Abstract

Biofuel cells are miniature power-generating systems that convert chemical energy to electrical energy by using biocatalysts to catalyze the oxidation of organic substances. Glucose dehydrogenase is an ideal anodic catalyst for biofuel cells because of its high catalytic efficiency, wide substrate specificity and insensitivity to oxygen. It is inherently limited to improve the efficiency of the biofuel cell system by enzyme modifications, immobilizations and electrodes modifications. To overcome these limitations, a powerful anode catalyst is essential. The glucose dehydrogenase in the membrane was washed by 1.5 % Triton X-100. Two types of glucose dehydrogenase in Pseudomonas aeruginosa PAO1 were co-purified by the DEAE sepharose chromatography, and existed in the form of complex. The activity of the glucose dehydrogenase was determined by dye-reduction method during the purification processes. By constant-potential method at 0.35 V and 25 ℃, using Ag/AgCl as a reference, one unit of GDHA and GDHB had a current density of 1814 ?嫀/cm2 and 2748 ?嫀/cm2, respectively. Compared with the current density of glucose oxidase of Aspergillus niger, the glucose dehydrogenase of P. aeruginosa PAO1 was a potential anodic catalyst in biofuel cell system.

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