CHARACTERIZATION OF ENZYME IMMOBILIZATION IN LIPOSOMES PREPARED FROM PROLIPOSOMES

This study investigated the influence of ionic strength, liposome net charge and enzyme concentration on the immobilization of chymotrypsin in liposomes obtained from proliposomes. Depending on ionic strength a nd chymotrypsin concentration, immobilization efficiencies (IE) as hig h as 96 and 68% were obtained for liposomes prepared with Pro-lipo(R) 3045 S and Pro-lipo(R) 3080 S respectively. Increasing ionic strength and enzyme concentration resulted in a decrease in IE for both types o f liposomes, and this was more pronounced for ionic strength. Relative ly high amounts of chymotrypsin were found to be immobilized on the su rface of the liposomes. Hydrophobic interactions between chymotrypsin and the hydrophobic tails of the phospholipids during liposome formati on were probably responsible for this phenomenon.