Immobilization of lipases and assay in continuous fixed bed reactor

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dc.contributor.authorDos Reis-Costa, Leonice [UNESP]
dc.contributor.authorSoares, Andreimar M.
dc.contributor.authorFrança, Suzelei C.
dc.contributor.authorTrevisan, Henrique C. [UNESP]
dc.contributor.authorRoberts, Timothy John C. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUNAERP
dc.date.accessioned2014-05-27T11:20:57Z
dc.date.available2014-05-27T11:20:57Z
dc.date.issued2003-12-01
dc.description.abstractLipases are versatile enzymes regarding the range of reactions they catalyse and substrates on which they act. They are as well important as catalyst in organic synthesis. Their immobilization on appropriate supports confer them greater stability besides the possibility of operating in continuous reactors. In order to explore these abilities, the reactions involving hydrolysis of p-nitrophenyl acetate (PNPA) and transesterification of PNPA with n-butanol were chosen. Lipases from two different sources were assayed, namely: microbial (Candida rugosa, CRL, Sigma Type VII) and pancreatic (PPL, Sigma, Type 11). Two immobilization methods were also used, namely: 1) adsorption, using as support the following silica derivatives (150-300μm e 450μ): phenyl, epoxy, amino and without derivation, and 2) covalent binding, using glutaraldehyde as binding agent and silica amino as support. This later method led to better results. Hydrolytic activity was 6.1 U/gsupport for CRL and 0.97U/gsupport for PPL, and of transesterification, 2,8U/gsupport for CRL and 1,9U/gsupport for PPL. Stability of the immobilized enzyme as a function of temperature was evaluated for CRL at 40°C and 50°C and for PPL at 32°C and 40°C. The assays were initially carried out batchwise, both for soluble and immobilized enzymes, aiming to the obtention of parameters for the continues reactor. Lipases immobilized by covalent binding were used in the assays of operacional stability in continuos reactors. For PPL in aqueous medium, at 32°C, and CRL in organic medium at 40°C, both operating continuously, no significant loss of activity was detected along the analysis period of 17 days. In the case of CRL in aqueous medium at 40°C there was a loss of activity around 40% after 18 days. For PPL in organic medium at 40°C the loss was 33% after 20 days. Compairing both sources with each other, very different results were obtained. Higher activitiy was found for CRL, both for hydrolysis and for transesterification reactions, with higher stability in organic medium. PPL showed lower activity as well as higher stability in aqueous medium. The immobilization method by covalent binding showed to be the most appropriate. Immobilized lipases are therefore relatively stable both in aqueous and organic medium.en
dc.description.affiliationDepto. de Bioquim. e Tecn. Quim. Instituto de Química UNESP, Araraquara - SP
dc.description.affiliationDepartamento de Biotecnologia Universidade de Ribeirão Preto UNAERP, 14096-380 Ribeirão Preto - SP
dc.description.affiliationDepartamento de Biotecnologia UNAERP, 14096-380 Ribeirão Preto/SP
dc.description.affiliationUnespDepto. de Bioquim. e Tecn. Quim. Instituto de Química UNESP, Araraquara - SP
dc.format.extent619-628
dc.identifierhttp://dx.doi.org/10.2174/0929866033478573
dc.identifier.citationProtein and Peptide Letters, v. 10, n. 6, p. 619-628, 2003.
dc.identifier.doi10.2174/0929866033478573
dc.identifier.issn0929-8665
dc.identifier.scopus2-s2.0-0348196709
dc.identifier.urihttp://hdl.handle.net/11449/67523
dc.identifier.wosWOS:000187351500011
dc.language.isoeng
dc.relation.ispartofProtein and Peptide Letters
dc.relation.ispartofjcr1.039
dc.relation.ispartofsjr0,429
dc.rights.accessRightsAcesso restrito
dc.sourceScopus
dc.subjectContinuous reactor
dc.subjectImmobilization
dc.subjectLipases
dc.subjectSilica
dc.subjectglutaraldehyde
dc.subjectimmobilized enzyme
dc.subjectsilicon dioxide
dc.subjecttriacylglycerol lipase
dc.subjectadsorption
dc.subjectanimal
dc.subjectbioreactor
dc.subjectCandida
dc.subjectchemistry
dc.subjectcomparative study
dc.subjectdesiccation
dc.subjectenzyme stability
dc.subjectmetabolism
dc.subjectswine
dc.subjecttemperature
dc.subjecttime
dc.subjectAdsorption
dc.subjectAnimals
dc.subjectBioreactors
dc.subjectDesiccation
dc.subjectEnzyme Stability
dc.subjectEnzymes, Immobilized
dc.subjectGlutaral
dc.subjectLipase
dc.subjectSilicon Dioxide
dc.subjectSwine
dc.subjectTemperature
dc.subjectTime Factors
dc.subjectAnimalia
dc.subjectCandida rugosa
dc.subjectSus scrofa
dc.titleImmobilization of lipases and assay in continuous fixed bed reactoren
dc.typeArtigo
dcterms.licensehttp://eurekaselect.com/209
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt

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