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dc.creatorMihailović, Mladen
dc.creatorTrbojević-Ivić, Jovana
dc.creatorBanjanac, Katarina
dc.creatorMilosavić, Nenad
dc.creatorVeličković, Dušan
dc.creatorCarević, Milica
dc.creatorBezbradica, Dejan
dc.date.accessioned2018-11-22T00:37:51Z
dc.date.available2018-11-22T00:37:51Z
dc.date.issued2016
dc.identifier.issn0352-5139
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/2391
dc.description.abstractIn this study, two commercial supports (Eupergit (R) C and Purolite (R) A109) were chemically modified in order to introduce thiosulfonate groups, which could subsequently exclusively react with the cysteine residues on the surface of enzymes. Thereafter, the maltase from Saccharomyces cerevisiae was immobilized onto the obtained thiosulfonate-activated supports, resulting in high expressed enzymatic activities (around 50 %), while on the other hand, immobilization on unmodified supports yielded expressed activities less than 5 %. Moreover, protein loadings up to 12.3 mg g(-1) and immobilized activities up to 3580 IU g(-1) were achieved by employment of these thiosulfonate supports. Desorption experiments, performed on samples taken during immobilization, proved that immobilization on the thiosulfonate supports was the first step of fast adsorption onto the supports and the formation of covalent bonds between the thiosulfonate groups and the thiol groups of cysteine represented a second slower step. More importantly, although enzyme coupling occurred via covalent bond formation, the performed immobilization proved to be reversible, since it was shown that 95 % of the immobilized activity could be detached from the support after treatment with a thiol reagent (beta-mercaptoethanol). Thus, the support could be reused after enzyme inactivation.en
dc.publisherSerbian Chemical Soc, Belgrade
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
dc.rightsopenAccess
dc.sourceJournal of the Serbian Chemical Society
dc.subjectalpha-glucosidaseen
dc.subjectcovalent disulfide bridgesen
dc.subjectEupergit (R) Cen
dc.subjectPurolite (R) A109en
dc.titleImmobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supportsen
dc.typearticle
dc.rights.licenseBY-NC-ND
dcterms.abstractТрбојевић-Ивић, Јована; Царевиц, Милица; Велицковиц, Дусан; Милосавиц, Ненад; Безбрадица, Дејан; Михаиловиц, Младен; Бањанац, Катарина;
dc.citation.volume81
dc.citation.issue12
dc.citation.spage1371
dc.citation.epage1382
dc.identifier.wos000392946100004
dc.identifier.doi10.2298/JSC160730099M
dc.citation.other81(12): 1371-1382
dc.citation.rankM23
dc.type.versionpublishedVersion
dc.identifier.scopus2-s2.0-85009798661
dc.identifier.fulltexthttp://cherry.chem.bg.ac.rs/bitstream/id/9367/2389.pdf
dc.identifier.rcubKon_3207


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