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HORSERADISH PEROXIDASE-DEXTRAN COMPLEXES WITH ENHANCED STABILITIES AGAINST TEMPERATURE STORAGE LIFETIME

The optimal methodology to prepare a novel modified enzyme is to develop a polymer-enzyme complex with a high catalytic activity in aqueous solution. The non-covalent complexes were prepared with various molar ratios (n D /n HRP 0,05; 0,1; 1; 5; 10; 15; 20) by using 75kDa dextran and purified enzyme. The thermal stabilities of the obtained conjugates were evaluated with the activities determined at different temperatures (25, 30, 35, 40, 50, 60, 70, 80°C) applying 60 min incubation time for pH 7. The complex with molar ratio n D /n HRP : 10 showed the highest thermal stability. Its activity was very high (ca. 1,5-fold that of pure enzyme), and almost the same without incubation and when applying 1 h incubation time, and could be measured also at 80 °C. We finally succeeded in preparing a dextran-HRP complex which showed higher activity than pure enzyme in aqueos solution at all temperatures for pH 7. In addition, the above complex at pH 7 had very long storage lifetime compared to purified enzyme at +4 °C; which is considered to be a good feature for usage in practice.