Stevens R A, Levin R E
Appl Environ Microbiol. 1977 May;33(5):1156-61. doi: 10.1128/aem.33.5.1156-1161.1977.
An exocellular inducible alginase from a strain of Alginovibrio aquatilis was purified 61-fold by ammonium sulfate precipitation and column chromatography on Sephadex G-150 and diethylaminoethyl-cellulose. The purified enzyme was more resistant than the crude enzyme to elevated temperatures. The monovalent cations Cs+, Rb+, K+, Na+, and Li+, in order of decreasing enzyme activation, were required for activity. The pH optimum of the purified alginase was 8.0 and its molecular weight from exclusion chromatography on Sephadex G-150 was 110,000.
从一株水生藻胶弧菌中提取的一种胞外诱导型藻胶酶，通过硫酸铵沉淀以及在葡聚糖G - 150和二乙氨基乙基纤维素柱上进行层析，纯化了61倍。纯化后的酶比粗酶更耐高温。该酶的活性需要单价阳离子Cs⁺、Rb⁺、K⁺、Na⁺和Li⁺，其激活酶的能力依次递减。纯化后的藻胶酶最适pH值为8.0，通过葡聚糖G - 150排阻色谱法测得其分子量为110,000。
