ACTIVITY AND STABILITY OF BACILLUS-CEREUS PENICILLINASE ENTRAPPED IN AEROSOL OT REVERSE MICELLES

The kinetics of enzyme catalyzed hydrolysis of penicillin G and stabil ity of the enzyme alpha-penicillinase, entrapped in aerosol OT reverse micellar droplets have been investigated spectrophotometrically. Vari ous physical parameters, such as, water pool size (related to W-o), pH and temperature, were optimized for maximum activity of penicillinase in water/aerosol OT/isooctane reverse micelles. The enzyme showed max imum activity of W-o = 14 and pH, 7.0. At any temperature the enzyme w as to be more active in reverse micelles than in aqueous solution. At optimum conditions of W-o, pH and temperature the enzyme was 100% more active in reverse micelles than its maximum activity in aqueous solut ion. In both the systems, the activity starts falling at and above 25 degrees C. CD Spectral studies showed that the enzyme in reverse micel les possesses more helical structure than it has in aqueous solution a nd at the optimum conditions in which it showed maximum activity, the alpha-helicity was also maximum. The enzyme was very stable in reverse micelles at and above room temperature compared to the same in aqueou s solution.