桔青霉单宁酶的分离纯化及部分性质研究
Isolation, Purification, and Some Properties of Penicillium chrysogenum Tannase.
机构信息
Bacteriology Laboratory, Central Leather Research Institute, Madras-600 020, India.
出版信息
Appl Environ Microbiol. 1983 Aug;46(2):525-7. doi: 10.1128/aem.46.2.525-527.1983.
Abstract
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.
摘要
从产黄青霉中分离得到的单宁酶经硫酸铵沉淀、DEAE-纤维素柱层析和 Sephadex G-200 凝胶过滤纯化 24 倍，回收率为 18.5%。最佳酶活在 pH5.0 到 6.0 和 30 到 40 摄氏度下记录。该酶在 30 摄氏度下稳定，在 pH4.0 到 6.5 范围内稳定。当单宁酸作为底物时，K(m)值为 0.48 x 10 M。20mM 的金属盐对酶的抑制程度不同。
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