Relative catalytic efficiencies and transcript levels of three <scp>d</scp>‐ and two <scp>l</scp>‐lactate dehydrogenases for optically pure <scp>d</scp>‐lactate production in <i>Sporolactobacillus inulinus</i>

Wu, Bin; Yu, Qi; Zheng, Shan; Pedroso, Marcelo Monteiro; Guddat, Luke W.; He, Bingfang

doi:10.1002/mbo3.704

Cited by 5 publications

(4 citation statements)

References 48 publications

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“…These results were similar to those reported in previous studies on the transcriptional analysis of genes encoding LDHs in S. inulinus . They confirmed that the optical purity of d -lactic acid was regulated by the catalytic efficiency of D-LDH and transcriptional levels of ldh D-encoding genes, which correlated with different neutralizing agents 35 . Although the relative catalytic efficiency of the enzymes responsible for the optical purity of lactic acid produced by Sporolactobacillus strains is poorly understood, the regulation of lactate racemization activity at the transcription level has been reported in four Lactobacillus strains 11 .…”

Section: Resultsmentioning

confidence: 70%

“…In previous reports on S. inulinus YBS1-5, D-LDH activity was induced by Ca 2+ but slightly inhibited by Mg 2+ , whereas L-LDH activity was inhibited by Ca 2+ but induced by Mg 2+ . Additionally, LDH activity was not affected by Na + or K + 35 . Jia et al reported that D-LDH activity of Leuconostoc mesenteroides was slightly enhanced by K + but not by Mg 2+ , and fructose 1,6-biophosphate did not influence the enzymatic activity, indicating that D-LDH does not contain an allosteric site, similar to the structure of D-LDH from Fusobacterium nucleatum and Pseudomonas aeruginosa 29 .…”

Section: Resultsmentioning

confidence: 84%

“…The L- and D-LDH enzymes are encoded by ldh L and ldh D, respectively. However, although the enzyme lactate racemase responsible for the interconversion of lactate isomers has been reported in a few Lactobacillus strains, studies on the transcriptional level of this enzyme in Sporolactobacillus strains are scarce 11 , 35 . In our previous study, genome sequence annotation of S. terrae SBT-1 revealed two L-LDH-encoding genes ( hic D1 and ldh 3), three D-LDH-encoding genes ( ldh A1, ldh A_1, and ldh A_2), and a lactate racemase-encoding gene ( lar A) 13 .…”

Section: Resultsmentioning

confidence: 99%

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Association between organic nitrogen substrates and the optical purity of d-lactic acid during the fermentation by Sporolactobacillus terrae SBT-1

Thitiprasert,

Jaiaue,

Amornbunchai

et al. 2024

Sci Rep

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The development of biotechnological lactic acid production has attracted attention to the potential production of an optically pure isomer of lactic acid, although the relationship between fermentation and the biosynthesis of highly optically pure d-lactic acid remains poorly understood. Sporolactobacillus terrae SBT-1 is an excellent d-lactic acid producer that depends on cultivation conditions. Herein, three enzymes responsible for synthesizing optically pure d-lactic acid, including d-lactate dehydrogenase (D-LDH; encoded by ldhDs), l-lactate dehydrogenase (L-LDH; encoded by ldhLs), and lactate racemase (Lar; encoded by larA), were quantified under different organic nitrogen sources and concentration to study the relationship between fermentation conditions and synthesis pathway of optically pure lactic acid. Different organic nitrogen sources and concentrations significantly affected the quantity and quality of d-lactic acid produced by strain SBT-1 as well as the synthetic optically pure lactic acid pathway. Yeast extract is a preferred organic nitrogen source for achieving high catalytic efficiency of d-lactate dehydrogenase and increasing the transcription level of ldhA2, indicating that this enzyme plays a major role in d-lactic acid formation in S. terrae SBT-1. Furthermore, lactate racemization activity could be regulated by the presence of d-lactic acid. The results of this study suggest that specific nutrient requirements are necessary to achieve a stable and highly productive fermentation process for the d-lactic acid of an individual strain.

