In the absence of oxygen, E. coli relies on fermentative pathways to generate energy. One of the key pathways involves the reduction of pyruvate to lactate by lactate dehydrogenase. The NAD-dependent D-lactate dehydrogenase specifically catalyzes the conversion of pyruvate to D-lactate, using NADH as a cofactor, which is oxidized to NAD+ in the process. This reaction is vital for maintaining the redox balance within the cell and ensuring a continuous supply of NAD+ for glycolysis.
The recombinant production of D-lactate dehydrogenase in E. coli involves the insertion of the gene encoding this enzyme into the bacterial genome or a plasmid vector. This genetic modification allows for the overexpression of the enzyme, facilitating its study and potential industrial applications. Recombinant E. coli strains engineered to overproduce D-LDH can be used in various biotechnological processes, including the production of D-lactic acid, which is a valuable chemical in the food, pharmaceutical, and polymer industries .
While the recombinant production of D-LDH in E. coli has shown promise, there are several challenges that need to be addressed:
Future research efforts are focused on addressing these challenges and exploring new applications for D-lactic acid and other products derived from recombinant E. coli strains. Advances in metabolic engineering, synthetic biology, and fermentation technology will play a crucial role in realizing the full potential of these biotechnological innovations .