scholarly journals Cloning of d-lactate dehydrogenase genes of Lactobacillus delbrueckii subsp. bulgaricus and their roles in d-lactic acid production

3 Biotech ◽  
2017 ◽  
Vol 7 (3) ◽  
Author(s):  
Yanna Huang ◽  
Chunping You ◽  
Zhenmin Liu
Keyword(s):  
Lactic Acid ◽  
Lactate Dehydrogenase ◽  
Acid Production ◽  
Lactic Acid Production ◽  
Lactobacillus Delbrueckii ◽  
Lactobacillus Delbrueckii Subsp

scholarly journals Major Role of NAD-Dependent Lactate Dehydrogenases in the Production of l-Lactic Acid with High Optical Purity by the Thermophile Bacillus coagulans

2014 ◽  
Vol 80 (23) ◽  
pp. 7134-7141 ◽  
Author(s):  
Limin Wang ◽  
Yumeng Cai ◽  
Lingfeng Zhu ◽  
Honglian Guo ◽  
Bo Yu
Keyword(s):  
Lactic Acid ◽  
Lactate Dehydrogenase ◽  
Acid Production ◽  
Lactic Acid Production ◽  
Optical Purity ◽  
Bacillus Coagulans ◽  
Lactobacillus Delbrueckii ◽  
Content Type ◽  
High Optical Purity ◽  
Optically Pure

ABSTRACTBacillus coagulans2-6 is an excellent producer of optically purel-lactic acid. However, little is known about the mechanism of synthesis of the highly optically purel-lactic acid produced by this strain. Three enzymes responsible for lactic acid production—NAD-dependentl-lactate dehydrogenase (l-nLDH; encoded byldhL), NAD-dependentd-lactate dehydrogenase (d-nLDH; encoded byldhD), and glycolate oxidase (GOX)—were systematically investigated in order to study the relationship between these enzymes and the optical purity of lactic acid.Lactobacillus delbrueckiisubsp.bulgaricusDSM 20081 (ad-lactic acid producer) andLactobacillus plantarumsubsp.plantarumDSM 20174 (adl-lactic acid producer) were also examined in this study as comparative strains, in addition toB. coagulans. The specific activities of key enzymes for lactic acid production in the three strains were characterizedin vivoandin vitro, and the levels of transcription of theldhL,ldhD, and GOX genes during fermentation were also analyzed. The catalytic activities ofl-nLDH andd-nLDH were different inl-,d-, anddl-lactic acid producers. Onlyl-nLDH activity was detected inB. coagulans2-6 under native conditions, and the level of transcription ofldhLinB. coagulans2-6 was much higher than that ofldhDor the GOX gene at all growth phases. However, for the twoLactobacillusstrains used in this study,ldhDtranscription levels were higher than those ofldhL. The high catalytic efficiency ofl-nLDH toward pyruvate and the high transcription ratios ofldhLtoldhDandldhLto the GOX gene provide the key explanations for the high optical purity ofl-lactic acid produced byB. coagulans2-6.

Continuous d-lactic acid production by a novelthermotolerant Lactobacillus delbrueckii subsp. lactis QU 41

2010 ◽  
Vol 89 (6) ◽  
pp. 1741-1750 ◽  
Author(s):  
Yukihiro Tashiro ◽  
Wataru Kaneko ◽  
Yanqi Sun ◽  
Keisuke Shibata ◽  
Kentaro Inokuma ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Acid Production ◽  
Lactic Acid Production ◽  
Lactobacillus Delbrueckii ◽  
Lactobacillus Delbrueckii Subsp

scholarly journals Production of biopolymer precursors beta-alanine and L-lactic acid from CO2 with metabolically versatile Rhodococcus opacus DSM 43205

2020 ◽  
Author(s):  
Laura Salusjärvi ◽  
Leo Ojala ◽  
Gopal Peddinti ◽  
Michael Lienemann ◽  
Paula Jouhten ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Metabolic Engineering ◽  
Lactate Dehydrogenase ◽  
Acid Production ◽  
Lactic Acid Production ◽  
Water Electrolysis ◽  
Rhodococcus Opacus ◽  
Beta Alanine ◽  
Polymer Precursors ◽  
Autotrophic Bacteria

AbstractHydrogen oxidizing autotrophic bacteria are promising hosts for CO2 conversion into chemicals. In this work, we engineered the metabolically versatile lithoautotrophic bacterium Rhodococcus opacus strain DSM 43205 for synthesis of polymer precursors. Aspartate decarboxylase (panD) or lactate dehydrogenase (ldh) were expressed for beta-alanine or L-lactic acid production, respectively. The heterotrophic cultivations on glucose produced 25 mg L-1 beta-alanine and 742 mg L-1 L-lactic acid, while autotrophic cultivations with CO2, H2 and O2 resulted in the production of 1.8 mg L-1 beta-alanine and 146 mg L-1 L-lactic acid. Beta-alanine was also produced at 345 µg L-1 from CO2 in electrobioreactors, where H2 and O2 were provided by water electrolysis. This work demonstrates that R. opacus DSM 43205 can be readily engineered to produce chemicals from CO2 and provides base for its further metabolic engineering.

scholarly journals Efficient Production of l-Lactic Acid by Metabolically Engineered Saccharomyces cerevisiae with a Genome-Integrated l-Lactate Dehydrogenase Gene

2005 ◽  
Vol 71 (4) ◽  
pp. 1964-1970 ◽  
Author(s):  
Nobuhiro Ishida ◽  
Satoshi Saitoh ◽  
Kenro Tokuhiro ◽  
Eiji Nagamori ◽  
Takashi Matsuyama ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactate Dehydrogenase ◽  
Acid Production ◽  
Lactic Acid Production ◽  
Bifidobacterium Longum ◽  
Yeast Cells ◽  
Efficient Production ◽  
Coding Region ◽  
A Genome ◽  
Dehydrogenase Gene

ABSTRACT We developed a metabolically engineered yeast which produces lactic acid efficiently. In this recombinant strain, the coding region for pyruvate decarboxylase 1 (PDC1) on chromosome XII is substituted for that of the l-lactate dehydrogenase gene (LDH) through homologous recombination. The expression of mRNA for the genome-integrated LDH is regulated under the control of the native PDC1 promoter, while PDC1 is completely disrupted. Using this method, we constructed a diploid yeast transformant, with each haploid genome having a single insertion of bovine LDH. Yeast cells expressing LDH were observed to convert glucose to both lactate (55.6 g/liter) and ethanol (16.9 g/liter), with up to 62.2% of the glucose being transformed into lactic acid under neutralizing conditions. This transgenic strain, which expresses bovine LDH under the control of the PDC1 promoter, also showed high lactic acid production (50.2 g/liter) under nonneutralizing conditions. The differences in lactic acid production were compared among four different recombinants expressing a heterologous LDH gene (i.e., either the bovine LDH gene or the Bifidobacterium longum LDH gene): two transgenic strains with 2μm plasmid-based vectors and two genome-integrated strains.

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