dc.creator | Žuža, Milena | |
dc.creator | Šiler-Marinković, Slavica | |
dc.creator | Knežević, Zorica | |
dc.date.accessioned | 2021-03-10T10:50:00Z | |
dc.date.available | 2021-03-10T10:50:00Z | |
dc.date.issued | 2007 | |
dc.identifier.issn | 0352-6542 | |
dc.identifier.uri | http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1195 | |
dc.description.abstract | This 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.publisher | Univerzitet u Nišu - Tehnološki fakultet, Leskovac | |
dc.rights | openAccess | |
dc.source | Zbornik radova Tehnološkog fakulteta, Leskovac | |
dc.title | Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier | en |
dc.type | article | |
dc.rights.license | ARR | |
dc.citation.epage | 42 | |
dc.citation.issue | 16 | |
dc.citation.other | (16): 33-42 | |
dc.citation.spage | 33 | |
dc.identifier.rcub | https://hdl.handle.net/21.15107/rcub_technorep_1195 | |
dc.type.version | publishedVersion | |