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dc.creatorJakovetić, Sonja
dc.creatorLuković, Nevena
dc.creatorBošković-Vragolović, Nevenka
dc.creatorBezbradica, Dejan
dc.creatorPicazo-Espinosa, Rafael
dc.creatorKnežević-Jugović, Zorica
dc.date.accessioned2021-03-10T12:09:39Z
dc.date.available2021-03-10T12:09:39Z
dc.date.issued2013
dc.identifier.issn0888-5885
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/2431
dc.description.abstractEthyl cinnamate, an ester known as flavor and fragrance compound, has been synthesized using two immobilized bioreactor systems, batch and fluidized bed bioreactors. The enzyme used for this synthesis is a commercial lipase B preparation, Novozyme 435. Initial kinetic studies were conducted in both employed bioreactor configurations, and kinetic constants were obtained. Several models were tried for fitting of experimental data, but the best fit, for both bioreactors, was obtained when the ping-pong bi-bi mechanism was used. Interestingly enough, ethanol inhibition occurred in batch bioreactor, but it did not exist in the fluidized bed bioreactor. Solid-liquid mass transfer coefficients were calculated for both bioreactors to determine whether mass transfer limitations existed in either of these systems. The calculation of Damkohler numbers and Thiele modulus confirmed that mass transfer limitations had no effect on the overall reaction in both bioreactors.en
dc.publisherAmer Chemical Soc, Washington
dc.relationE!6750
dc.rightsrestrictedAccess
dc.sourceIndustrial & Engineering Chemistry Research
dc.titleComparative Study of Batch and Fluidized Bed Bioreactors for Lipase-Catalyzed Ethyl Cinnamate Synthesisen
dc.typearticle
dc.rights.licenseARR
dc.citation.epage16697
dc.citation.issue47
dc.citation.other52(47): 16689-16697
dc.citation.rankM21
dc.citation.spage16689
dc.citation.volume52
dc.identifier.doi10.1021/ie402069c
dc.identifier.rcubconv_4276
dc.identifier.scopus2-s2.0-84889243686
dc.identifier.wos000327812400016
dc.type.versionpublishedVersion


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