Приказ основних података о документу

dc.creatorMiljković, Miona
dc.creatorLazić, Vesna M.
dc.creatorBanjanac, Katarina
dc.creatorDavidović, Slađana
dc.creatorBezbradica, Dejan
dc.creatorMarinković, Aleksandar
dc.creatorSredojević, Dušan
dc.creatorNedeljković, Jovan
dc.creatorDimitrijević-Branković, Suzana
dc.date.accessioned2021-03-10T13:51:42Z
dc.date.available2021-03-10T13:51:42Z
dc.date.issued2018
dc.identifier.issn0141-8130
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/4014
dc.description.abstractThe TiO2 based hybrid supports with different functional groups (amino, glutaraldehyde or epoxy) were prepared and their influence on immobilization of dextransucrase (DS) was studied. Novel synthetic route for surface modification of TiO2 with amino and glutaraldehyde groups was developed taking advantage of charge transfer complex (CTC) formation between surface Ti atoms and salicylate-type of ligand (5 aminosalicylic acid (5-ASA)). The proposed coordination of 5-ASA to the surface of TiO2 powder and optical properties of CTC was presented. The pristine TiO2 and amino functionalized TiO2 have higher sorption capacity for DS (12.6 and 12.0 mg g(-1), respectively) compared to glutaraldehyde and epoxy activated supports (9.6 and 9.8 mg g(-1) respectively). However, immobilized enzyme to either glutaraldehyde or epoxy functionalized TiO2 have almost two times higher expressed activities compared to pristine TiO2 support (258, 235 and 142 IU g(-1), respectively). Thermal stability of enzyme immobilized on glutaraldehyde and epoxy functionalized supports was studied at 40 degrees C, as well as operational stability under long-run working conditions in repeated cycles. After five cycles, DS imobilized on glutaraldehyde activated support retained almost 70% of its initial expressed activity, while, after five cycles, performance of DS immobilized on epoxy activated support was significantly lower (15%).en
dc.publisherElsevier Science Bv, Amsterdam
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/45020/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Technological Development (TD or TR)/31035/RS//
dc.rightsrestrictedAccess
dc.sourceInternational Journal of Biological Macromolecules
dc.subjectSurface functionalization of TiO2en
dc.subjectDextransucraseen
dc.subjectEnzyme immobilizationen
dc.titleImmobilization of dextransucrase on functionalized TiO2 supportsen
dc.typearticle
dc.rights.licenseARR
dc.citation.epage1223
dc.citation.other114: 1216-1223
dc.citation.rankaM21
dc.citation.spage1216
dc.citation.volume114
dc.identifier.doi10.1016/j.ijbiomac.2018.04.027
dc.identifier.pmid29634963
dc.identifier.scopus2-s2.0-85045236109
dc.identifier.wos000435056900140
dc.type.versionpublishedVersion


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Приказ основних података о документу