Candida rugosa lipase-catalyzed intramolecular O- to N- transacylation of butyryl propranolol in the presence of cyclodextrins.
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-beta-cyclodextrin (HP-beta-CD) is described. Under the used condition, lipase catalyzed the intramolecular transacylation of O-BP into N-butyryl propranolol (N-BP). Propranolol, the product of the expected hydrolysis reaction, was not detected in the reaction medium. A chiral analysis of the reaction product indicated that lipase showed a preference for (R)-O-butyryl propranolol since it first transformed the (R)-enantiomer and then the corresponding (S)-enantiomer. The influence of different reaction conditions on the initial rate is also studied.
Avila-González
Rizette
R
Departamento de Bioquímica y Biología Molecular-A, Facultad de Biología, Universidad de Murcia, Campus de Espinardo, E-30100 Murcia, Spain.
Pérez-Gilabert
Manuela
M
López-López
Miguel A
MA
García-Carmona
Francisco
F
D000215:Acylation; D002175:Candida / Q000201:enzymology*; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D003505:Cyclodextrins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000378:metabolism*; D013058:Mass Spectrometry; D011433:Propranolol / Q000031:analogs & derivatives* / Q000378:metabolism*; D013696:Temperature
D003505:Cyclodextrins; C111856:butyryl propranolol; D011433:Propranolol; D008049:Lipase