Приказ основних података о документу

dc.creatorMihailović, Mladen
dc.creatorStojanović, Marija
dc.creatorBanjanac, Katarina
dc.creatorCarević, Milica
dc.creatorPrlainović, Nevena
dc.creatorMilosavić, Nenad
dc.creatorBezbradica, Dejan
dc.date.accessioned2021-03-10T12:36:18Z
dc.date.available2021-03-10T12:36:18Z
dc.date.issued2014
dc.identifier.issn1359-5113
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/2853
dc.description.abstractIn this study, Purolite (R) A109, polystyrenic macroporous resin, was used as immobilization support due to its good mechanical properties and high particle diameter (400 mu m), which enables efficient application in enzyme reactors due to lower pressure drops. The surface of support had been modified with epichlorhydrine and was tested in lipase immobilization. Optimized procedure for support modification proved to be more efficient than conventional procedure for hydroxy groups (at 22 degrees C for 18 h), since duration of procedure was shortened to 40 min by performing modification at 52 degrees C resulting with almost doubled concentration of epoxy groups (563 mu mol g(-1)). Lipase immobilized on epoxy-modified support showed significantly improved thermal stability comparing to both, free form and commercial immobilized preparation (Novozym (R) 435). The highest activity (47.5 IU g(-1)) and thermal stability (2.5 times higher half-life than at low ionic strength) were obtained with lipase immobilized in high ionic strength. Thermal stability of immobilized lipase was further improved by blocking unreacted epoxy groups on supports surface with amino acids. The most efficient was treatment with phenylalanine, since in such a way blocked immobilized enzyme retained 65% of initial activity after 8 h incubation at 65 degrees C, while non-blocked derivative retained 12%.en
dc.publisherElsevier Sci Ltd, Oxford
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172013/RS//
dc.rightsrestrictedAccess
dc.sourceProcess Biochemistry
dc.subjectLipaseen
dc.subjectPurolite((R)) A109en
dc.subjectCandida antarcticaen
dc.subjectImmobilizationen
dc.subjectAmino acidsen
dc.titleImmobilization of lipase on epoxy-activated Purolite((R)) A109 and its post-immobilization stabilizationen
dc.typearticle
dc.rights.licenseARR
dc.citation.epage646
dc.citation.issue4
dc.citation.other49(4): 637-646
dc.citation.rankM21
dc.citation.spage637
dc.citation.volume49
dc.identifier.doi10.1016/j.procbio.2014.01.013
dc.identifier.scopus2-s2.0-84897913807
dc.identifier.wos000335281800014
dc.type.versionpublishedVersion


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Приказ основних података о документу