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dc.contributor.authorDanisman, T
dc.contributor.authorTan, S
dc.contributor.authorKacar, Y
dc.contributor.authorErgene, A
dc.date.accessioned2020-06-25T17:40:08Z
dc.date.available2020-06-25T17:40:08Z
dc.date.issued2004
dc.identifier.citationclosedAccessen_US
dc.identifier.issn0308-8146
dc.identifier.urihttps://doi.org/10.1016/j.foodchem.2003.07.015
dc.identifier.urihttps://hdl.handle.net/20.500.12587/3300
dc.descriptionKacar, Yasemin/0000-0002-8682-9228en_US
dc.descriptionWOS: 000188543800018en_US
dc.description.abstractPoly (2-hydroxyethyl methacrylate-glycidyl methacrylate) (pHEMA-GMA) membrane was prepared by UV-initiated photopolymerization. Invertase was immobilized by the condensation reaction of the epoxy groups of glycidyl methacrylate in the membrane structure with amino groups of the enzyme. The (Km) values were 22 mM and 58 mM for free and immobilized enzyme, respectively. Immobilization improved the pH stability and temperature stability of the enzyme. Thermal stability was found to increase with immobilization. The half times for the activity decay at 70 degreesC were found to be 11 and 38 min for the free and immobilized enzyme, respectively. The immobilized enzyme activity was found to be quite stable in later experiments. (C) 2003 Elsevier Ltd. All rights reserved.en_US
dc.language.isoengen_US
dc.publisherElsevier Sci Ltden_US
dc.relation.isversionof10.1016/j.foodchem.2003.07.015en_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectpHEMA-GMA membraneen_US
dc.subjectepoxy groupsen_US
dc.subjectcovalent bondingen_US
dc.subjectenzyme immobilizationen_US
dc.subjectinvertaseen_US
dc.titleCovalent immobilization of invertase on microporous pHEMA-GMA membraneen_US
dc.typearticleen_US
dc.contributor.departmentKırıkkale Üniversitesien_US
dc.identifier.volume85en_US
dc.identifier.issue3en_US
dc.identifier.startpage461en_US
dc.identifier.endpage466en_US
dc.relation.journalFood Chemistryen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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