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KMID : 0380619830150040333
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Korean Journal of Food Science and Technology
1983 Volume.15 No. 4 p.333 ~ p.341
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Purification of Acorn Tannin Hydrolyzing Enzyme of Aspergillus sp . AN - 11 and Physiochemical Properties of It
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Abstract
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Tannase of Aspergillus sp. AN-11 isolated from cntaminated acorns was purified by a procedure involving ammonium sulfate precipitation, DEAE-cellulose column chromatography and Sephadex G-200 gel filtration. Physiochemical properties of the purified tannase was investigated. Tannase was purified about 37 folds with the yield of 49% from the culture broth of Aspergillus sp. AN-11. The purified tannase was homogeneous on polyacrylamide gel disc electrophoresis and was dissociable into two identical subunits on SDS-polyacrylamide gel electrophoresis. The molecular weight of the tannase was determined to be 200,000 by gel filtration on Sephadex G-200. The purified tannase showed a typical protein ultraviolet spectrum. The enzyme had a optimum pH 5.5 and optimum temperature at 30 to 40℃. The enzyme was stable at a pH range from 5.0 to 6.5 and at the temperature below 30℃. The enzyme was inactivated remarkably by CuCl₂ and ZnCl₂. The Km value of the enzyme was 7.58×10^(-4) M.
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