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dc.creatorKnezevic, Zorica
dc.creatorMilosavić, Nenad
dc.creatorBezbradica, Dejan
dc.creatorJakovljević, Živana
dc.creatorProdanović, Radivoje
dc.date.accessioned2018-11-22T00:09:50Z
dc.date.available2018-11-22T00:09:50Z
dc.date.issued2006
dc.identifier.issn1369-703X
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/787
dc.description.abstractThe present study compares the results of three different covalent immobilization methods employed for immobilization of lipase from Candida rugosa on Eupergit C supports with respect to enzyme loadings, activities and coupling yields. It seems that method yielding the highest activity retention of 43.3% is based on coupling lipase via its carbohydrate moiety previously modified by periodate oxidation. Study of thermal deactivation kinetics at three temperatures (37, 50 and 75 degrees C) revealed that the immobilization method also produces an appreciable stabilization of the biocatalyst, changing its thermal deactivation profile. By comparison of the t(1/2) values obtained at 75 C, it can be concluded that the lipase immobilized via carbohydrate moiety was almost 2-fold more stable than conventionally immobilized one and 18-fold than free lipase. The immobilization procedure developed is quite simple, and easily reproduced, and provides a promising solution for application of lipase in aqueous and microaqueous reaction system. (c) 2006 Elsevier B.V. All rights reserved.en
dc.publisherElsevier Science Sa, Lausanne
dc.rightsrestrictedAccess
dc.sourceBiochemical Engineering Journal
dc.subjectimmobilized enzymesen
dc.subjectCandida rugosa lipaseen
dc.subjectEupergiten
dc.subjectenzyme deactivationen
dc.subjectkinetic parametersen
dc.subjectmicroemulsionsen
dc.titleImmobilization of lipase from Candida rugosa on Eupergit (R) supports by covalent attachmenten
dc.typearticle
dc.rights.licenseARR
dcterms.abstractЈаковљевиц, Зивана; Продановић, Радивоје; Кнезевиц, Зорица; Милосавиц, Ненад; Безбрадица, Дејан;
dc.citation.volume30
dc.citation.issue3
dc.citation.spage269
dc.citation.epage278
dc.identifier.wos000239101800007
dc.identifier.doi10.1016/j.bej.2006.05.009
dc.citation.other30(3): 269-278
dc.citation.rankM21
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-33745267288
dc.identifier.rcubKon_1740


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