Einfluß von Stofftransport und Kinetik immobilisierter Lipasen in heterogenen Stoffsystemen auf Auslegung und Entwicklung von Enzymreaktoren

The solvent-free interesterification of triglycerides with immobilized lipases was studied as a model system of an enzymcatalysed reaction in higher viscous media. An industrial-manufactured 1,3-specific lipase was used to examine engineering parameters for the development of a continuous process. Utilizing specially designed HPLC- and DSC-methods the kinetics of interesterification were determined as function of temperature (52-80 degree C), water content and diameter of the diocatalyst (5-10 % and 100-600 My m, respectively). The kinetics of interesterification can be described by a reversible first order reaction. The amount of one of the products, dimyristoylmonooleyl, passes through a temperature-dependent pseudo-equilibrium. Reaction velocity of hydrolysis (sidereaction of interesterification) is higher as reaction velocity of interesterification. Overall reaction velocity is influenced by internal mass transfer. Pressure drop in continuous interesterification in a fixed bed reac tor is acceptable if the temperature is higher than 60 degree C. External mass transfer and flow through the catalyst bed can be described by model equations.