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Provedor de dados:  Electron. J. Biotechnol.
País:  Chile
Título:  Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study
Autores:  Saponji,Svetlana
Kneevi-Jugovi,Zorica D
Bezbradica,Dejan I
Zuza,Milena G
Saied,Omar Ali
Boskovi-Vragolovi,Nevenka
Mijin,Dusan Z
Data:  2010-11-01
Ano:  2010
Palavras-chave:  Bioreactors
Covalent immobilization
Ester
Non-aqueous system
Optimization technique
Resumo:  Lipase from Candida rugosa was covalently immobilized on Sepabeads EC-EP for application for amyl caprylate synthesis in an organic solvent system. Several solvents were tested in terms of biocatalyst stability and the best result was obtained with isooctane. The lipase-catalyzed esterification in the selected system was performed in batch and fluidized bed reactor systems. The influence of several important reaction parameters including temperature, initial water content, enzyme loading, acid/alcohol molar ratio, and time of addition of molecular sieves is carefully analyzed by means of an experimental design. Almost complete conversion (> 99%) of the substrate to ester could be performed in a batch reactor system, using lipase loading as low as 37 mg g-1 dry support and in a relatively short time (24 hrs) at 37�C, when high initial substrate molar ratio of 2.2 is used. Kinetics in a fluidized bed reactor system seems to still have a slightly better profile than in the batch system (90.2% yields after 14 hrs). The fluidized bed reactor operated for up 70 hrs almost with no loss in productivity, implying that the proposed process and the immobilized system could provide a promising approach for the amyl caprylate synthesis at the industrial scale.
Tipo:  Journal article
Idioma:  Inglês
Identificador:  http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000600012
Editor:  Pontificia Universidad Católica de Valparaíso
Formato:  text/html
Fonte:  Electronic Journal of Biotechnology v.13 n.6 2010
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