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dc.creatorProdanović, Olivera
dc.creatorProkopijević, Miloš
dc.creatorSpasojević, Dragica
dc.creatorStojanović, Željko
dc.creatorRadotić, Ksenija
dc.creatorKnezevic-Jugovic, Zorica D.
dc.creatorProdanović, Radivoje
dc.date.accessioned2018-11-22T00:22:18Z
dc.date.available2018-11-22T00:22:18Z
dc.date.issued2012
dc.identifier.issn0273-2289
dc.identifier.urihttps://cherry.chem.bg.ac.rs/handle/123456789/1552
dc.description.abstractA macroporous copolymer of glycidyl methacrylate and ethylene glycol dimethacrylate, poly(GMA-co-EGDMA), with various surface characteristics and mean pore size diameters ranging from 44 to 200 nm was synthesized, modified with 1,2-diaminoethane, and tested as a carrier for immobilization of horseradish peroxidase (HRP) by two covalent methods, glutaraldehyde and periodate. The highest specific activity of around 35 U g(-1) dry weight of carrier was achieved on poly(GMA-co-EGDMA) copolymers with mean pore diameters of 200 and 120 nm by the periodate method. A study of deactivation kinetics at 65 A degrees C and in 80 % dioxane revealed that periodate immobilization also produced an appreciable stabilization of the biocatalyst, while stabilization factor depended strongly on the surface characteristics of the copolymers. HRP immobilized on copolymer with a mean pore diameter of 120 nm by periodate method showing not only the highest specific activity but also good stability was further characterized. It appeared that the immobilization resulted in the stabilization of enzyme over a broader pH range while the Michaelis constant value (K (m)) of the immobilized HRP was 10.8 mM, approximately 5.6 times higher than that of the free enzyme. After 6 cycles of repeated use in a batch reactor for pyrogallol oxidation, the immobilized HRP retained 45 % of its original activity.en
dc.publisherHumana Press Inc, Totowa
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/173017/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172049/RS//
dc.rightsrestrictedAccess
dc.sourceApplied Biochemistry and Biotechnology
dc.subjectMacroporous polymersen
dc.subjectCopolymerizationen
dc.subjectEnzymesen
dc.subjectHorseradish peroxidaseen
dc.subjectCovalent immobilizationen
dc.subjectMorphologyen
dc.subjectBiological applications of polymersen
dc.titleImproved Covalent Immobilization of Horseradish Peroxidase on Macroporous Glycidyl Methacrylate-Based Copolymersen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractПродановић, Радивоје; Кнезевиц-Југовиц, Зорица Д.; Продановиц, Оливера; Радотиц, Ксенија; Спасојевиц, Драгица; Стојановиц, Зељко; Прокопијевиц, Милос;
dc.citation.volume168
dc.citation.issue5
dc.citation.spage1288
dc.citation.epage1301
dc.identifier.wos000311310300026
dc.identifier.doi10.1007/s12010-012-9857-7
dc.citation.other168(5): 1288-1301
dc.citation.rankM23
dc.identifier.pmid22941271
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-84871904972


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