This technology utilizes a mutant enzyme derived from Pediococcus acidilactici, where the 51st amino acid of D-lactate dehydrogenase is substituted with leucine, methionine, or phenylalanine to enhance substrate affinity for phenylpyruvic acid. The gene containing this mutation, the recombinant vector, and the transformed microorganism expressing it are provided.
D-3-phenyllactic acid is used in food and feed preservatives, pharmaceutical intermediates, and biodegradable bioplastic monomers. However, wild-type D-lactate dehydrogenase has low catalytic activity and affinity for phenylpyruvic acid because its original substrate is pyruvic acid. In whole-cell bioconversion, productivity was limited by competitive inhibition with intracellular pyruvic acid.
By modifying the residue that interacts with the phenyl group at the enzyme's active site, this technology increases catalytic efficiency by up to approximately 138 times compared to the wild type, achieving a conversion rate of over 98% from phenylpyruvic acid to D-3-phenyllactic acid. It can be applied to hydroxy acid production processes for preservatives, pharmaceutical intermediates, and bioplastic monomers, reducing both conversion losses and downstream purification burdens.
This invention was developed with support from the Ministry of Science and ICT's C1 Gas Conversion Technology common research project.
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