scholarly journals L-lactic acid production from D-xylose with Candida sonorensis expressing a heterologous lactate dehydrogenase encoding gene

2014 ◽  
Vol 13 (1) ◽  
Author(s):  
Kari T Koivuranta ◽  
Marja Ilmén ◽  
Marilyn G Wiebe ◽  
Laura Ruohonen ◽  
Pirkko Suominen ◽  
...  
2020 ◽  
Author(s):  
Laura Salusjärvi ◽  
Leo Ojala ◽  
Gopal Peddinti ◽  
Michael Lienemann ◽  
Paula Jouhten ◽  
...  

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.


2014 ◽  
Vol 80 (23) ◽  
pp. 7134-7141 ◽  
Author(s):  
Limin Wang ◽  
Yumeng Cai ◽  
Lingfeng Zhu ◽  
Honglian Guo ◽  
Bo Yu

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.


2005 ◽  
Vol 71 (4) ◽  
pp. 1964-1970 ◽  
Author(s):  
Nobuhiro Ishida ◽  
Satoshi Saitoh ◽  
Kenro Tokuhiro ◽  
Eiji Nagamori ◽  
Takashi Matsuyama ◽  
...  

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.


2015 ◽  
Vol 82 (4) ◽  
pp. 1295-1304 ◽  
Author(s):  
S. Andreas Angermayr ◽  
Aniek D. van der Woude ◽  
Danilo Correddu ◽  
Ramona Kern ◽  
Martin Hagemann ◽  
...  

ABSTRACTBoth enantiomers of lactic acid,l-lactic acid andd-lactic acid, can be produced in a sustainable way by a photosynthetic microbial cell factory and thus from CO2, sunlight, and water. Several properties of polylactic acid (a polyester of polymerized lactic acid) depend on the controlled blend of these two enantiomers. Recently, cyanobacteriumSynechocystissp. strain PCC6803 was genetically modified to allow formation of either of these two enantiomers. This report elaborates on thed-lactic acid production achieved by the introduction of ad-specific lactate dehydrogenase from the lactic acid bacteriumLeuconostoc mesenteroidesintoSynechocystis. A typical batch culture of this recombinant strain initially shows lactic acid production, followed by a phase of lactic acid consumption, until production “outcompetes” consumption at later growth stages. We show thatSynechocystisis able to used-lactic acid, but notl-lactic acid, as a carbon source for growth. Deletion of the organism's putatived-lactate dehydrogenase (encoded byslr1556), however, does not eliminate this ability with respect tod-lactic acid consumption. In contrast,d-lactic acid consumption does depend on the presence of glycolate dehydrogenase GlcD1 (encoded bysll0404). Accordingly, this report highlights the need to match a product of interest of a cyanobacterial cell factory with the metabolic network present in the host used for its synthesis and emphasizes the need to understand the physiology of the production host in detail.


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