Synthesis of Oleyl Oleate with Immobilized Lipase from Mucor miehei

The synthesis of oleyl oleate with immobilized 1,3-specific lipase from Mucor miehei is presented in this article. Oleyl alcohol was esterified with oleic acid in the presence of a Mucor miehei lipase (lipozyme^IM) to obtain oleyl oleate. The effects of various temperatures and various enzyme/substrate ratios have been investigated to determine optimal conditions for the esterification process. The highest conversion of oleic acid 86.9 % was obtained at 50°C. The optimal addition of lipase to substrates was determined to be 0.1 g per gram of reaction mixture. The esterification can be modeled successfully as a reverse second-order reaction. Thermodynamic properties of the reaction system at 50°C were also determined. Activation energy was 14.65 kJ/mol, entropy of activation –0.8 J/mol·K and free energy of activation was 98.568 kJ/mol.