Partial purification of the molybdenum-reducing enzyme from Bacillus pumilus strain Lbna

Lubna Kamil Abdulhussein Abo-Shakeer, M. H. Yakasai, M. F. Rahman, N. A. Bakar, M. Syed, N. Abdullah, A. Othman
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Abstract

Molybdenum is an emerging pollutant. Bioremediation of this heavy metal is possible by the mediation of Mo-reducing bacteria. These bacteria contain the Mo-reducing enzymes that can conver toxic soluble molybdenum into molybdenum blue; a less soluble and less toxic form of the metal. To date only the enzyme has been purified from only one bacterium. The aim of this study is to purify the Mo-reducing enzyme from a previously isolated Mo-reducing bacterium Bacillus pumilus strain Lbna using ammonium sulphate fractionation followed by ion exchange and then gel filtration. Two clear bands were obtained after the gel filtration step with molecular weights of 70 and 100 kDa. This indicates that further additional purification methods need to be used to get a purified fraction. Hence, additional steps of chromatography such as hydroxyapatite or chromatofocusing techniques can be applied in the future.
短小芽孢杆菌Lbna中钼还原酶的部分纯化
钼是一种新兴的污染物。这种重金属的生物修复是可能的调解钼还原细菌。这些细菌含有钼还原酶,可以将有毒的可溶性钼转化为钼蓝;一种不易溶解和毒性较小的金属形式。到目前为止,这种酶只从一种细菌中纯化出来。本研究的目的是利用硫酸铵分馏-离子交换-凝胶过滤,从先前分离的钼还原细菌短芽孢杆菌(Bacillus pumilus)菌株Lbna中纯化钼还原酶。凝胶过滤后得到两条分子量分别为70和100 kDa的清晰条带。这表明需要使用进一步的纯化方法来获得纯化的部分。因此,诸如羟基磷灰石或色谱聚焦技术等色谱的附加步骤可以在未来应用。
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