Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study

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 t...

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Autores principales:	Saponji,Svetlana, Kneevi-Jugovi,Zorica D, Bezbradica,Dejan I, Zuza,Milena G, Saied,Omar Ali, Boskovi-Vragolovi,Nevenka, Mijin,Dusan Z
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2010
Materias:	bioreactors covalent immobilization ester non-aqueous system optimization technique
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000600012
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spelling	oai:scielo:S0717-345820100006000122011-05-26Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor studySaponji,SvetlanaKneevi-Jugovi,Zorica DBezbradica,Dejan IZuza,Milena GSaied,Omar AliBoskovi-Vragolovi,NevenkaMijin,Dusan Z bioreactors covalent immobilization ester non-aqueous system optimization technique 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 37ï¿½C, 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.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.13 n.6 20102010-11-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000600012en
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	bioreactors covalent immobilization ester non-aqueous system optimization technique
spellingShingle	bioreactors covalent immobilization ester non-aqueous system optimization technique Saponji,Svetlana Kneevi-Jugovi,Zorica D Bezbradica,Dejan I Zuza,Milena G Saied,Omar Ali Boskovi-Vragolovi,Nevenka Mijin,Dusan Z Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study
description	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 37ï¿½C, 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.
author	Saponji,Svetlana Kneevi-Jugovi,Zorica D Bezbradica,Dejan I Zuza,Milena G Saied,Omar Ali Boskovi-Vragolovi,Nevenka Mijin,Dusan Z
author_facet	Saponji,Svetlana Kneevi-Jugovi,Zorica D Bezbradica,Dejan I Zuza,Milena G Saied,Omar Ali Boskovi-Vragolovi,Nevenka Mijin,Dusan Z
author_sort	Saponji,Svetlana
title	Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study
title_short	Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study
title_full	Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study
title_fullStr	Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study
title_full_unstemmed	Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study
title_sort	use of candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2010
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000600012
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Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: Batch and fluidized bed reactor study

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