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dc.creatorBezbradica, Dejan
dc.creatorJugović, Branimir
dc.creatorGvozdenović, Milica
dc.creatorJakovetić, Sonja
dc.creatorKnežević-Jugović, Zorica
dc.date.accessioned2021-03-10T11:39:13Z
dc.date.available2021-03-10T11:39:13Z
dc.date.issued2011
dc.identifier.issn1381-1177
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/1952
dc.description.abstractElectrochemical synthesis of polyaniline support for enzyme immobilization provides easier control over the properties of obtained polymer and reduced risk of biocatalyst inactivation with residues of toxic compounds. In the present study, immobilization of lipase from Candida rugosa on electrochemically synthesized PANI (activated with glutaraldehyde) resulted with high lipase loadings up to 93.7 mg of proteins per gram of dry support. The activation of support and immobilization were optimized, with respect to activity yield. The optimum concentration of glutaraldehyde was 2% (w/v) and optimum concentration of enzyme was 4 mg ml(-1). Modification of enzyme surface with carbodiimide and ethylenediamine was performed in order to increase concentration of amino groups. Aminated lipase exhibited higher specific activity (52%) and thermal stability (3 times) after immobilization, compared with non-modified lipase. Also, reusability of immobilized enzyme was significantly increased with amination, especially if immobilization was performed at pH 10, so in such a way obtained derivative retained 91% of activity after 15 reaction cycles.en
dc.publisherElsevier Science Bv, Amsterdam
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
dc.rightsrestrictedAccess
dc.sourceJournal of Molecular Catalysis B-Enzymatic
dc.subjectLipaseen
dc.subjectAminationen
dc.subjectPolyanilineen
dc.subjectElectrochemical synthesisen
dc.subjectGalvanostatic techniqueen
dc.titleElectrochemically synthesized polyaniline as support for lipase immobilizationen
dc.typearticle
dc.rights.licenseARR
dc.citation.epage60
dc.citation.issue1-2
dc.citation.other70(1-2): 55-60
dc.citation.rankM22
dc.citation.spage55
dc.citation.volume70
dc.identifier.doi10.1016/j.molcatb.2011.02.004
dc.identifier.rcubconv_3566
dc.identifier.scopus2-s2.0-79952816284
dc.identifier.wos000289453100008
dc.type.versionpublishedVersion


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