Abstract
A commercial xylanase was immobilized on Eudragit L-100 with the recovery activity of 87.3-126.2%. After immobilization, the optimum pH was not changed while its optimum temperature moved from 70 to 75°C. However, the immobilized enzyme did not show a higher thermal stability than the free xylanase. A slightly decrease in the Km values of free enzyme was observed upon immobilization. Meanwhile, Vmax values of the immobilized enzyme were 38% higher than those of the free xylanase. The result of Fluorescence spectroscopy used to probe the changes in the enzyme structure upon immobilization showed minute change and which may result in increase of immobilized enzyme activity. The application of immobilized enzyme hydrolyzing cottonseed husk and corncob pretreated by alkaline peroxide solution was the basically same as the free enzyme. The reusability of immobilized enzyme in the third cycles produced 163 and 126% reducing sugar hydrolyzing cottonseed husk and corncob.
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