Electrochemical quartz crystal microbalance studies on enzymatic specific activity and direct electrochemistry of immobilized glucose oxidase in the presence of sodium dodecyl benzene sulfonate and multiwalled carbon nanotubes.

The electrochemical quartz crystal microbalance (EQCM) technique was utilized to monitor in situ the adsorption of glucose oxidase (GOD) and the mixture of GOD and sodium dodecyl benzene sulfonate (SDBS) onto Au electrodes with and without modification of multiwalled carbon nanotubes (MWCNTs) or SDBS/MWCNTs composite, and the relationship between enzymatic specific activity (ESA) and direct electrochemistry of the immobilized GOD was quantitatively evaluated for the first time. Compared with the bare gold electrode at which a little GOD was adsorbed and the direct electrochemistry of the adsorbed GOD was negligible, the amount and electroactivity of adsorbed GOD were greatly enhanced when the GOD was mixed with SDBS and then adsorbed onto the SDBS/MWCNTs modified Au electrode. However, the ESA of the adsorbed GOD was fiercely decreased to only 16.1% of the value obtained on the bare gold electrode, and the portion of adsorbed GOD showing electrochemical activity exhibited very low enzymatic activity, demonstrating that the electroactivity and ESA of immobilized GOD responded oppositely to the presence of MWCNTs and SDBS. The ESA results obtained from the EQCM method were well supported by conventional UV-vis spectrophotometry. The direct electrochemistry of redox proteins including enzymes as a function of their biological activities is an important concern in biotechnology, and this work may have presented a new and useful protocol to quantitatively evaluate both the electroactivity and ESA of trace immobilized enzymes, which is expected to find wider applications in biocatalysis and biosensing fields.