Immobilization of chemically modified horse radish peroxidase within activated alginate beads

Immobilization of horse radish peroxidase (HRP) within alginate beads was improved by chemical modification of the enzyme and polysaccharide chains. HRP and alginate were oxidized by periodate and subsequently modified with ethylenediamine. Highest specific activity of 0.43 U/ml of gel and 81 % of bound enzyme activity was obtained using aminated HRP and alginate oxidized by periodate. Immobilized enzyme retained 75 % of original activity after 2 days of incubation in 80 % (v/v) dioxane and had increased activity at basic pH values compared to native enzyme. During repeated use in batch reactor for pyrogallol oxidation immobilized peroxidase retained 75 % of original activity. [Projekat Ministarstva nauke Republike Srbije, br. ON173017 i br. ON172049