Process Biotechnology
  Biotechnology Industry
Electronic Journal of Biotechnology ISSN: 0717-3458 Vol. 13 No. 6, Issue of November 15, 2010
© 2010 by Pontificia Universidad Católica de Valparaíso -- Chile Received April 26, 2010 / Accepted August 30, 2010
DOI: 10.2225/vol13-issue6-fulltext-8  

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

Svetlana Saponjić1 · Zorica D. Knežević-Jugović*1 · Dejan I. Bezbradica1 · Milena G. Zuza1 · Omar Ali Saied1 · Nevenka Bosković-Vragolović2 · Dusan Z. Mijin3

1Department of Biotechnology and Biochemical Engineering, Faculty of Technology and Metallurgy, University of Belgrade, Belgrade, Serbia
2Department of Chemical Engineering, Faculty of Technology and Metallurgy, University of Belgrade, Belgrade, Serbia
3Department of Organic Chemistry, Faculty of Technology and Metallurgy, University of Belgrade, Belgrade, Serbia 

*Corresponding author:

Financial support: This work was financed by the Ministry of Science and Technological Development of the Republic of Serbia (Project No. TR-20064).

Keywords: bioreactors, covalent immobilization, ester, non-aqueous system, optimization technique.

Abstract   Full Text

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 37ºC, 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.

Supported by UNESCO / MIRCEN network