| Abstract: | Lysozyme immobilized on polyacrylamide beads or cellulose fibers is found to retain activity for hydrolysis of the cell walls of Micrococcus lysodeikticus. The immobilization on cellulose is somewhat reversible; the polyacrylamide immobilized lysozyme does not release any enzyme upon washing as evidenced by UV and lytic activity tests. The specific catalytic activity of the lysozyme-polyacrylamide system is found to decline as the density of derivatized surface groups is increased; a model of protein deactivation due to excess surface coupling is presented as a possible rationale for such specific activity variations. |
