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dc.creatorBezbradica, Dejan
dc.creatorMateo, Cesar
dc.creatorGuisan, Jose M.
dc.date.accessioned2021-03-10T12:33:44Z
dc.date.available2021-03-10T12:33:44Z
dc.date.issued2014
dc.identifier.issn1381-1177
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/2813
dc.description.abstractImmobilization of enzymes on glutaraldehyde-activated supports has been largely used on supports previously activated with amine groups. Therefore, the supports are positively charged hence usually the immobilization is promoted through a two step mechanism: in a first step the enzyme is adsorbed on the support via an anionic exchange mechanism and then, the covalent immobilization occurs. In this paper a new glutaraldehyde activated support without a net charge is presented and characterized in immobilizations of trypsin, penicillin acylase G, lipase and E. coli BL21 cell extract. Immobilization mechanism was studied and this was produced without an adsorption step. This support promoted initially a reversible immobilization, converting into irreversible after incubation of the enzyme-support for several days or after a reduction step. In addition the stability of glutaraldehyde groups was studied retaining around 50 and 25% of its immobilization capacity for 24 h at pH 7 and 10 respectively. This fact allows the incubation of the enzyme with the support even at alkaline pH promoting an extra stabilization factor for trypsin on this support.en
dc.publisherElsevier, Amsterdam
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
dc.rightsrestrictedAccess
dc.sourceJournal of Molecular Catalysis B-Enzymatic
dc.subjectEnzyme immobilizationen
dc.subjectGlutaraldehydeen
dc.subjectCysteineen
dc.subjectAgaroseen
dc.subjectStabilityen
dc.titleNovel support for enzyme immobilization prepared by chemical activation with cysteine and glutaraldehydeen
dc.typearticle
dc.rights.licenseARR
dc.citation.epage224
dc.citation.other102: 218-224
dc.citation.rankM22
dc.citation.spage218
dc.citation.volume102
dc.identifier.doi10.1016/j.molcatb.2014.02.021
dc.identifier.rcubconv_4426
dc.identifier.scopus2-s2.0-84896334037
dc.identifier.wos000335872900031
dc.type.versionpublishedVersion


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