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BioMed Research International
Volume 2013 (2013), Article ID 596380, 6 pages
Research Article

Purification and Characterization of Tannin Acyl Hydrolase Produced by Mixed Solid State Fermentation of Wheat Bran and Marigold Flower by Penicillium notatum NCIM 923

1Department of Microbiology, Vijaygarh Jyotish Ray College, Kolkata 700032, West Bengal, India
2Department of Food Technology and Biochemical Engineering, Jadavpur University, Kolkata 700032, West Bengal, India

Received 29 April 2013; Accepted 27 September 2013

Academic Editor: Stelvio M. Bandiera

Copyright © 2013 Saswati Gayen and Uma Ghosh. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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. was found to be  M and  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.