Authors
Abstract
In the present communication, we report on diastase alpha amylase immobilization at guar gum-silica nanohybrid material (H5). The immobilized amylase (H5-Amyl) showed significantly higher bioactivity (21.62 U mg -1 ) as compared to free amylase (15.59 U mg -1 ) in solution at pH 5 and temperature 40°C. The kinetic parameters of the free (Km = 10.66 mg L -1 ; Vmax = 1.36 µmolemL -1 .min -1 ) and the immobilized enzyme (Km = 6.11 mg mL -1 ; Vmax = 1.45 µmolemL -1 .min -1 ) revealed that the immobilization has increased the overall catalytic property of the enzyme. The immobilized enzyme on recycling could show 87% of initial activity even in the sixth cycle. Since immobilization did not hamper the enzymatic reaction rate, the biocatalyst may be suitably exploited in food and pharmaceutical industries.
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