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Imobilizacija enzima na ugljenične nanocevi

dc.creatorPrlainović, Nevena
dc.creatorBezbradica, Dejan
dc.creatorKnežević-Jugović, Zorica
dc.creatorMarinković, Aleksandar
dc.creatorUskoković, Petar
dc.creatorMijin, Dušan
dc.date.accessioned2021-03-10T11:30:13Z
dc.date.available2021-03-10T11:30:13Z
dc.date.issued2011
dc.identifier.issn0367-598X
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/1811
dc.description.abstractThe discovery of carbon nanotubes (CNTs) has opened a new door in nanotechnology. With their high surface area, unique electronic, thermal and mechanical properties, CNTs have been widely used as carriers for protein immobilization. In fact, carbon nanotubes present an ideal support system without diffusional limitations, and also have the possibility of surface covalent functionalization. It is usually the oxidation process that introduces carboxylic acid groups. Enzymes and other proteins could be adsorbed or covalently attached onto carbon nanotubes. Adsorption of enzyme is a very simple and inexpensive immobilization method and there are no chemical changes of the protein. It has also been found that this technique does not alter structure and unique properties of nanotubes. However, a major problem in process designing is the relatively low stability of immobilized protein and desorption from the carrier. On the other hand, while covalent immobilization provides durable attachment, the oxidation process can reduce mechanical and electronic properties of carbon nanotubes. It can also affect the active site of enzyme and cause the loss of enzyme activity. Bioimmobilization studies have showed that there are strong interactions between carbon nanotubes surface and protein. The retention of enzyme structure and activity is critical for their application and it is of fundamental interest to understand the nature of these interactions. Atomic force microscopy (AFM), transmission electron microscopy (TEM), scanning electron microscopy (SEM) and circular dichroism (CD) spectroscopy provide an insight into the structural changes that occur during the immobilization. The aim of this paper is to summarize progress of protein immobilization onto carbon nanotubes.en
dc.description.abstractNanocevi poseduju veliki potencijal primene u raznim oblastima nauke i inženjerstva. Velika mehanička čvrstoća, odlična termička i električna provodljivost, veliki odnos površine prema zapremini i minimalna difuziona ograničenja čine ih idealnim nosačima za imobilizaciju biomolekula kao što su proteini, antigeni, antitela, vitamini, hormoni, antibiotici i dr. U ovom radu opisane su tehnika adsorpcije i kovalentnog vezivanja enzima na nemodifikovane, oksidovane i amino funkcionalizovane ugljenične nanocevi. Takođe je opisan uticaj površine ugljeničnih nanocevi na strukturne promene enzima, kao i na promene u pogledu aktivnosti i stabilnosti.sr
dc.publisherAssociation of Chemical Engineers of Serbia
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172013/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/45019/RS//
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceHemijska industrija
dc.subjectcarbon nanotubesen
dc.subjectenzymeimmobilizationen
dc.subjectadsorptionen
dc.subjectcovalent attachmenten
dc.subjectugljenične nanocevisr
dc.subjectimobilizacija enzimasr
dc.subjectadsorpcijasr
dc.subjectkovalentno vezivanjesr
dc.titleImmobilization of enzymes onto carbon nanotubesen
dc.titleImobilizacija enzima na ugljenične nanocevisr
dc.typearticle
dc.rights.licenseBY-NC-ND
dc.citation.epage430
dc.citation.issue4
dc.citation.other65(4): 423-430
dc.citation.rankM23
dc.citation.spage423
dc.citation.volume65
dc.identifier.doi10.2298/HEMIND110330028P
dc.identifier.fulltexthttp://TechnoRep.tmf.bg.ac.rs/bitstream/id/8669/0367-598X1104423P.pdf
dc.identifier.rcubconv_1323
dc.identifier.scopus2-s2.0-80052627832
dc.identifier.wos000297887000010
dc.type.versionpublishedVersion


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