Characterization of a d-Lactate Dehydrogenase from Lactobacillus fermentum JN248 with High Phenylpyruvate Reductive...

Phenyllactic acid (PLA) is a novel antimicrobial compound. A novel NADH-dependent d-lactate dehydrogenase (d-LDH), named as LF-d-LDH0653, with high phenylpyruvate (PPA) reducing activity was isolated from Lactobacillus fermentum JN248. Its optimum pH and temperature were 8.0 and 50 °C, respectively. The Michaelis-Menten constant (K_m ), turnover number (k_cat ), and catalytic efficiency (k_cat /K_m ) for NADH were 1.20 mmol/L, 67.39 s^-1 , and 56.16 (mmol/L)^-1 s^-1 , respectively. The (K_m ), (k_cat ), and (k_cat /K_m ) for phenylpyruvate were 1.68 mmol/L, 122.66 s^-1 , and 73.01 (mmol/L)^-1 s^-1 , respectively. This enzyme can catalyze phenylpyruvate and the product presented excellent optical purity (enantioselectivity >99%). The results suggest that LF-d-LDH0653 is a promising biocatalyst for the efficient synthesis of optically pure d-PLA.

A novel d-LDH with phenylpyruvate reducing activity has been isolated and identified. It could be used as a reference for improving the production of optically pure d-PLA. d-PLA has a potential for application as antimicrobial an agent in dairy industry and baking industry, pharmaceutical agent in medicine and cosmetics.