Lipase from Candida rugosa was coated with glutamic acid didodecyl ester ribitol amide as catalyst in organic solvents. The surfactant-coated lipase showed considerable activity for the esterification of lauryl alcohol and lauric acid in iso-octane, while almost no activity was observed when the native powder lipase was used. The optimal pH of the buffer used for preparation of the coated lipase was around 7. The optimum reaction temperature was around 30degreesC and the best solvent was iso-octane. The half-life of the coated lipase at 30degreesC was approximate to10 h. The surfactant-coated Candida rugosa lipase was most suitable for catalyzing esterification reactions of fatty acid and fatty alcohol both with a medium chain length. (C) 2002 Elsevier Science Ltd. All rights reserved.