LIPASE-CATALYZED SYNTHESIS OF LYSOPHOSPHOLIPIDS IN A CONTINUOUS BIOREACTOR

A novel enzymatic method of lysolecithin synthesis was developed with immobilized lipase as a catalyst. The enzymatic transesterification wa s carried out in a number of alcohols, and the reaction was optimized with regard to the water content and temperature of the medium. Simila r kinetics of transesterification were observed with several individua l phospholipids. The reaction was also performed continuously in a pac ked column bioreactor, which was operated for 1180 h. The lipase displ ayed strict regioselectivity toward sn-1 fatty acid in the phospholipi d molecule, thus yielding exclusively sn-1 lysolecithins as the final product. sn-2 Lysophospholipids were subsequently obtained by acyl mig ration catalyzed by ammonia vapor. Advantages associated with the use of lipases as opposed to conventional, phospholipase-A(2) catalyzed hy drolysis are briefly discussed.