purification and characterization of tannin acyl hydrolase produced by mixed solid state fermentation of wheat bran and marigold flower by penicillium notatum ncim 923
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2013
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Abstract
Tannin acyl hydrolase produced extracellularly by the fungal strain Penicillium notatum NCIM 923 in mixed solid state fermentation of wheat bran and marigold flower in the ratio 4 : 1 was purified from the cell-free extract broth by ammonium sulphate fractionation followed by diethylaminoethyl-cellulose column chromatography. Tannase was purified by 19.89-fold with yield of 11.77%. The specific activity of crude tannase was found to be 1.31 U/mg protein while that of purified tannase was 22.48 U/mg protein. SDS-PAGE analysis indicated that the enzyme is dimeric with one major band of molecular mass 97 kDa and a very light band of molecular mass 43 kDa. Temperature of 35 to 40°C and pH 5 were optimum for tannase activity. The enzyme retained more than 60% of its stability at 60°C and 40% stability at pH 3 and 8, respectively. Km was found to be 0.33×10-2 M and Vmax=40 U/mg. Since the enzyme is active over a wide range of pH and temperature, it could find potential use in the food processing industry.
| Reference Key |
gayen2013biomedpurification
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| Authors | ;Saswati Gayen;Uma Ghosh |
| Journal | spectrochimica acta - part a: molecular and biomolecular spectroscopy |
| Year | 2013 |
| DOI |
10.1155/2013/596380
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