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RevistaBioresource Technology
Año2013
Volumen134
Páginas417-422
Internacional

IMPROVED PRODUCTION OF BUTYL BUTYRATE BY USING LIPASE FROM Thermomyces lanuginosus IMMOBILIZED ON STYRENE-DIVINYLBENZENE BEADS

Autores:Cristina Garcia-Galan, Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Andréa B. Martins1a, John L. R Friedrich1a, Cristina Garcia-Galan2, Oveimar Barbosa2,3, Marco A. Z. Ayub1b, Roberto Fernandez-Lafuente2*, Rafael C. Rodrigues1a,*
 
1aBiocatalysis and Enzyme Technology Lab and 1bBiochemical Engineering Lab (BiotecLab), Institute of Food Science and Technology, Federal University of Rio Grande do Sul State, Av. Bento Gonçalves, 9500, P.O. Box 15090, ZC 91501-970, Porto Alegre, RS, Brazil.
2Department of Biocatalysis, ICP - CSIC. Campus UAM-CSIC. Cantoblanco, ZC 28049, Madrid, Spain.
3Escuela de Química, Grupo de Investigación en Bioquímica y Microbiología (GIBIM), Universidad Industrial de Santander, Bucaramanga, Colombia.
Two immobilized preparations from Thermomyces lanuginosus lipase (TLL) were compared in the synthesis of butyl butyrate. The commercial Lipozyme TL-IM, and TLL immobilized on styrene-divinylbenzene beads (MCI-TLL) were tested in the esterification reaction using n-hexane as solvent. The variables temperature (30 to 60 °C), substrate molar ratio (1:1 to 5:1), added water (0 to 1 %), and biocatalyst content (3 to 40 %) were evaluated in terms of initial reaction rate for each biocatalyst. SDS-PAGE analysis revealed that MCI-TLL had an immobilized enzymatic load twice as high as Lipozyme TL-IM, but with an activity 3-fold higher. MCI-TLL presented high initial reaction rates up to 1.0 M butyric acid, while Lipozyme TL-IM showed a decrease in its activity above 0.5 M. Moreover, MCI-TLL allowed a productivity of 14.5 mmol g-1h-1, while Lipozyme TL-IM 3.2 mmol g-1h-1, both by mass of biocatalyst.
Palabras clave:interfacial activated lipases; esterification; butyl butyrate; TLL; styrene-divinylbenzene beads.
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