Tannin acyl hydrolase produced extra-cellularly by Aspergillus niger in solid state fermentation of Rice husk. The enzyme was purified from the cell-free extract by ammonium sulphate precipitation followed by diethylaminoethyl-cellulose column chromatography. The protein content of crude and purified was found to be 7•6 and 0•45 mg/ml respectively. The specific activity of crude tannase was found to be 28•5 U/mg of protein while that of purified tannase was 173•0 U/mg of protein. The optimum temperature and pH of the crude sample was analysed and found to be 35 to 40 ºC and pH 5 respectively. The enzyme obtained was applied for declarification of pomegranate juice. In the declarification of fruit juice, a 56% decrease in tannin content was observed after 2 h of incubation at 37 ºC with 1 ml of purified tannase (173 U/mg).