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Decyl acetate synthesis by enzyme catalysis in sc-CO2

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dc.contributor.authorRebocho, Sílvia F.
dc.contributor.authorRibeiro, Adriano S.
dc.contributor.authorFerreira, Olga
dc.contributor.authorOliveira, Manuela V.
dc.contributor.authorVidinha, Pedro
dc.contributor.authorBarreiros, Susana F.
dc.contributor.authorMacedo, Eugénia A.
dc.contributor.authorLoureiro, José M.
dc.date.accessioned2010-03-04T12:18:15Z
dc.date.available2010-03-04T12:18:15Z
dc.date.issued2008
dc.description.abstractThe synthesis of decyl acetate, from the transesterification of vinyl acetate with decanol, was studied in a high-pressure experimental set-up, equipped with a variable volume batch reactor, operating isothermally at 35 ºC and 100 bar, using CO2 in supercritical conditions as solvent, and Candida antarctica lipase B (CALB), immobilized on the macroporous resin Lewatit B (Novozym 435®), as catalyst. The enzymatic content was determined for each particle size of the catalyst. It was shown that the smallest particles have a larger specific amount of enzyme, and the results indicate that the enzyme is located in an external shell of the particle, following an “egg-shell” model type, with a thickness of ca. 60 μm (assuming a homogeneous distribution), independent of the particle size. Both external and internal mass transfer resistances were evaluated. External resistances were easily eliminated by stirring and internal diffusional limitations can be considered as negligible. The effect of the feed concentration of substrates on the initial reaction rate was also studied. It was observed that, above a certain concentration of decanol in excess relatively to vinyl acetate, the reaction is inhibited by the alcohol. On the contrary, the reaction is favoured when the reactor is fed with excess of vinyl acetate, with a significant enhancement of its initial rate. These results are consistent with a Ping-pong bi-bi type mechanism with competitive inhibition by the alcohol, commonly used in the description of enzymatic reactions of esterification/ transesterification.pt
dc.description.sponsorshipFinancial support for this work was in part provided by national research grant POCI/EQU/56732/2004 and by LSRE financing by FEDER/POCI/2010, for which the authors are thankful. A.S.Ribeiro and P.Vidinha acknowledge their Ph.D. scholarship by FCT (SFRH/BD/13084/2003 and SFRH/BD/13787/2003).pt
dc.identifier.citationRebocho, Sílvia F.; Ribeiro, Adriano S.; Ferreira, Olga; Oliveira, Manuela V.; Vidinha, Pedro; Barreiros, Susana; Macedo, Eugénia A.; Loureiro, José M. (2008). Decyl acetate synthesis by enzyme catalysis in sc-CO2. In Proceedings of the 10th International Chemical and Biological Engineering Conference - CHEMPOR (CD-ROM). Braga. p.114-119. ISBN 978-972-97810-3-2pt
dc.identifier.isbn978-972-97810-3-2
dc.identifier.urihttp://hdl.handle.net/10198/2190
dc.language.isoengpt
dc.publisherCHEMPORpt
dc.subjectSupercritical CO2pt
dc.subjectImmobilized lipase B of Candida antarcticapt
dc.subjectTransesterificationpt
dc.subjectPing-pong bi-bi mechanismpt
dc.subjectDecyl acetatept
dc.titleDecyl acetate synthesis by enzyme catalysis in sc-CO2pt
dc.typeconference object
dspace.entity.typePublication
oaire.citation.conferencePlaceBragapt
oaire.citation.endPage119pt
oaire.citation.startPage114pt
oaire.citation.titleProceedings of the 10th International Chemical and Biological Engineering Conference - CHEMPOR 2008 (CD-ROM)pt
person.familyNameFerreira
person.givenNameOlga
person.identifier.ciencia-id9F1D-C75A-4A54
person.identifier.orcid0000-0001-8414-3479
person.identifier.ridM-4567-2013
person.identifier.scopus-author-id57203083219
rcaap.rightsopenAccesspt
rcaap.typeconferenceObjectpt
relation.isAuthorOfPublication59e0c608-0c21-4191-af5e-529d21970399
relation.isAuthorOfPublication.latestForDiscovery59e0c608-0c21-4191-af5e-529d21970399

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