The synthesis of dipeptide AcPheLeuNH2 catalyzed by immobilized pancreatic lipase was carried out in a two- liquid-phase hollow-fiber membrane reactor

operated in a batch mode. Kinetic properties of free and immobilized enzyme

partition behavior between aqueous buffer phase and organic solvent phase

and effective diffusion coefficients of substrates and products through the membrane were investigated respectively. Based on the preliminary experimental results

the performance of the enzyme membrane reactor

which is evaluated by the purity and the yield

is discussed.