Приказ основних података о документу

dc.creatorMojović, Ljiljana
dc.creatorŠiler-Marinković, Slavica
dc.creatorKukić, G.
dc.creatorBugarski, Branko
dc.creatorVunjak-Novaković, Gordana
dc.date.accessioned2021-03-10T09:35:56Z
dc.date.available2021-03-10T09:35:56Z
dc.date.issued1994
dc.identifier.issn0141-0229
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/51
dc.description.abstractCelite-immobilized lipase from Rhizopus arrhizus was encapsulated in lecithin reverse micelles and used to interesterify triacylglycerols of palm oil midfraction with stearic acid in n-hexane. The reaction kinetics were studied in a gas-lift reactor with an internal draft tube. The equilibrium state was reached more rapidly in the gas-lift reactor (9 h) than in comparative shake-flask studies (12 h). A 2.8-fold increase in the productivity of interesterification by Celite-immobilized and lecithin-protected lipase was achieved in the gas-lift reactor when compared with shake-flask experiments. The high productivity of the enzymatic interesterification was attributed to the combined effects of enzyme immobilization and reactor design.en
dc.publisherElsevier Science Inc, New York
dc.rightsrestrictedAccess
dc.sourceEnzyme and Microbial Technology
dc.subjectCelite-immobilized lipaseen
dc.subjectgas-lift reactoren
dc.subjectInteresterificationen
dc.subjectpalm oil midfractionen
dc.subjectreverse micellesen
dc.titleRhizopus arrhizus lipase-catalyzed interesterification of palm oil midfraction in a gas-lift reactoren
dc.typearticle
dc.rights.licenseARR
dc.citation.epage162
dc.citation.issue2
dc.citation.other16(2): 159-162
dc.citation.spage159
dc.citation.volume16
dc.identifier.doi10.1016/0141-0229(94)90079-5
dc.identifier.pmid
dc.identifier.scopus2-s2.0-0028140542
dc.type.versionpublishedVersion


Документи

Thumbnail

Овај документ се појављује у следећим колекцијама

Приказ основних података о документу