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 was carried out in a number of alcohols, and the reaction was optimized with regard to the water content and temperature of the medium. Similar kinetics of transesterification were observed with several individual phospholipids. The reaction was also performed continuously in a packed-column bioreactor, which was operated for 1180 h. The lipase displayed strict regio-selectivity towardsn-1 fatty acid in the phospholipid molecule, thus yielding exclusivelysn-1 lysolecithins as the final product.sn-2 Lysophospholipids were subsequently obtained by acyl migration catalyzed by ammonia vapor. Advantages associated with the use of lipases as opposed to conventional, phospholipase-A₂ catalyzed hydrolysis are briefly discussed.