Purification and characterization of gallic acid decarboxylase from Enterobacter spp. isolated from a region in Rajasthan, India

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Purification and characterization of gallic acid decarboxylase from Enterobacter spp. isolated from a region in Rajasthan, India

Manish Soni, Kanti Prakash Sharma, Sanket Kaushik, P. J. John
Int. J. Biosci.2( 12), 97-104, December 2012.
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Abstract

Gallic acid decarboxylase is a gallate dependent enzyme, which catalyses gallic acid to pyrogallol. Pyrogallol has a number of industrial applications. The enzyme produced by Enterobacter spp.isolated from a soil sample collected from a region in Rajasthan, India was purified using DEAE cellulose ion exchange chromatography and Sephadex G-50 gel filtration chromatography. Enterobacter spp. was grown in shake flask broth culture in presence of gallic acid as a substrate to induce gallic acid decarboxylase enzyme. Molecular weight of gallic acid decarboxylase was 57 kDa as determined on SDS PAGE. Enzyme was purified to a fold of 15.32 and a yield of 14.48%. Purified gallic acid decarboxylase had maximum activity at a pH and temperature of 7.0 and 350 C respectively. In presence of Mg2+ but not any other metal ions, enzyme showed more activity. The decline in activity was observed by adding detergents.

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