Please use this identifier to cite or link to this item: https://scidar.kg.ac.rs/handle/123456789/19849
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dc.contributor.authorMiletic, Nemanja-
dc.contributor.authorAbetz, Volker-
dc.contributor.authorEbert, Katrin-
dc.contributor.authorLoos, Katja-
dc.date.accessioned2024-01-11T12:35:54Z-
dc.date.available2024-01-11T12:35:54Z-
dc.date.issued2010-
dc.identifier.citationMiletić, N., Ebert, K., Abetz, V., Loos, K. (2010): Immobilization of Candida antarctica lipase B on polystyrene nanoparticles. Macromolecular Rapid Communications, 31(1), 71-74.en_US
dc.identifier.issn1022-1336en_US
dc.identifier.urihttps://scidar.kg.ac.rs/handle/123456789/19849-
dc.description.abstractPolystyrene (PS) nanoparticles were prepared via a nanoprecipitation process. The influence of the pH of the buffer solution used during the immobilization process on the loading of Candida antarctica lipase B (Cal-B) and on the hydrolytic activity (hydrolysis of p-nitrophenyl acetate) of the immobilized Cal-B was studied. The pH of the buffer solution has no influence on enzyme loading, while immobilized enzyme activity is very dependent on the pH of adsorption. Cal-B immobilized on PS nanoparticles in buffer solution pH 6.8 performed higher hydrolytic activity than crude enzyme powder and Novozyme 435.en_US
dc.language.isoenen_US
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.sourceMacromolecular rapid communications-
dc.subjectCandida antarctica lipase Ben_US
dc.subjectEnzymesen_US
dc.subjectNanoparticlesen_US
dc.subjectPolystyreneen_US
dc.titleImmobilization of Candida antarctica lipase B on Polystyrene Nanoparticlesen_US
dc.typearticleen_US
dc.description.versionPublisheden_US
dc.identifier.doi10.1002/marc.200900497en_US
dc.type.versionPublishedVersionen_US
dc.identifier.wos000273624100007en_US
Appears in Collections:Faculty of Agronomy, Čačak

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