Tannase isolated from Penicillium chrysogenum was purified 24-fold with 18.5% recovery after ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Sephadex G-200 gel filtration. Optimum enzyme activity was recorded at pH 5.0 to 6.0 and at 30 to 40 degrees C. The enzyme was stable up to 30 degrees C and within the pH range of 4.0 to 6.5. The K(m) value was found to be 0.48 x 10 M when tannic acid was used as the substrate. Metal salts at 20 mM inhibited the enzyme to different levels.
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Rajakumar et al. (1983) studied this question.