Covalent immobilisation of invertase onto a reactive film composed of 2-hydroxyethyl methacrylate and glycidyl methacrylate: properties and application in a continuous flow system

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dc.contributor.authorBayramoglu, G
dc.contributor.authorAkgol, S
dc.contributor.authorBulut, A
dc.contributor.authorDenizli, A
dc.contributor.authorArica, MY
dc.date.accessioned2020-06-25T17:35:30Z
dc.date.available2020-06-25T17:35:30Z
dc.date.issued2003
dc.departmentKırıkkale Üniversitesi
dc.descriptionAkgol, Sinan/0000-0002-8528-1854; AKGOL, Sinan/0000-0003-2836-7181
dc.description.abstractInvertase was covalently immobilised on the poly(hydroxyethyl methacrylate-co-glycidyl methacrylate) (poly(HEMA-GMA)) film. The invertase immobilisation capacity of the films was increased as the GMA ratio increased in the film structure. The immobilised invertase on the poly(HEMA-GMA-3) composition exhibited an activity of 32.7 U cm(-2) film. The optimum temperature of the immobilised invertase increased by 5 degreesC, and the optimal pH values for the free and the immobilised enzymes were determined as 5.0. The retained activity of the immobilised invertase was between 53 and 85%. Kinetic parameters were determined for immobilised invertase as well as for the free enzyme. The values of the Michael's constant K-m of invertase were significantly larger, ca. 2.7 times upon immobilisation, indicating decreased affinity by the enzyme for its substrate, whereas V-max was smaller for immobilised invertase. Activity of the immobilised invertase was quite stable with respect to free counterpart. After 168 h reaction, only 8% of immobilised invertase activity was lost. The operational inactivation rate constant (k(opi)) of the immobilised invertase at 35 degreesC with 200 mM sucrose was 8.23 x 10(-6) min(-1). (C) 2002 Elsevier Science B.V. All rights reserved.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1016/S1369-703X(02)00170-5
dc.identifier.endpage126en_US
dc.identifier.issn1369-703X
dc.identifier.issue2en_US
dc.identifier.scopus2-s2.0-0345352783
dc.identifier.scopusqualityQ2
dc.identifier.startpage117en_US
dc.identifier.urihttps://doi.org/10.1016/S1369-703X(02)00170-5
dc.identifier.urihttps://hdl.handle.net/20.500.12587/3134
dc.identifier.volume14en_US
dc.identifier.wosWOS:000182361900006
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevier Science Saen_US
dc.relation.ispartofBiochemical Engineering Journal
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectimmobilisationen_US
dc.subjectimmobilised enzymesen_US
dc.subjectinvertaseen_US
dc.subjectsucrose hydrolysisen_US
dc.subjectkinetic parametersen_US
dc.subjectenzyme bioreactorsen_US
dc.subjectfilmen_US
dc.titleCovalent immobilisation of invertase onto a reactive film composed of 2-hydroxyethyl methacrylate and glycidyl methacrylate: properties and application in a continuous flow systemen_US
dc.typeArticle

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