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dc.creatorMiletić, N.
dc.creatorRohandi, R.
dc.creatorVuković, Zorica
dc.creatorNastasović, Aleksandra
dc.creatorLoos, K.
dc.date.accessioned2019-01-30T17:21:38Z
dc.date.available2019-01-30T17:21:38Z
dc.date.issued2009
dc.identifier.issn1381-5148
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/600
dc.description.abstractCrosslinked macroporous hydrophilic poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) [abbreviated poly(GMA-co-EGDMA)] with identical chemical structure (60% of glycidyl methacrylate) but with varied average pore sizes (from 30 to 560 nm), specific surface areas (from 13.2 to 106.0 m2/g), specific volumes (from 0.755 to 1.191 cm3/g) and particle sizes (<100 μm-630 μm) were synthesized via suspension polymerization. Modifications of poly(GMA-co-EGDMA) with various diamines (1,2-diaminoethane, 1,4-diaminobutane, 1,6-diaminohexane and 1,8-diaminooctane), 2-fluoroethylamine, glutaraldehyde and cyanuric chloride were carried out. The influence of the interaction between Candida antarctica lipase B (Cal-B) and various carriers during immobilization on the loading and hydrolytic activity (hydrolysis of para-nitrophenyl acetate) of the immobilized Cal-B were studied. Immobilization of Cal-B was performed at different temperatures and pH values. Cal-B immobilized at 30 °C and pH 6.8 was leading to increased activities. Purely physical adsorption between enzyme and copolymer was observed on carriers in which amine or fluorine groups were introduced into the carrier structure by modification with various diamines or 2-fluoroethylamine. As a consequence enzyme loading and activity decreases. In contrary, modification of the poly(GMA-co-EGDMA) with glutaraldehyde and cyanuric chloride results in a covalent connection between enzyme and carrier. The obtained results show a significant increase in Cal-B activity. The influence of the amount of glutaraldehyde and cyanuric chloride used for modification was screened. Increasing the amount of glutaraldehyde or cyanuric chloride used for modification resulted in an increase of the enzyme loading. Consequently, higher amount of glutaraldehyde used led to a higher fraction of the enzyme molecules that are covalently connected on to the carrier. As the amount of glutaraldehyde or cyanuric chloride used for modifications increases, activity of immobilized C. antarctica lipase B primarily increases, showing the highest value for 0.66% and 0.050% w/w, respectively, and subsequently decreases. We could show that Cal-B immobilized on epoxy-containing copolymer modified with glutaraldehyde and cyanuric chloride performs higher activity than free enzyme powder.en
dc.publisherElsevier Science Bv, Amsterdam
dc.relationinfo:eu-repo/grantAgreement/MESTD/MPN2006-2010/142039/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/MPN2006-2010/166001/RS//
dc.rightsrestrictedAccess
dc.sourceReactive and Functional Polymers
dc.subjectCandida antarctica lipase Ben
dc.subjectCyanuric chloride activationen
dc.subjectEnzyme immobilizationen
dc.subjectEpoxy-activated supporten
dc.subjectGlutaraldehyde activationen
dc.titleSurface modification of macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) resins for improved Candida antarctica lipase B immobilizationen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractНастасовић, Aлександра; Милетић, Н.; Роханди, Р.; Лоос, К.; Вуковић, Зорица;
dc.citation.volume69
dc.citation.issue1
dc.citation.spage68
dc.citation.epage75
dc.citation.other69(1): 68-75
dc.citation.rankM21
dc.identifier.doi10.1016/j.reactfunctpolym.2008.11.001
dc.identifier.rcubConv_4182
dc.identifier.scopus2-s2.0-58949100868
dc.identifier.wos000263992700011
dc.type.versionpublishedVersion


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