Enzymatic production of d-3-phenyllactic acid by Pediococcus pentosaceus d-lactate dehydrogenase with NADH regeneration by Ogataea parapolymorpha formate dehydrogenase

Abstract

3-Phenyllactic acid (PLA) is an antimicrobial compound with broad and effective antimicrobial activity against both bacteria and fungi. Enzymatic production of PLA can be carried out from phenylpyruvic acid by lactate dehydrogenase (LDH); however, the enzymatic reaction is accompanied by NADH oxidation that inhibits PLA biotransformation. Here, NADH regeneration was achieved using the formate dehydrogenase from Ogataea parapolymorpha and introduced into the D-PLA production process using the D-LDH from Pediococcus pentosaceus. Optimum PLA production by dual enzyme treatment was at pH 6.0 and 50 °C with both enzymes at 0.4 μM. Using 0.2 mM NADH, D-PLA production by NADH regeneration system reached 5.5 mM, which was significantly higher than that by a single-enzyme reaction.

Characterization of a d‐Lactate Dehydrogenase from Lactobacillus fermentum JN248 with High Phenylpyruvate Reductive Activity

“…d ‐PLA has been further verified based in its effective antimicrobial activity (Dieuleveux and Gueguen ; Dieuleveux and others ; Yu and others ). d ‐PLA can be produced by many microorganisms, especially LAB.…”

Efficient Production of (R)-2-Hydroxy-4-Phenylbutyric Acid by Using a Coupled Reconstructed d-Lactate Dehydrogenase and Formate Dehydrogenase System

“…FDH is a good choice for NADH regeneration in a biocatalysis system because its substrate, formate, has a low cost and its product, carbon dioxide, is easily separated [21]–[25]. In this work, FDH was coexpressed with d -nLDH Y52L/F299Y in E. coli DF and the ( R )-HPBA production capability of the novel biocatalyst was investigated.…”

Reducing 3,4-dihydroxyphenylpyruvic acid tod-3,4-dihydroxyphenyllactic acid via a coenzyme nonspecificd-lactate dehydrogenase fromLactobacillus reuteri

“…d ‐LDH is an NADH‐dependent reductase, and the cofactor NADH is required during substrate reduction (Yu et al . ). However, suitable systems for the regeneration of NADP + are rare: Richter et al .…”

“…The kinetics of D-LDH82319 indicated that it had good affinity for DPA, NADH and NADPH. D-LDH is an NADH-dependent reductase, and the cofactor NADH is required during substrate reduction (Yu et al 2014). However, suitable systems for the regeneration of NADP + are rare: Richter et al (2011) described a structureguided alteration in the cofactor specificity of the L-LDH744 from B. subtilis for regeneration of NADP + .…”