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dc.creatorŽuža, Milena
dc.creatorŠiler-Marinković, Slavica
dc.creatorKnežević, Zorica
dc.date.accessioned2021-03-10T10:50:00Z
dc.date.available2021-03-10T10:50:00Z
dc.date.issued2007
dc.identifier.issn0352-6542
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/1195
dc.description.abstractThis paper reports the covalent immobilization of penicillin G acylase from E. coli on sepabeads EC-EP, an epoxy-activated polymethacrylic carrier, and describes kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillin and semi-synthetic b-lactam antibiotics synthesis reactions. It appears that both free and immobilized penicillin acylase followed simple Michaelis-Menten kinetics, implying the same reaction mechanism in both systems. .en
dc.publisherUniverzitet u Nišu - Tehnološki fakultet, Leskovac
dc.rightsopenAccess
dc.sourceZbornik radova Tehnološkog fakulteta, Leskovac
dc.titleImmobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrieren
dc.typearticle
dc.rights.licenseARR
dc.citation.epage42
dc.citation.issue16
dc.citation.other(16): 33-42
dc.citation.spage33
dc.identifier.rcubhttps://hdl.handle.net/21.15107/rcub_technorep_1195
dc.type.versionpublishedVersion


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