Abstract:
Tannase is an industrially important enzyme that is mainly used in the food, chemical, beverage and pharmaceutical industry. Tannase is responsible for the hydrolysis of ester and depside linkages in tannins to liberate gallic acid and glucose. A study on purification and characterization of tannase from Aspergillus niger was carried out. The enzyme was purified by ethanol precipitation and followed by column chromatography Sepahdex G-75 gel filtration. The enzyme activity obtained was increased from 1.958 U/ml to 2.29 U/ml, respectively after the purification process. SDS-PAGE analysis of purified proteins fraction revealed that their molecular weights are 66 kDa. Effects of temperature, time reaction and pH on the activity of purified tannase were studied. Purified tannase had maximum activity at pH 5 and 6.5, 60°C and 30 minutes with 0.022 U/ml and 0.031 U/ml, 0.32 U/ml and 0.101 U/ml, respectively.
