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RevistaJournal of Molecular catalysys B: Enzymatic
Año2013
Volumen94
Páginas 51-56
Internacional

Optimization of synthesis of methyl esters catalyzed by lipase B from Candida antarctica immobilized in hydrophobic supports

Autores:Roberto Fernandez-Lafuente, Cristina Garcia-Galan
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Jakeline K. Poppe1, Cristina Garcia-Galan2, Carla R. Matte1, Roberto Fernandez-Lafuente2, Rafael C. Rodrigues1, Marco Antônio Z. Ayub1*.
 
1Biochemical Engineering Lab (BiotecLab), Institute of Food Science and Technology, Federal University of Rio Grande do Sul, 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.

In this work two immobilized preparations of lipase (EC 3.1.1.3) B from Candida
antarctica (CALB) were compared for the synthesis of fatty acid methyl esters (FAME)
 using soybean oil. Commercial Novozym 435 (CALB-435) and CALB immobilized on
 styrene-divinylbenzene beads (CALB-MCI) were tested for the transesterification
 reactions. Central composite design (CCD) and response surface methodology (RSM)
 were used to optimize the reaction parameters, substrate molar ratio, enzyme content,
 and the added amount of water, on the initial reaction rate as response. The biocatalysts
 showed different optimal conditions for the production of FAME. For CALB-435,
optima conditions were 5.6:1 molar ratio methanol:oil, 25 % enzyme, and 5.44 % of
added water, while for MCI-CALB, these optima were 3:1 molar ratio methanol:oil, 25% enzyme, and 1.18 % of added water, resulting in initial reaction rates of 51.47 mmol L-1 h-1, and 57 mmol L-1 h-1 13 of FAME, respectively. Conversions of 93.38 % using CALB-435, and 99.03 % using CALB-MCI were obtained after 72 h of reaction under the optimized conditions. Repeated batches of reaction were carried out to test the
operational stability of biocatalysts, with both preparations keeping around 70 % of their initial activity after eight batches.
Palabras clave:methyl esters; CALB; transesterification; RSM; enzyme reuse
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