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]
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机译：通过化学修饰酶和多糖链可以改善辣根过氧化物酶（HRP）在藻酸盐珠粒中的固定。 HRP和藻酸盐被高碘酸盐氧化，然后用乙二胺改性。使用胺化的HRP和高碘酸盐氧化的藻酸盐可获得0.43 U / ml凝胶的最高比活度和81％的结合酶活性。与天然酶相比，固定化酶在80％（v / v）二恶烷中孵育2天后，保留了其原始活性的75％，并且在碱性pH值下具有增强的活性。在间歇反应器中反复使用邻苯三酚氧化过程中，固定的过氧化物酶保留了原始活性的75％。 [Projekat Ministarstva nauke Republike Srbije，br。 ON173017 i br。 [ON172049]
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