ACTIVITY AND STABILITY STUDIES OF ULTRAFINE NANOENCAPSULATED CATALASEAND PENICILLINASE

The enzymes catalase (bovine liver, EC 1.11.1.6) and alpha-penicillina se (bacillus cereus strain 569, type I, EC 3.5.2.6) were successfully encapsulated in the polyacrylamide matrix. The encapsulation was carri ed out in the water pool of water/aerosol OT/n-hexane reverse micelles . The polymeric particles of encapsulated enzymes were reasonably mono disperse and had diameters in the range of several tens of nanometers as measured from quasi-elastic laser light scattering. The activity-pH profile of the encapsulated enzymes in buffer followed the same patte rn as that of free enzymes. However, the encapsulated enzymes were fou nd to be less active than their free forms. The enzymes in the encapsu lated form were more stable (both thermal stability and shelf-life) as compared to free enzymes. The activity of the encapsulated enzymes wa s found to be dependent on the degree of cross-linking of the polymer matrix. The greater the cross-linking in the matrix, the lesser were t he activity of the encapsulated enzyme.