Catalytic Performances of Chemically Immobilized Urease Under Static and Dynamic Conditions: a Comparative Study

dc.contributor.author Yürekli, Yılmaz
dc.contributor.author Alsoy Altınkaya, Sacide
dc.coverage.doi 10.1016/j.molcatb.2011.03.006
dc.date.accessioned 2017-03-07T07:17:37Z
dc.date.available 2017-03-07T07:17:37Z
dc.date.issued 2011
dc.description.abstract Immobilized urease has been used for direct removal of urea from aqueous solution and as biological sensing material in the preparation of urea biosensors. The former application is carried out under dynamic condition using ultrafiltration membrane either in tubular form or in flat sheet, while the latter is used in static condition. In this study, the performance of chemically immobilized urease on poly(acrylonitrile-co-sodium methallyl sulfonate) ultrafiltration membrane was determined under both static and dynamic conditions. Results reveal that the immobilization enhanced the thermal and storage stabilities of urease. The hydraulic permeability of urea solution was not influenced by the addition of enzyme layer. The maximum reaction rate measured under pressure in the ultrafiltration unit was found higher compared to the rate observed just under mixing without any pressure applied. The highest urea conversion was found at the lowest transmembrane pressure and the urea concentration in the feed solution. The catalytic activity of the membrane was completely preserved at the end of 450 min of filtration. en_US
dc.identifier.citation Yürekli, Y., and Alsoy Altınkaya, S. (2011). Catalytic performances of chemically immobilized urease under static and dynamic conditions: A comparative study. Journal of Molecular Catalysis B: Enzymatic, 71(1-2), 36-44. doi:10.1016/j.molcatb.2011.03.006 en_US
dc.identifier.doi 10.1016/j.molcatb.2011.03.006 en_US
dc.identifier.doi 10.1016/j.molcatb.2011.03.006
dc.identifier.issn 1381-1177
dc.identifier.scopus 2-s2.0-79956125301
dc.identifier.uri http://doi.org/10.1016/j.molcatb.2011.03.006
dc.identifier.uri https://hdl.handle.net/11147/4990
dc.language.iso en en_US
dc.publisher Elsevier Ltd. en_US
dc.relation.ispartof Journal of Molecular Catalysis B: Enzymatic en_US
dc.rights info:eu-repo/semantics/openAccess en_US
dc.subject Covalent immobilization en_US
dc.subject EDC/NHS crosslinker en_US
dc.subject Membrane enzymatic reactor en_US
dc.subject Ultrafiltration en_US
dc.subject Urease en_US
dc.title Catalytic Performances of Chemically Immobilized Urease Under Static and Dynamic Conditions: a Comparative Study en_US
dc.type Article en_US
dspace.entity.type Publication
gdc.author.institutional Yürekli, Yılmaz
gdc.author.institutional Alsoy Altınkaya, Sacide
gdc.author.yokid 28311
gdc.bip.impulseclass C5
gdc.bip.influenceclass C5
gdc.bip.popularityclass C4
gdc.coar.access open access
gdc.coar.type text::journal::journal article
gdc.collaboration.industrial false
gdc.description.department İzmir Institute of Technology. Chemical Engineering en_US
gdc.description.endpage 44 en_US
gdc.description.issue 1-2 en_US
gdc.description.publicationcategory Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı en_US
gdc.description.startpage 36 en_US
gdc.description.volume 71 en_US
gdc.identifier.openalex W2030075899
gdc.identifier.wos WOS:000291451000006
gdc.index.type WoS
gdc.index.type Scopus
gdc.oaire.accesstype BRONZE
gdc.oaire.diamondjournal false
gdc.oaire.impulse 2.0
gdc.oaire.influence 3.3107106E-9
gdc.oaire.isgreen true
gdc.oaire.keywords Ultrafiltration
gdc.oaire.keywords Membrane enzymatic reactor
gdc.oaire.keywords EDC/NHS crosslinker
gdc.oaire.keywords Urease
gdc.oaire.keywords Covalent immobilization
gdc.oaire.popularity 5.5744636E-9
gdc.oaire.publicfunded false
gdc.oaire.sciencefields 02 engineering and technology
gdc.oaire.sciencefields 0210 nano-technology
gdc.oaire.sciencefields 01 natural sciences
gdc.oaire.sciencefields 0104 chemical sciences
gdc.openalex.collaboration National
gdc.openalex.fwci 0.47296481
gdc.openalex.normalizedpercentile 0.69
gdc.opencitations.count 12
gdc.plumx.crossrefcites 13
gdc.plumx.mendeley 11
gdc.plumx.scopuscites 16
gdc.scopus.citedcount 16
gdc.wos.citedcount 13
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relation.isOrgUnitOfPublication.latestForDiscovery 9af2b05f-28ac-4021-8abe-a4dfe192da5e

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