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dc.creatorVelicić, Zorica
dc.creatorRusmirović, Jelena
dc.creatorPrlainović, Nevena
dc.creatorTomić, Nataša
dc.creatorVeličković, Zlate
dc.creatorTaleb, Khaled
dc.creatorMarinković, Aleksandar
dc.date.accessioned2021-03-10T14:20:22Z
dc.date.available2021-03-10T14:20:22Z
dc.date.issued2020
dc.identifier.issn1022-9760
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/4461
dc.description.abstractIn this work, the optimization of synthesis of terpolymer monolith based on glycidyl methacrylate (GMA), ethylene glycol dimethacrylate (EGDMA) and additional cross-linkers: trimethylolpropanetriacrylate (TMPTA) or triethylene glycol dimethacrylate (TEGDMA) was performed. Moreover, novel vinyl functionalized cross-linkable polymers: ethanolamine (EA)/methacryloyl (MAC) modified poly (methyl methacrylate) (PMMA), and hydrolyzed poly (ethylene-co-vinyl acetate) copolymer (EVOH) modified with MAC either directly or via ethyl malonyl chloride/EA bridging group (m-EVA) were used as cross-linkable polymer to improve mechanical/elastic properties of the obtained monoliths. Optimization procedure, performed applying response surface methodology (RSM), was focused on the production of materials with improved dimensional stability/integrity and porosity with abundance of epoxide groups capable for immobilization of lipase from Candida rugosa (CRL). Structural characterization of the synthesized monoliths was determined using FTIR, Raman and H-1 NMR spectroscopies, while morphology/porosity was determined by SEM technique and image analysis; and mechanical properties by diametral compression testing. The most potential monolith containing m-EVA polymeric cross-linker, i.e. GMA/EGDMA/TEGDMA/m-EVA monolith, was used as CRL carrier in a two-step immobilization process. Enzyme loading and the activity of obtained preparations for various initial enzyme concentrations were monitored after 4 and 48 h of immobilization. The resulting catalysts show high potency in biocatalytic reactions with the highest percentage of retained initial lipase activity of 64.5%.en
dc.publisherSpringer, Dordrecht
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200135/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200325/RS//
dc.rightsrestrictedAccess
dc.sourceJournal of Polymer Research
dc.subjectMacroporous copolymersen
dc.subjectresponse surface methodology (RSM)en
dc.subjectCandida rugosa lipaseen
dc.subjectEnzyme immobilizationen
dc.subjectCompression testingen
dc.titleThe optimization of glycidyl methacrylate based terpolymer monolith synthesis: an effective Candida rugosa lipase immobilization supporten
dc.typearticle
dc.rights.licenseARR
dc.citation.issue5
dc.citation.other27(5): -
dc.citation.rankM22~
dc.citation.volume27
dc.identifier.doi10.1007/s10965-020-02127-z
dc.identifier.rcubconv_6108
dc.identifier.scopus2-s2.0-85084144196
dc.identifier.wos000531408400004
dc.type.versionpublishedVersion


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