Lactate dehydrogenase synthetic applicability

The successful synthetic application of this electroenzymatic system has first been shown for the in-situ electroenzymatic reduction of pyruvate to D-lactate using the NADH-dependent D-lactate dehydrogenase. Electrolysis at — 0.6 V vs a Ag/AgCl-reference electrode of 50 mL of a 0.1 M tris-HCL buffer of pH 7.5 containing pentamethylcyclopentadienyl-2,2 -bipyridinechloro-rhodium(III) (1 x 10 3 M), NAD+ (2 x 10 3 M), pyruvate (2 x 10 2 M), 1300 units D-lactate dehydrogenase (divided cell, carbon foil electrode) after 3 h resulted in the formation of D-lactate (1.4 x 10 2 M) with an enantiomeric excess of 93.5%. This means that the reaction occurred at a rate of 5 turnovers per hour with respect to the mediator with a 70% turnover of the starting material. The current efficiency was 67% [67],... 

Engineered enzymes have application in the resolution of stereoisomers, especially in the pharmaceutical industry for the preparation of pure isomers of synthetically prepared drugs. For example, lactate dehydrogenase from Bacillus stearothermophilus has been engineered to accept substrates with a long branched side chain, without loss of its stereospecificity (the native enzyme reduces pyruvate to L-lactate). 

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