Monday, May 5, 2008
12-11

Stability of lipases in supercritical CO2 for Biodiesel Production by Ethanolysis of Castor Oil

Priscilla F.F. Amaral1, Ana Iraidy Santa Brigida2, Diego S. Pinto1, Pedro W. Falcão3, Luciana R. B. Goncalves2, Maria Alice Z. Coelho1, and Fernando L.P. Pessoa3. (1) Biochemical Engineering Department, Universidade Federal do Rio de Janeiro, CT, Bl. E, Cidade Universitária, 21949-900, Rio de janeiro, Brazil, (2) Chemical Engineering, Universidade Federal do Ceará, Campus do Pici, Bloco 709, Fortaleza, Brazil, (3) Chemical Engineering Department, Universidade Federal do Rio de Janeiro, CT, Bl. E, Cidade Universitária, 21949-900, Rio de janeiro, Brazil

Biodiesel (fatty acid alkyl esters) have drawn attention in the last decade as a renewable, biodegradable, and nontoxic fuel. It is an alcohol ester product from the transesterification of triglycerides in vegetable oils or animal fats. This can be accomplished by reacting lower alcohols such as methanol or ethanol with triglycerides. Chemical processes give high conversion of triacylglycerols to their corresponding alkyl esters in short reaction times but have drawbacks such as being energy intensive, difficult glycerol recovery, difficult removal of alkaline catalyst from the product and treatment of alkaline wastewater, and the interference of the reaction by free fatty acids and water. Enzymatic methods may overcome these problems. In the present work three different lipases (CALB immobilized in coconut fiber by adsorption, Novozyme 435, Lipozyme TL IM) were screened for a potential application in transesterification reaction in supercritical CO2 (SCCO2). SCCO2 has several advantages such as high solute diffusivities and low viscosity, which can accelerate mass transfer-limited enzymatic. We have studied the stability of the immobilized enzymes in the ethanolysis of castor oil (Ricinus comunis) in SCCO2 and the influence of important parameters such as pressure, temperature and water content

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