Immobilized lipase (Candida Antarctica lipase, CAL) efยฎciently catalyzes the transesteri-ยฎcation and amidation of the racemic ferrocenes, 1-hydroxyethylferrocene, (AE)-1, 1-hydroxy 3 ferrocenophane, (AE)-4, 1-amonoethylferrocene, (AE)-2, and 1-amono 3 ferrocenophane, (AE)-5, with acyl esters, resulting in the formation of R products possessing high enantiomeric purity. When 1hydroxyethylferrocene, (AE)-1, and 1-hydroxy 3 ferrocenophane, (AE)-4, was used as substrate diisopropyl ether was a suitable solvent. In the reaction conditions investigated, the use of vinyl acetate in diisopropyl ether gave the best yield of (R)-1a (49%, 99% ee) after 2 h of incubation at 30 ยฐC. But, with the amino ferrocenes, 1-amonoethylferrocene, (AE)-2, and 1-amono3 ferrocenophane, (AE)-5, as substrate, diisopropyl ether was unsuitable as a solvent owing to the low solubility of the substrate in this solvent. Using tetrahydrofuran as a solvent, enzymatic amidation of 1-amonoethylferrocene, (AE)-2, gave the best yield of (R)-2a (21%, 99% ee) after 120 h of incubation at 30 ยฐC. CAL working in organic solvent is able to efยฎciently carry out the resolution of ferrocenyl alcohol and amine derivatives which have similar structures, such as (AE)-1 and (AE)-2, (AE)-4 and (AE)-5 which possess central chirality. This enzyme accepted only non-bulky primary alcohols and amines as ferrocenyl substrates.