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dc.creatorKnežević, Zorica
dc.creatorMojović, Ljiljana
dc.creatorAdnađević, Borivoj
dc.date.accessioned2021-03-10T09:45:00Z
dc.date.available2021-03-10T09:45:00Z
dc.date.issued1998
dc.identifier.issn0141-0229
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/192
dc.description.abstractLipase from Candida cylindracea immobilized on hydrophobic zeolite type Y was used to hydrolyze palm oil in a microaqueous two-phase reaction system containing isooctane as organic medium and lecithin as surfactant. The lipase was immobilized to zeolite by adsorption. The maximum amount of bound protein at 8.2 mg g(-1) and an immobilization efficiency of 33% were achieved under optimum conditions. The kinetics of lipase binding to zeolite were assessed by using the general model of topochemical reaction. Based on the values of the specific kinetic model parameters, we propose that the adsorption process is controlled by surface kinetics that was later experimentally confirmed The activation energy for lipase adsorption on zeolite was 43 kJ mol(-1). The lipase immobilized an zeolite had 35% of the activity of the free enzyme. After the seventh cycle, immobilized lipase retained 10% of the initial activity in palm oil hydrolysis.en
dc.publisherElsevier Science Inc, New York
dc.rightsrestrictedAccess
dc.sourceEnzyme and Microbial Technology
dc.subjectCandida cylindracea lipaseen
dc.subjectzeoliteen
dc.subjectimmobilizationen
dc.subjecthydrolysisen
dc.subjectpalm oilen
dc.subjectkinetic modelen
dc.titlePalm oil hydrolysis by lipase from Candida cylindracea immobilized on zeolite type Yen
dc.typearticle
dc.rights.licenseARR
dc.citation.epage280
dc.citation.issue4
dc.citation.other22(4): 275-280
dc.citation.rankM22
dc.citation.spage275
dc.citation.volume22
dc.identifier.doi10.1016/S0141-0229(97)00187-7
dc.identifier.rcubconv_1846
dc.identifier.scopus2-s2.0-0032032079
dc.identifier.wos000072255700010
dc.type.versionpublishedVersion


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