Diastase α-amylase Immobilization On Sol-gel Derived Guar Gum-gelatin-silica Nanohybrid
Vandana Singh, Devendra Singh
Volume 5, Issue 1, Page 17-23 | DOI: 10.5185/amlett.2013.7513
Guar gum; gelatin; tetramethoxysilane; sol-gel; amylase; immobilization.
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. Copyright © 2014 VBRI press.