Enzymatic transformation in an electrochemical reactor utilizing a redox mediator-modified enzyme electrode for NAD(H) regeneration

A kinetic study of NAD+ reduction on a ruthenium modified glassy carbon electrode

“…However, they did not report the yield of active NADH. Fry et al [7][8][9] have published a series of papers on the reduction of NAD þ to NADH on glassy carbon and vitreous carbon electrodes modified by a layer of immobilized methyl viologen and lipoamide dehydrogenase. They showed that the enzyme catalyzed reduction of NAD þ on such modified electrodes results in the production of enzymatically active NADH, but the amount of active NADH produced was not explicitly reported.…”

Electrochemical reduction of NAD+ on a polycrystalline gold electrode

“…Electrochemical systems using chemically modified [13][14][15][16][17][18] and enzyme-mediated electrodes [19][20][21][22][23][24] have been proposed, and the yield in the active 1,4-NADH produced ranged from ca. 75% on a cholesterolmodified gold-amalgam electrode [13] to ca.…”

Simple Preparation of Diaphorase/Polysiloxane Viologen Polymer Modified Electrode for Sensing NAD and NADH

“…Only a few were focused on the co-immobilization of enzymes and electron mediators. [27][28][29] The present study introduces a very simple coimmobilization method by applying a mixture of polysiloxane viologen polymer (PSV) and diaphorase, followed by the encapsulation with hydrophilic polyurethane polymer. The modified electrode shows good electrocatalytic activities for both NAD + reduction and NADH oxidation.…”

“…[21][22][23][24][25] In most of the system, mediator and DI are dissolved in solution. Only a few were focused on the co-immobilization of enzymes and electron mediators.…”

“…[11][12][13] To overcome the drawbacks, indirect electrochemical regeneration of NADH was developed by using various metal complexes or NAD(H)-accepting oxidoreductase enzymes. [4][5][6]8,[15][16][17][18][19][20][21][22][23][24][25] The enzyme-catalyzed generation systems are of great interest and most frequently studied with formate dehydrogenase, 6,15) glucose-6-phosphate dehydrogenase, 16) lipoamide dehydrogenase, 17) and diaphorase. [18][19][20][21][22][23][24][25] Among them, diaphorase (DI) has been most commonly used because of its thermal stability, insensitivity to dioxygen, and the high rates for enzymatic reaction.…”