Catalytic activity of oxidases hosted in lipidic cubic phases on electrodes.

The monoolein-based liquid crystalline cubic phase was used as the matrix to incorporate redox enzymes--glucose (GOx), pyranose (PyOx) oxidases and laccase. Thin layer of the cubic phase embedding GOx or PyOx activated glucose oxidation in the presence and absence of appropriate mediators. The electrodes exhibited unchanged voltammetric response to glucose for not less than six days. The potentials and ratio of catalytic to diffusion currents could be modified by choosing appropriate electroactive probes as mediators. Ferrocenecarboxylic acid and Ru(NH3)6(2+) provided contact between the electrode and the enzyme. The sensitivity to glucose for glucose oxidase was 0.4+/-0.05, 11+/-3.1 microA/cm2/mM without mediator and with ferrocenecarboxylic acid respectively and 0.9+/-0.06, 31+/-5.6 microA/cm2/mM for pyranose oxidase without and with mediator. The system based on glucose oxidase and Ru(NH3)6(2+) as mediator was found useful due to the most negative potential of the process. The catalyses of oxygen reduction by two laccases: Cerrena unicolor and Trametes hirsuta embedded in the cubic phase together with 2,2'-azino-bis-3-ethylbenzothiazoline-6-sulfonate (ABTS) as the mediator were found efficient and the reduction potential was positive enough to be considered in the application of lyotropic liquid crystals as a material for biofuel cells.