Studies on Fungal Tannase: Part I. Formation, Purification and Catalytic Properties of Tannase of Aspergillus flavus
Studies on Fungal Tannase: Part I. Formation, Purification and Catalytic Properties of Tannase of Aspergillus flavus
复制标题
真菌鞣酸酶的研究：第一部分黄曲霉鞣酸酶的形成、纯化及其催化性能
DOI：
10.1080/00021369.1968.10859194
复制
发表时间：
1968
期刊：
影响因子：
--
通讯作者：
N. Sato
中科院分区：
文献类型：
--
作者：
H. Yamada;O. Adachi;Masahiro Watanabe;N. Sato
在以单宁酸为唯一碳源的培养基上生长的黄曲霉菌丝体中发现了单宁酶。黄曲霉（Aspergillus flavus）在单宁酸培养基上生长，经硫酸铵沉淀、单宁酸沉淀、DEAE-纤维素柱层析、SephadexG-200凝胶过滤和丙酮分级分离，从菌丝体提取物中纯化出单宁酶，纯化倍数约为30倍。该酶在60°C以下稳定，在50 ~ 60 ° C范围内酶活最高。没食子酸甲酯的最佳和稳定的pH范围被认为是在5.0至5.5。黄曲霉单宁酶水解单宁酸的酯键。单宁酸、葡萄糖-1-没食子酸酯和没食子酸甲酯的底物-酶解离常数分别为0.5 × 10 − 4 m、1.4 × 10 − 4 m和8.6 × 10− 4 m。
Tannase was found in the myceĩium of Aspergillus flavus grown on the medium containing tannic acid as a sole carbon source. The enzyme formation might be inducible and was dominant at the initial stage of growth.Tannase was purified about 30-fold from the mycelial extract of Aspergillus flavus grown on the tannic acid medium by a procedure involving ammonium sulfate and tannic acid precipitation, DEAE-cellulose column chromatography, Sephadex G-200 gel filtration and acetone fractionation. The final enzyme preparation showed single symmetric peak upon ultracentrifugation and electrophoresis.The enzyme was stable up to 60°C and showed optimum activity at 50 to 60°C. The optimal and stable pH ranges were found to be at 5.0 to 5.5 for methylgallate. The tannase of Aspergillus flavus hydrolyzed the ester linkages of tannic acid. The substrate- enzyme dissociation constants for substrates were found to be 0.5 × l0−4m, 1.4 × l0−4m and 8.6 × 10−4m for tannic acid, glucose-1-gallate and methylgallate, respectively.