用乳过氧化物酶(LPO)和伴刀豆球蛋白A(Con A)共修饰金电极,首次得到了乳过氧化物酶的直接电化学响应,在此基础上研究了乳过氧化物酶对过氧化氢(H2O2)的电催化活性,并研究了一氧化氮(NO)对LPO电催化活性的影响。在Con A的作用下,乳过氧化物酶在循环伏安图中显示1对准可逆的氧化还原峰,表现出薄层电化学行为。在pH 7.4的磷酸缓冲溶液中的表观氧化还原电位为-190 mV。该共修饰电极对H2O2表现出电催化还原活性,由此构建的传感器对H2O2的检测范围是2.0×10^-5-4.0×10^-3mol/L。实验发现,微摩尔量级的NO会抑制乳过氧化物酶对H2O2的催化活性。
Direct electrochemical behavior of lactoperoxidase(LPO) was firstly obtained by employing a concanavalin A(Con A) and lactoperoxidase co-modified gold electrode.Then the electrocatalytic activity of LPO toward hydrogen peroxide(H2O2) and the influence of nitric oxide(NO) on the electrocatalytic activity of LPO were investigated.With the aid of Con A,LPO displayed a pair of quasi-reversible redox peaks in pH 7.4 phosphate buffer solution with a formal redox potential of-190 mV in cyclic voltammogram(CV) and showed typical thin-layer electrochemical behavior.The co-modified electrode exhibited electrocatalytic activity toward the reduction of H2O2,which was utilized to fabricate a H2O2 biosensor with the detection range of 2.0×10-5^-4.0×10^-3 mol/L.The experimental result also proved that NO showed a suppressive effect on the reduction of H2O2 at the concentration of micro-molar level.