Immobilization of Aspergillus oryzae ?-Galactosidase onto Duolite A568 Resin via Simple Adsorption Mechanism

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dc.authoridMutlu, Mehmet/0000-0001-7146-1937
dc.authoridMUTLU, MEHMET/0000-0001-9610-9817
dc.authorwosidMutlu, Mehmet/S-5351-2019
dc.authorwosidMUTLU, MEHMET/B-3240-2013
dc.contributor.authorGurdas, Sevim
dc.contributor.authorGulec, Haci Ali
dc.contributor.authorMutlu, Mehmet
dc.date.accessioned2024-06-12T10:54:25Z
dc.date.available2024-06-12T10:54:25Z
dc.date.issued2012
dc.departmentTrakya Üniversitesien_US
dc.description.abstractIn this study, a rapid, simple and economic method of enzyme immobilization was developed to hydrolyze lactose. Duolite A568 resin was used for the immobilization of beta-galactosidase via simple adsorption mechanism. The effects of immobilization parameters such as time, pH, and temperature were studied. Immobilization parameters for maximum enzyme activity were estimated at 35 A degrees C temperature, pH 4.5, 5 mg/mL enzyme concentration, and approximately 60 min immobilization time. A significant amount of enzyme was immobilized with high catalytic activity. Enzyme immobilization procedure explained in this study slightly affected the enzyme kinetic. The value of Michaelis constant K (m) for immobilized enzyme was significantly larger, indicating decreased affinity by the enzyme for its substrate. It was observed that both free and immobilized enzyme showed maximum activity at 65 A degrees C reaction temperature. Immobilized beta-galactosidase was significantly more active at all temperatures as compared to its free form. However, optimal pH of immobilized enzyme was slightly affected by immobilization procedure. The optimum pH of immobilized enzyme was shifted up 0.5 unit to a more alkaline value of 6.0 compared to the free enzyme.en_US
dc.description.sponsorshipCumhuriyet University (CUBAP) [M-343]en_US
dc.description.sponsorshipThis study was supported by The Fund of Scientific Research Projects of Cumhuriyet University (CUBAP; project no. M-343).en_US
dc.identifier.doi10.1007/s11947-010-0384-7
dc.identifier.endpage911en_US
dc.identifier.issn1935-5130
dc.identifier.issue3en_US
dc.identifier.scopus2-s2.0-84858001031en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage904en_US
dc.identifier.urihttps://doi.org/10.1007/s11947-010-0384-7
dc.identifier.urihttps://hdl.handle.net/20.500.14551/19045
dc.identifier.volume5en_US
dc.identifier.wosWOS:000301442700008en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofFood And Bioprocess Technologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBeta-Galactosidaseen_US
dc.subjectImmobilized Enzymeen_US
dc.subjectDuolite A568en_US
dc.subjectActivation Energyen_US
dc.subjectLactose Hydrolysisen_US
dc.subjectKluyveromyces-Fragilisen_US
dc.subjectPart 1en_US
dc.subjectGlutaraldehydeen_US
dc.subjectSupporten_US
dc.subjectReactoren_US
dc.subjectSurfaceen_US
dc.subjectBeadsen_US
dc.subjectBatchen_US
dc.subjectLactaseen_US
dc.titleImmobilization of Aspergillus oryzae ?-Galactosidase onto Duolite A568 Resin via Simple Adsorption Mechanismen_US
dc.typeArticleen_US

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