Abstract: The porcine pancreas lipase (PPLipase) was modified by Tween40, Sucrose ester S970 and Span60 in aqueous solution, and then the Tween40-PPLipase, S970-PPLipase and Span60-PPLipase were used to catalyze the interesterification of camellia and linoleic acid in solvent free system. The results indicated that the acyl incorporation (Ia) was increased with the enzyme loading increasing before the reaction balance reached.The interesterification volecities of the reactions catalyzed by Tween40-PPLipase, Span60-PPLipase and S970-PPLipase were higher than that catalyzed by PPLipase when the enzyme loadings were same. At enzyme load 5% level, the Ia of the interesterifiecation catalyzed by PPLipase was 16.1% at 2h, however the Ias of the interesterification catalyzed by Tween40-PPLipase, Span60-PPLipase and S970-PPLipase were 20.4%, 21.1% and 22.4%, respectively. When the reaction balance reached, the Ias of the interesterifications catalyzed by Tween40-PPLipase, S970-PPLipase, Span60-PPLipase and PPLipase were same roughly, about 25%.