Relative catalytic efficiencies and transcript levels of three d- and two l-lactate dehydrogenases for optically pure d-lactate production in Sporolactobacillus inulinus.

Abstract

As the optical purity of the lactate monomer is pivotal for polymerization, the production of optically pure d‐lactate is of significant importance. Sporolactobacillus inulinus YBS1‐5 is a superior optically pure d‐lactate‐producing bacterium. However, little is known about the relationship between lactate dehydrogenases in S. inulinus YBS1‐5 and the optical purity of d‐lactate. Three potential d‐lactate dehydrogenase (D‐LDH1‐3)‐ and two putative l‐lactate dehydrogenase (L‐LDH1‐2)‐encoding genes were cloned from the YBS1‐5 strain and expressed in Escherichia coli D‐LDH1 exhibited the highest catalytic efficiency toward pyruvate, whereas two L‐LDHs showed low catalytic efficiency. Different neutralizers significantly affected the optical purity of d‐lactate produced by strain YBS1‐5 as well as the transcription levels of ldhDs and ldhLs. The high catalytic efficiency of D‐LDH1 and elevated ldhD1 mRNA levels suggest that this enzyme is essential for d‐lactate synthesis in S. inulinus YBS1‐5. The correlation between the optical purity of d‐lactate and transcription levels of ldhL1 in the case of different neutralizers indicate that ldhL1 is a key factor affecting the optical purity of d‐lactate in S. inulinus YBS1‐5.