In the present paper, a novel enzymatic reaction between (
R,
S)
-O-butyryl propranolol(
O-BP) and lipase from
Candida rugosa in the presence of hydroxypropyl-
ges/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-cyclodextrin(HP-
ges/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-CD) is described. Under the used condition, lipase catalyzed the intramoleculartransacylation of
O-BP into
N-butyryl propranolol (
N-BP). Propranolol, the productof the expected hydrolysis reaction, was not detected in the reaction medium. A chiralanalysis of the reaction product indicated that lipase showed a preference for (
R)-
O-butyryl propranolol since it first transformed the (
R)
-enantiomer and then thecorrespondin
g (
S)-enantiomer. The influence of different reaction conditions on theinitial rate is also studied.