Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/2576
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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.authorAlsoy Altınkaya, 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., Alsoy 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.issn1873-3123-
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.isoenen_US
dc.publisherElsevier Ltd.en_US
dc.relation.ispartofJournal of Membrane Scienceen_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.authoridTR28311en_US
dc.authoridTR2091en_US
dc.authoridTR2675en_US
dc.institutionauthorYürekli, Yılmaz-
dc.institutionauthorAlsoy Altınkaya, Sacide-
dc.institutionauthorYemenicioğlu, Ahmet-
dc.departmentIzmir Institute of Technology. Chemical Engineeringen_US
dc.identifier.volume365en_US
dc.identifier.issue1-2en_US
dc.identifier.startpage59en_US
dc.identifier.endpage67en_US
dc.identifier.wosWOS:000284750300007en_US
dc.identifier.scopus2-s2.0-78049295053en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1016/j.memsci.2010.08.042-
dc.relation.doi10.1016/j.memsci.2010.08.042en_US
dc.coverage.doi10.1016/j.memsci.2010.08.042en_US
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
item.fulltextWith Fulltext-
item.grantfulltextopen-
item.cerifentitytypePublications-
crisitem.author.dept03.02. Department of Chemical Engineering-
crisitem.author.dept03.08. Department of Food Engineering-
Appears in Collections:Chemical Engineering / Kimya Mühendisliği
Food Engineering / Gıda Mühendisliği
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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