A phosphate buffer containing a mixture of glucose oxidase, acrylic acid derivatives, N,N'-1,2 dihydroxy-ethylene-bis(acrylamide), N,N'-(methylene)-bisacrylamide and surface-modified silica was radically polymerized with (NH4)2S2O8. The polymer formed a thin layer around the silica beads. After sieving of these polymer particles, the surface bound protein was eluted. In rebinding assays and enzyme activity tests a specific binding capacity for glucose oxidase of up to 0.557 microgram GOD/100 mg dry weight of polymer particles could be determined. These polymer particles have the potential to be used as specific separation or detection material.
