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A monolithic lipase reactor for biodiesel production by transesterification of triacylglycerides into fatty acid methyl esters.
Urban, Jiri; Svec, Frantisek; Fréchet, Jean M J.
Afiliação
  • Urban J; Department of Chemistry, University of California, Berkeley, California 94720, USA.
Biotechnol Bioeng ; 109(2): 371-80, 2012 Feb.
Article em En | MEDLINE | ID: mdl-21915852
An enzymatic reactor with lipase immobilized on a monolithic polymer support has been prepared and used to catalyze the transesterification of triacylglycerides into the fatty acid methyl esters commonly used for biodiesel. A design of experiments procedure was used to optimize the monolithic reactor with variables including control of the surface polarity of the monolith via variations in the length of the hydrocarbon chain in alkyl methacrylate monomer, time of grafting of 1-vinyl-4,4-dimethylazlactone used to activate the monolith, and time used for the immobilization of porcine lipase. Optimal conditions involved the use of a poly(stearyl methacrylate-co-ethylene dimethacrylate) monolith, grafted first with vinylazlactone, then treated with lipase for 2 h to carry out the immobilization of the enzyme. Best conditions for the transesterification of glyceryl tributyrate included a temperature of 37°C and a 10 min residence time of the substrate in the bioreactor. The reactor did not lose its activity even after pumping through it a solution of substrate equaling 1,000 reactor volumes. This enzymatic reactor was also used for the transesterification of triacylglycerides from soybean oil to fatty acid methyl esters thus demonstrating the ability of the reactor to produce biodiesel.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Reatores Biológicos / Enzimas Imobilizadas / Biocombustíveis / Lipase Tipo de estudo: Diagnostic_studies Limite: Animals Idioma: En Ano de publicação: 2012 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Reatores Biológicos / Enzimas Imobilizadas / Biocombustíveis / Lipase Tipo de estudo: Diagnostic_studies Limite: Animals Idioma: En Ano de publicação: 2012 Tipo de documento: Article