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dc.contributor.authorGuedidi, Sadika
dc.contributor.authorYürekli, Yılmaz
dc.contributor.authorDeratani, André
dc.contributor.authorDéjardin, Philippe
dc.contributor.authorInnocent, Christophe
dc.contributor.authorAltınkaya, Sacide
dc.contributor.authorRoudesli, Sadok
dc.contributor.authorYemenicioğlu, Ahmet
dc.date.accessioned2016-12-06T08:53:59Z
dc.date.available2016-12-06T08:53:59Z
dc.date.issued2010-12
dc.identifier.citationGuedidi, S., Yürekli, Y., Deratani, A., Déjardin, P., Innocent, C., Altınkaya, S., Roudesli, S., and Yemenicioğlu, A. (2010). Effect of enzyme location on activity and stability of trypsin and urease immobilized on porous membranes by using layer-by-layer self-assembly of polyelectrolyte. Journal of Membrane Science, 365(1-2), 59-67. doi:10.1016/j.memsci.2010.08.042en_US
dc.identifier.issn0376-7388
dc.identifier.urihttp://doi.org/10.1016/j.memsci.2010.08.042
dc.identifier.urihttp://hdl.handle.net/11147/2576
dc.description.abstractThe layer-by-layer (LbL) self-assembly of polyelectrolyte is one of the simplest ways to immobilize enzyme on membrane. In this paper, the immobilization of trypsin (TRY) and urease (URE) on polyacrylonitrile based membranes using the LbL assembly technique was presented. The studied systems consisted in bilayered assemblies with the enzyme layer as the outer layer and trilayered assemblies with the enzyme layer as the inner sandwiched layer. The membrane pore size was chosen so that the smaller enzyme TRY was mainly immobilized within the membrane and confined in the porous membrane structure while URE immobilization mainly took place at the membrane surface. No dramatic difference on reactivity was evidenced between these two enzyme locations. The catalytic activity of immobilized enzymes was found to be lower than the free ones in solution but their stability was dramatically enhanced. The higher activity was observed when the enzyme is deposited as the outer layer of the LbL assembly. On the other hand, the more stable catalytic membranes were obtained when the outer layer consists of a polyelectrolyte covering the enzyme layer. © 2010 Elsevier B.V.en_US
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.relation.isversionof10.1016/j.memsci.2010.08.042en_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectEnzyme immobilizationen_US
dc.subjectCatalytic membraneen_US
dc.subjectLayer-by-layer self-assemblyen_US
dc.subjectPolyelectrolytesen_US
dc.titleEffect of enzyme location on activity and stability of trypsin and urease immobilized on porous membranes by using layer-by-layer self-assembly of polyelectrolyteen_US
dc.typearticleen_US
dc.contributor.authorIDTR28311en_US
dc.contributor.authorIDTR2091en_US
dc.contributor.authorIDTR2675en_US
dc.contributor.iztechauthorYürekli, Yılmaz
dc.contributor.iztechauthorAltınkaya, Sacide
dc.contributor.iztechauthorYemenicioğlu, Ahmet
dc.relation.journalJournal of Membrane Scienceen_US
dc.contributor.departmentİYTE, Mühendislik Fakültesi, Kimya Mühendisliği Bölümüen_US
dc.identifier.volume365en_US
dc.identifier.issue1-2en_US
dc.identifier.startpage59en_US
dc.identifier.endpage67en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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