The family of alcohol dehydrogenase (ADH) consists of a class of enzymes that catalyze the oxidation of a wide range of primary and secondary alcohols to aldehydes and ketones. ADH can be obtained from various sources, among them the yeast Saccharomyces cerevisiae, whose cofactor can shows several structures in enzyme structure. In this research project, we intend to use the NAD-dependent ADH (extracted from Saccharomyces cerevisiae) in electrochemical studies for application in bioanodes. The electrochemical system NAD+ /NADH has been considered attractive for both the development of amperometric biosensors, and also for the application in biofuel cells (BFC) bioanodes. For instance, BFC containing ADH NAD-dependent bioanodes are very attractive for ethanol oxidation, since the formal redox potential of the NAD +/NADH is -0.315 V vs. SHE, pH 7.0 at 25 ° C. It is well known that the pathway in which the enzymes are immobilized influences the BFC performance, thus in this work several processes of immobilization of ADH will be investigated, in order to achieve the electron transfer from the enzyme cofactor. Finally, the biocatalytic experimental for ethanol oxidation will be carried out. For the latter, enzymes immobilized on polycrystalline gold electrodes and glassy carbon electrodes will be investigated. For the immobilization of ADH on the electrodes, two main methods will be compared, cross-linking and physical adsorption.
News published in Agência FAPESP Newsletter about the scholarship: