Diastase α-amylase immobilization on sol-gel derived guar gum-gelatin-silica nanohybrid

Vandana Singh*, Devendra Singh

Department of chemistry, University of Allahabad, Allahabad 211002, India  

Adv. Mater. Lett., 2014, 5 (1), pp 17-23

DOI: 10.5185/amlett.2013.7513

Publication Date (Web): Dec 28, 2013

E-mail: vschemau@gmail.com


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.


Guar gum, gelatin, tetramethoxysilane, sol-gel, amylase, immobilization.

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