Purification and some properties of yeast tannase.

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 6B and Sephadex G–200. The purified tannase was homogeneous on SDS-polyacrylamide 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.