Purification and some properties of yeast tannase.
- 1 January 1976
- journal article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 40 (1) , 79-85
- https://doi.org/10.1271/bbb1961.40.79
Abstract
Tannase (tannin acyl hydrolase, EC 3. 1. 1. 20) was purified from the culture broth of Candida sp. by rivanol fractionation and chromatography of columns of ECTEOLA-cellulose, Sepharose 6 B and Sephadex G-200. The purified tannase was homogeneous on SDS-poly-acrylamide gel electrophoresis. The stable pH range of the enzyme was 3.5 to 7.5. The optimum pH was 6.0 for gallotannin as a substrate. The enzyme was stable up to 40°C. The yeast tannase hydrolyzed the ester and depside linkages of tannic acid. The enzyme activity was not influenced by various metal ions and EDTA.Keywords
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