Lipase-catalyzed transesterification of phosphatidylcholine at controlled water activity
The incorporation of a free fatty acid into the sn-1 position of phosphatidylcholine by lipase-catalyzed transesterification was investigated. The thermodynamic water activity of both the enzyme preparation and the substrate solution was adjusted to the same value prior to the reaction. The reaction rate increased with increasing water activity but the yield of modified phosphatidylcholine decreas
