J. Phys. IV France 07 (1997) C1-671-C1-672
Immobilization of a Neutral Protease in Magnetic Particles Using Direct Binding ProcedureM. Koneracká1, C.N. Ramchand2, R.V. Mehta3 and P. Kopcanský1
1 Institute of Experimental Physics of the Slovak Academy of Sciences, Watsonova 47, 043 53 Kosice, Slovakia
2 Department of Biomedical Sciences, University of Sheffield, Sheffield, U.K.
3 Department of Physics, University of Bhavnagar, Bhavnagar, India
In a recent study we have found that Bovine serum albumine (BSA) can be bound to freshly precipitated magnetic particles directly by a novel procedure. In this procedure BSA linked covalently to the -OH group of Fe3O4 using Carbodiimide. The binding was confirmed by FTIR spectra and electron microscopy. We have also immobilized several enzymes which have biomedical application using this procedure and confirmed the binding by the above mentioned method. In the present experiment we have immobilized Dispase, a neutral protease using the direct binding procedure. 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.
© EDP Sciences 1997