dc.date.issued2004
dc.departmentKırıkkale Üniversitesi
dc.description.abstractEpoxy groups containing porous membranes were prepared by UV-initiated photopolymerisation of hydroxyethylmethacrylate (HEMA) and glycidyl methacrylate (GMA). Epoxy supports could provide multipoint covalent attachment of enzymes, therefore, to stabilize their three-dimensional structure. alpha-Amylase was immobilized onto the poly(HEMA-GMA-1-3) membranes by means of the amide linkage formation between the amino groups of alpha-amylase and the epoxy groups of the support. The alpha-amylase immobilization capacity of the membranes was increased as the GMA ratio increased in the membrane structure. The retained activity of the immobilized alpha-amylase was 76% with poly(HEMA-GMA-2) membrane. The decrease in activity of the immobilized a-amylase could be considered to be due to reduced conformational flexibility of the immobilized alpha-amylase molecules for binding its large substrate, starch, as a result of the covalent immobilization. The immobilized alpha-amylase has more resistance to temperature inactivation than that of the free form. The optimum pH value of alpha-amylase was not affected by the immobilization reaction, but the pH profile was broadened for the immobilized enzyme. Kinetic parameters were determined for immobilized alpha-amylase as well as for the free enzyme. The values of the Michaelis constant K-m of alpha-amylase, were significantly larger (ca. 2.3 times) upon immobilization, indicating decreased affinity of the enzyme for its substrate, whereas V-max was smaller for immobilized a-amylase. In a 120 h continuous operation at 35 degreesC only 4% of immobilized alpha-amylase activity was lost. The operational inactivation rate constant (k(opi)) of the immobilized a-amylase with 2% starch was 8.06x 10(-6) min(-1). (C) 2003 Elsevier Ltd. All rights reserved.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1016/S0308-8146(03)00283-8
dc.identifier.endpage599en_US
dc.identifier.issn0308-8146
dc.identifier.issn1873-7072
dc.identifier.issue4en_US
dc.identifier.scopus2-s2.0-0242594589
dc.identifier.scopusqualityQ1
dc.identifier.startpage591en_US
dc.identifier.urihttps://doi.org/10.1016/S0308-8146(03)00283-8
dc.identifier.urihttps://hdl.handle.net/20.500.12587/3317
dc.identifier.volume84en_US
dc.identifier.wosWOS:000186886100014
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevier Sci Ltden_US
dc.relation.ispartofFood Chemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectpolymer membraneen_US
dc.subjectalpha-amylaseen_US
dc.subjectimmobilizationen_US
dc.subjectstarch hydrolysisen_US
dc.subjectenzyme kineticsen_US
dc.subjectenzyme reactoren_US
dc.titleImmobilization of a thermostable α-amylase onto reactive membranes: kinetics characterization and application to continuous starch hydrolysisen_US
dc.typeArticle

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