IMMOBILIZATION OF A NEUTRAL PROTEASE IN MAGNETIC PARTICLES USING DIRECT BINDING PROCEDURE

In a recent study we have found that Bovine serum albumine (BSA) lan b e bound to freshly precipitated magnetic particles directly by a novel procedure. In this procedure BSA linked covalently to the -OH group o f Fe3O4 using Carbodiimide. The binding was confirmed by FTIR spectra and electron microscopy. We have also immobilized several enzymes whic h have biomedical application using this procedure and confirmed the b inding by the above mentioned method. In the present experiment we hav e immobilized Dispase, a neutral protease using the direct binding pro cedure. We have found that the protein was bound to the extend of 90% using the dye binding procedure. We have measured the activity of this enzyme by its proteolytic property and showed that it retained 80% of its activity after immobilization.