Beschreibung:
<jats:title>Abstract</jats:title><jats:p>Horseradish peroxidase was immobilized onto crosslinked acrylamide beads after a pretreatment of the enzyme with glycidyl‐methacrylate. The enzyme initiates the polymerization of the acrylic comonomers. The activity of the solid materials increases by increasing the amount of glycidyl‐methacrylate and the time of reaction between the vinyl monomer and the enzyme, while it is not greatly influenced by the concentration of the acrylamides.</jats:p><jats:p>The beads obtained showed little dependence on diffusion; the K<jats:sub>m</jats:sub> values using guaiacol and H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> as substrates were the same as for free peroxidase.</jats:p><jats:p>No decrease in stability was observed after 150h storage at room temperature or after freeze‐drying.</jats:p><jats:p>By continuous flow measurements, using guaiacol or iodide as cosubstrate, a different adsorption of the reaction products was found.</jats:p>