ENZYMATIC-HYDROLYSIS OF CHLORAMPHENICOL PALMITATE IN THE PRESENCE OF BETA-CYCLODEXTRIN

The aim of this study was to investigate whether beta-cyclodextrin (be ta-CD) can influence the hydrolysis of chloramphenicol palmitate (CAP) polymorphs by lipase. Polymorph II of CAP is hydrolyzed 37 times fast er by pancreatic lipase than polymorph I. The physical mixture of beta -CD and CAP LI in the molar ratio 1:1 shows a slightly higher hydrolys is rate, but not the physical mixture of beta-CD with CAP I. However, the solid beta-CD/CAP inclusion compound shows an increased hydrolysis rate independently on the polymorph used for its preparation. This co uld be of therapeutic significance, An excess of the hydrolysis produc ts chloramphenicol and palmitic acid, respectively, does not influence the enzy matic hydrolysis of the inclusion compound. The enzymatic hy drolysis rate of CAP II in the physical mixture with beta-CD is increa sed in the presence of palmitic acid compared to the reactions without beta-CD, beta-CD has no catalytic effect on the nonenzymatic hydrolys is of solid or dissolved CAP.