Transesterification of castor oil in a solvent-free medium using the lipase from Burkholderia cepacia LTEB11 immobilized on a hydrophobic support

We demonstrate, for the first time, the lipase-catalyzed ethanolysis of castor oil in a solvent-free system. The lipase used was that of Burkholderia cepacia LTEB11, immobilized on Accurel EP 100. With a loading of 4.5% (mass of enzyme preparation in relation to the mass of triacylglycerols in the castor oil) and an ethanol to oil molar ratio of 3:1, 90% conversion of fatty acids to their corresponding ethyl esters was achieved in 6 h. These results are comparable to results reported in the literature for the lipase-catalyzed ethanolysis of castor oil in supercritical CO2 and in systems containing n-hexane as the solvent. Our system has the advantage of being simpler to operate.