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dc.creatorProkopijević, Miloš
dc.creatorProdanović, Olivera
dc.creatorSpasojević, Dragica
dc.creatorStojanović, Željko
dc.creatorRadotić, Ksenija
dc.creatorProdanović, Radivoje
dc.date.accessioned2018-11-22T00:27:48Z
dc.date.available2018-11-22T00:27:48Z
dc.date.issued2014
dc.identifier.issn1615-7591
dc.identifier.urihttps://cherry.chem.bg.ac.rs/handle/123456789/1768
dc.description.abstractSoybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K (m) value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents.en
dc.publisherSpringer, New York
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.sourceBioprocess and Biosystems Engineering
dc.subjectPeriodateen
dc.subjectGlutaraldehydeen
dc.subjectImmobilized enzymeen
dc.subjectStabilityen
dc.subjectCopolymeren
dc.titleSoybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristicsen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractПрокопијевиц, Милос; Стојановиц, Зељко; Радотиц, Ксенија; Спасојевиц, Драгица; Продановиц, Оливера; Продановић, Радивоје;
dc.citation.volume37
dc.citation.issue5
dc.citation.spage799
dc.citation.epage804
dc.identifier.wos000334932300005
dc.identifier.doi10.1007/s00449-013-1050-z
dc.citation.other37(5): 799-804
dc.citation.rankM22
dc.identifier.pmid24061564
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-84905649784
dc.identifier.rcubKon_2651


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