利用放射性同位素研究来自 Pyrococcus furiosus 的耐热铁蛋白酶对磷酸盐和砷酸盐的去除效率。
Phosphate and arsenate removal efficiency by thermostable ferritin enzyme from Pyrococcus furiosus using radioisotopes.
机构信息
Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands; Department of Radiation, Radionuclides and Reactors, Delft University of Technology, Mekelweg 15, 2629 JB Delft, The Netherlands; BiAqua B.V., Schipholweg 275, 1171 PK Badhoevedorp, The Netherlands.
BiAqua B.V., Schipholweg 275, 1171 PK Badhoevedorp, The Netherlands.
出版信息
Water Res. 2015 Jun 1;76:181-6. doi: 10.1016/j.watres.2015.02.054. Epub 2015 Mar 13.
Oxo-anion binding properties of the thermostable enzyme ferritin from Pyrococcus furiosus were characterized with radiography. Radioisotopes (32)P and (76)As present as oxoanions were used to measure the extent and the rate of their absorption by the ferritin. Thermostable ferritin proved to be an excellent system for rapid phosphate and arsenate removal from aqueous solutions down to residual concentrations at the picomolar level. These very low concentrations make thermostable ferritin a potential tool to considerably mitigate industrial biofouling by phosphate limitation or to remove arsenate from drinking water.
应用放射性技术研究了来自 Pyrococcus furiosus 的耐热铁蛋白的氧阴离子结合特性。将放射性同位素 (32)P 和 (76)As 作为氧阴离子用于测量它们被铁蛋白吸收的程度和速率。耐热铁蛋白被证明是一种极好的系统，可从水溶液中快速去除磷酸盐和砷酸盐，残留浓度低至皮摩尔级。这些非常低的浓度使耐热铁蛋白成为一种有潜力的工具，可以显著减轻磷酸盐限制引起的工业生物污垢，或从饮用水中去除砷酸盐。
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