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Section: Resultsmentioning

confidence: 70%

Section: Resultsmentioning

confidence: 84%

Section: Resultsmentioning

confidence: 99%

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Association between organic nitrogen substrates and the optical purity of d-lactic acid during the fermentation by Sporolactobacillus terrae SBT-1

Thitiprasert,

Jaiaue,

Amornbunchai

et al. 2024

Sci Rep

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“…Recently, S. inulinus has attracted the attention of researchers due to its superior productivity of D‐lactate (>180 g L −1 ) with high optical purity (Reddy Tadi et al, 2017 ; Zhao et al, 2014 ). Wu et al ( 2019 ) reported that three D‐LDHs and two L‐LDHs exist in the chromosome of S. inulinus CASD and that these enzymes have different activities for pyruvate reduction. Meanwhile, a D‐lactate dehydrogenase named DLDH744 from S. inulinus CASD was found to have sufficient enzymatic activity to produce PLA with low efficiency ( k cat /Km as 1.49 ± 0.076 mM −1 s −1 ; Wang et al, 2016 ).…”

Section: Introductionmentioning

confidence: 99%

Biological characterization of D‐lactate dehydrogenase responsible for high‐yield production of D‐phenyllactic acid in Sporolactobacillus inulinus

Park

Seong

Kim

et al. 2022

Microbial Biotechnology

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PLA (3‐D‐phenyllactic acid) is an ideal antimicrobial and immune regulatory compound present in honey and fermented foods. Sporolactobacillus inulinus is regarded as a potent D‐PLA producer that reduces phenylpyruvate (PPA) with D‐lactate dehydrogenases. In this study, PLA was produced by whole‐cell bioconversion of S. inulinus ATCC 15538. Three genes encoding D‐lactate dehydrogenase (d‐ldh1, d‐ldh2, and d‐ldh3) were cloned and expressed in Escherichia coli BL21 (DE3), and their biochemical and structural properties were characterized. Consequently, a high concentration of pure D‐PLA (47 mM) was produced with a high conversion yield of 88%. Among the three enzymes, D‐LDH1 was responsible for the efficient conversion of PPA to PLA with kinetic parameters of Km (0.36 mM), kcat (481.10 s−1), and kcat/Km (1336.39 mM−1 s−1). In silico structural analysis and site‐directed mutagenesis revealed that the Ile307 in D‐LDH1 is a key residue for excellent PPA reduction with low steric hindrance at the substrate entrance. This study highlights that S. inulinus ATCC 15538 is an excellent PLA producer, equipped with a highly specific and efficient D‐LDH1 enzyme.

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l-Lactate dehydrogenase from Cyanidioschyzon merolae shows high catalytic efficiency for pyruvate reduction and is inhibited by ATP

Yamamoto,

Osanai,

Ito

2024

Plant Mol Biol

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Abstractl-Lactate is a commodity chemical used in various fields. Microorganisms have produced l-lactate via lactic fermentation using saccharides derived from crops as carbon sources. Recently, l-lactate production using microalgae, whose carbon source is carbon dioxide, has been spotlighted because the prices of the crops have increased. A red alga Cyanidioschyzon merolae produce l-lactate via lactic fermentation under dark anaerobic conditions. The l-lactate titer of C. merolae is higher than those of other microalgae but lower than those of heterotrophic bacteria. Therefore, an increase in the l-lactate titer is required in C. merolae. l-Lactate dehydrogenase (l-LDH) catalyzes the reduction of pyruvate to l-lactate during lactic fermentation. C. merolae possesses five isozymes of l-LDH. The results of previous transcriptome analysis suggested that l-LDHs are the key enzymes in the lactic fermentation of C. merolae. However, their biochemical characteristics, such as catalytic efficiency and tolerance for metabolites, have not been revealed. We compared the amino acid sequences of C. merolael-LDHs (CmLDHs) and characterized one of the isozymes, CmLDH1. BLAST analysis revealed that the sequence similarities of CmLDH1 and the other isozymes were above 99%. The catalytic efficiency of CmLDH1 under its optimum conditions was higher than those of l-LDHs of other organisms. ATP decreased the affinity and turnover number of CmLDH1 for NADH. These findings contribute to understanding the characteristics of l-LDHs of microalgae and the regulatory mechanisms of lactic fermentation in C. merolae.

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

Cited by 5 publications

References 48 publications

Association between organic nitrogen substrates and the optical purity of d-lactic acid during the fermentation by Sporolactobacillus terrae SBT-1

Association between organic nitrogen substrates and the optical purity of d-lactic acid during the fermentation by Sporolactobacillus terrae SBT-1

Biological characterization of D‐lactate dehydrogenase responsible for high‐yield production of D‐phenyllactic acid in Sporolactobacillus inulinus

l-Lactate dehydrogenase from Cyanidioschyzon merolae shows high catalytic efficiency for pyruvate reduction and is inhibited by ATP

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