介孔分子筛上的蛋白质直接电化学

Direct Electron Transfer of Protein Immobilized on Mesoporous Molecular Sieves Matrix

将介孔分子筛用于不同含血红素蛋白质的直接电子传递研究,分别研究了辣根过氧化物酶、血红蛋白和肌红蛋白在六方介孔硅(HMS)上的直接电化学,探讨了介孔分子筛与这些蛋白质间的相互作用,构建了过氧化氢和亚硝酸根的新型的生物传感器.这些工作扩展了HMS在蛋白质固定、直接电子传递研究和无试剂生物传感器制备方面的应用.

The direct electron transfer of different heme proteins immobilized on mesoporous molecular sieves was studied. The direct electrochemistry of horseradish peroxidase (HRP), hemoglobin (Hb) and myoglobin (Mb) immobilized on hexagonal mesoporous silica (HMS) was described, respectively. The immobilized heme proteins at modified glassy carbon electrodes (GCE) showed good direct electrochemical behaviors, which depended on the specific properties of the HMS. Two couples of redox peaks corresponding to the Fe(III) to Fe(II) conversion of the proteins intercalated in the mesopores and adsorbed on the surface of the HMS in 0.1 mol (.) L-1, pH 7.0 PBS(phosphate-buffered saline), respectively, were observed. The amount of proteins intercalated in the mesopores of HMS was proved to be related to the porous size. The result showed the electrode processes to be surface-controlled electrode processes with a single proton transfer. The interactions between proteins and HMS were investigated by using FT-IR, N-2 adsorption isotherms and electrochemical methods, and the new biosensors of hydrogen peroxide (H2O2) and nitrite (NO2-) were constructed. These works extended the application of HMS in immobilizing protein, the direct electron transfer of protein and the construction of reagentless biosensors.