Modified Candida rugosa lipase was co-lyophilized with two gemini-type amphiphiles, L- and D-2-(3-{bis-[3(2, 3, 4, 5, 6-pentahydroxy-hexanoylamino)-propyl]-carbamoyl}-propionylamino)-pentanedioic acid didodecyl ester or dodecanoic acid 2-[(3-{bis-[ 3-( 2,3,4, 5,6- pentahydroxy-hexanoylamino)-propyl]-carbamoyl}-propionyl)-(2-dodecanoyloxy- ethyl)- amino]- ethyl ester. Enzymatic activities of the modified lipases in the transesterification between racemic 2,2-dimethyl-1,3-dioxolane-4-methanol and vinyl butyrate in cyclohexane were enhanced as much as by 37-78, 1.5-5- and 41-83-fold of magnitude relative to that of native enzyme, respectively. The lack of significant enhancement of the enzymatic activity, only in the case of the D-isomeric amphiphile-modified lipase, was considered from the topological view of the amphiphile.