| Abstract: | Hen's egg white lysozyme (EC 3.2.1.17) has been covalently attached to a polystyrene matrix via interaction of protein nucleophiles with an aromatic imidazolide function under anhydrous conditions. The polymer-enzyme complex is prepared in a way which allows nonaqueous solubilization of the complex. The activity of the bound enzyme compares favorably with the activity of the native protein. The pH optima for the matrix-supported protein are shifted toward the basic side. The effect of substrate concentration on rate has been determined. (A preliminary report of this work has been published: G. J. Bartling, H. D. Brown, S. K. Chattopadhyay, Nature 243 , 342–344 (1973).) |
