Ferreyra Nancy F, Solís Velia M
INFIQC, Departamento de Físico Química, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Pabellón Argentina, Ciudad Universitaria, Cordoba 5000, Argentina.
Bioelectrochemistry. 2004 Aug;64(1):61-70. doi: 10.1016/j.bioelechem.2003.12.012.
The enzyme-catalysed reduction of nitrate was studied utilising Aspergillus niger nitrate reductase (NR) and phenosafranin in solution as the enzyme regenerator, working at lower potentials than that of the more common methyl viologen mediator. Cyclic voltammograms when enzyme, phenosafranin and substrate were together put in evidence the enzyme-catalysed reduction of nitrate, although with a relatively slow kinetics. From slope values not dependent on mediator concentration, the apparent Michaelis-Menten constant was evaluated. Analytical parameters for the enzyme-modified electrode in the presence of phenosafranin for the determination of nitrate content in water were assessed, including a recovery assay for nitrate added to a river water sample. The stability of the electrode was checked.
利用黑曲霉硝酸还原酶（NR）和溶液中的酚藏花红作为酶再生剂，研究了酶催化的硝酸盐还原反应，其工作电位低于更常用的甲基紫精介质。当酶、酚藏花红和底物一起存在时的循环伏安图证明了酶催化的硝酸盐还原反应，尽管动力学相对较慢。根据不依赖于介质浓度的斜率值，评估了表观米氏常数。评估了在酚藏花红存在下用于测定水中硝酸盐含量的酶修饰电极的分析参数，包括对添加到河水样品中的硝酸盐的回收率测定。检查了电极的稳定性。
