The news reporters obtained a quote from the research, "The dependence of the T1 site current maxima on the scan rate was found linear, suggesting a redox process controlled by surface chemistry with the anodic peak potential shifting negatively with the pH over the range from 5.6 to 7.0. The bioelectrocatalytic oxidation of the enzyme substrate L-ascorbate was observed under both aerobic and anaerobic conditions with a current response being more than 3.5 times higher in absence of oxygen than in its presence. Inhibition studies confirmed that the L-ascorbate oxidation results from the bioelectrocatalytic activity of the immobilized AOx. Amperometry carried out at pH = 7.0 and 298 K at a constant potential as low as 150 mV gave the following operational parameters: a detection limit of 1.5 mu M; linear dynamic range up to 4.8 mM and a sensitivity of 2.56 mu A mM(-1) mm(-2) (4.03 mu A mM(-1) mm(-2) at 200 mV). Under these conditions a real sample was assayed with a recovery between 95 and 102%."
According to the news reporters, the research concluded: "The enzyme electrode preserved up to 63% of its initial activity after 8 months storage."
For more information on this research see: Direct Electrochemistry of Ascorbate Oxidase Self-Assembled on Au-Modified Glassy Carbon.
Our news correspondents report that additional information may be obtained by contacting N. Dimcheva, UF Plovdiv,
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