Publication:
Xylanase immobilization on functionalized polyaniline support by covalent attachment

dc.contributor.authorKAHRAMAN, MEMET VEZİR
dc.contributor.authorsMadakbas, Seyfullah; Danis, Ozkan; Demir, Serap; Kahraman, Memet Vezir
dc.date.accessioned2022-03-12T18:08:22Z
dc.date.available2022-03-12T18:08:22Z
dc.date.issued2013
dc.description.abstractChemically synthesized polyaniline (PANI) was used as polymeric support for xylanase immobilization. The polymer was first activated with glutaraldehyde and then xylanase was successfully immobilized. Xylanase bound polymer was characterized using FTIR. The optimum pH of the immobilized enzyme was at pH 5, which was shifted 1.0?pH unit to the acidic region when compared to the free enzyme. Thermal stability of the xylanase was improved with the immobilization. The characteristic properties of the immobilized and native enzyme, such as kinetic activity, reusability and storage stability were also studied at optimum pH and temperature. Immobilized enzyme exhibited better reusability and storage stability than the free one. Vmax values for the free and immobilized enzymes were calculated as 1.44 and 0.44?mg/mL/min, respectively. The Km values for the immobilized xylanase were found to be lower.
dc.identifier.doi10.1002/star.201200104
dc.identifier.eissn1521-379X
dc.identifier.issn0038-9056
dc.identifier.urihttps://hdl.handle.net/11424/231143
dc.identifier.wosWOS:000312999200016
dc.language.isoeng
dc.publisherWILEY-V C H VERLAG GMBH
dc.relation.ispartofSTARCH-STARKE
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectImmobilization
dc.subjectPANI
dc.subjectXylanase
dc.subjectALPHA-AMYLASE
dc.subjectACTIVATION
dc.subjectCARBONATE
dc.subjectENZYMES
dc.titleXylanase immobilization on functionalized polyaniline support by covalent attachment
dc.typearticle
dspace.entity.typePublication
local.avesis.id42ca566c-b104-4c42-9fac-64003b010f80
local.import.packageSS17
local.indexed.atWOS
local.indexed.atSCOPUS
local.journal.numberofpages5
oaire.citation.endPage150
oaire.citation.issue1-2
oaire.citation.startPage146
oaire.citation.titleSTARCH-STARKE
oaire.citation.volume65
relation.isAuthorOfPublication7676f3ad-0384-4001-b17d-b928ae2de7e6
relation.isAuthorOfPublication.latestForDiscovery7676f3ad-0384-4001-b17d-b928ae2de7e6

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