Application of immobilized lipases for the interesterification of lipids

The lipase-catalyzed interesterification has advantages over chemical processes which use alkali metals because a 1,3-regioselective interesterification can be performed. The important engineering parameters for the design of a solvent-free continuous process were examined. An industrial-manufactured immobilized 1,3-specific lipase (Lipozyme high TM. NOVO, Kopenhagen) was used. Olive oil and olive oil/trimyristine mixtures were chosen as model system. The influence of temperature, water content, and internal mass transfer on the reaction rate of the lipase-catalyzed reactions (interesterification and hydrolysis) were examined in thermostated stirred-tank reactors. Continuous interesterification was performed in fixed-bed reactors. The effect of external mass transport limitations on the reacton rate was studied. The pressure drop across the biocatalyst bed was determined as a function of temperature, flow rate, height of the catalyst bed, and reactor diameter. The results show that the continuous interesterification with Lipozyme high TM in a solvent-free process can be performed at temperatures between 60 and 70 degree C