scholarly journals Improved Production of Homo-d-Lactic Acid via Xylose Fermentation by Introduction of Xylose Assimilation Genes and Redirection of the Phosphoketolase Pathway to the Pentose Phosphate Pathway in l-Lactate Dehydrogenase Gene-Deficient Lactobacillus plantarum

2009 ◽  
Vol 75 (24) ◽  
pp. 7858-7861 ◽  
Author(s):  
Kenji Okano ◽  
Shogo Yoshida ◽  
Ryosuke Yamada ◽  
Tsutomu Tanaka ◽  
Chiaki Ogino ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactate Dehydrogenase ◽  
Lactobacillus Plantarum ◽  
Pentose Phosphate Pathway ◽  
Xylose Fermentation ◽  
Pentose Phosphate ◽  
Dehydrogenase Gene ◽  
Phosphoketolase Pathway ◽  
Optically Pure

ABSTRACT The production of optically pure d-lactic acid via xylose fermentation was achieved by using a Lactobacillus plantarum NCIMB 8826 strain whose l-lactate dehydrogenase gene was deficient and whose phosphoketolase genes were replaced with a heterologous transketolase gene. After 60 h of fermentation, 41.2 g/liter of d-lactic acid was produced from 50 g/liter of xylose.

scholarly journals Homo-d-Lactic Acid Fermentation from Arabinose by Redirection of the Phosphoketolase Pathway to the Pentose Phosphate Pathway in l-Lactate Dehydrogenase Gene-Deficient Lactobacillus plantarum

2009 ◽  
Vol 75 (15) ◽  
pp. 5175-5178 ◽  
Author(s):  
Kenji Okano ◽  
Shogo Yoshida ◽  
Tsutomu Tanaka ◽  
Chiaki Ogino ◽  
Hideki Fukuda ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactate Dehydrogenase ◽  
Lactobacillus Plantarum ◽  
Pentose Phosphate Pathway ◽  
Pentose Phosphate ◽  
Lactic Acid Fermentation ◽  
Acid Fermentation ◽  
Dehydrogenase Gene ◽  
Phosphoketolase Pathway ◽  
Optically Pure

ABSTRACT Optically pure d-lactic acid fermentation from arabinose was achieved by using the Lactobacillus plantarum NCIMB 8826 strain whose l-lactate dehydrogenase gene was deficient and whose phosphoketolase gene was substituted with a heterologous transketolase gene. After 27 h of fermentation, 38.6 g/liter of d-lactic acid was produced from 50 g/liter of arabinose.

scholarly journals Efficient Production of Optically Pure d-Lactic Acid from Raw Corn Starch by Using a Genetically Modified l-Lactate Dehydrogenase Gene-Deficient and α-Amylase-Secreting Lactobacillus plantarum Strain

2008 ◽  
Vol 75 (2) ◽  
pp. 462-467 ◽  
Author(s):  
Kenji Okano ◽  
Qiao Zhang ◽  
Satoru Shinkawa ◽  
Shogo Yoshida ◽  
Tsutomu Tanaka ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactate Dehydrogenase ◽  
Lactobacillus Plantarum ◽  
Corn Starch ◽  
Optical Purity ◽  
Lactic Acid Fermentation ◽  
Efficient Production ◽  
Acid Fermentation ◽  
Dehydrogenase Gene ◽  
Optically Pure

ABSTRACT In order to achieve direct and efficient fermentation of optically pure d-lactic acid from raw corn starch, we constructed l-lactate dehydrogenase gene (ldhL1)-deficient Lactobacillus plantarum and introduced a plasmid encoding Streptococcus bovis 148 α-amylase (AmyA). The resulting strain produced only d-lactic acid from glucose and successfully expressed amyA. With the aid of secreting AmyA, direct d-lactic acid fermentation from raw corn starch was accomplished. After 48 h of fermentation, 73.2 g/liter of lactic acid was produced with a high yield (0.85 g per g of consumed sugar) and an optical purity of 99.6%. Moreover, a strain replacing the ldhL1 gene with an amyA-secreting expression cassette was constructed. Using this strain, direct d-lactic acid fermentation from raw corn starch was accomplished in the absence of selective pressure by antibiotics. This is the first report of direct d-lactic acid fermentation from raw starch.

scholarly journals A new high phenyl lactic acid-yieldingLactobacillus plantarum IMAU10124 and a comparative analysis of lactate dehydrogenase gene

2014 ◽  
Vol 356 (1) ◽  
pp. 89-96 ◽  
Author(s):  
Xiqing Zhang ◽  
Shuli Zhang ◽  
Yan Shi ◽  
Fadi Shen ◽  
Haikuan Wang
Keyword(s):  
Lactic Acid ◽  
Comparative Analysis ◽  
Lactate Dehydrogenase ◽  
Dehydrogenase Gene

Metabolic activities of sheep erythrocytes. I. Glycolytic activities

1962 ◽  
Vol 13 (1) ◽  
pp. 31 ◽  
Author(s):  
RA Leng ◽  
EF Annison
Keyword(s):  
Carbon Dioxide ◽  
Methylene Blue ◽  
Lactic Acid ◽  
Oxygen Uptake ◽  
Pentose Phosphate Pathway ◽  
Glucose Oxidation ◽  
Lactic Acid Production ◽  
Pentose Phosphate ◽  
Sheep Erythrocytes ◽  
Metabolic Activities

Sheep erythrocytes, which in most animals are impermeable to glucose, show low glycolytic activities relative to human cells. When 14C-labelled glucose was incubated with erythrocyte suspensions the oxygen uptake was 10.9 ± 1.8 µl/hr/ml of cells (5 replications), and glucose oxidation (measured by recovery of [14C]carbon dioxide) was 0.03 ± 0.007 µmole/hr/ml (5). Addition of methylene blue (0.4 µmole/ ml) increased oxygen uptake to 56 ± 3.5 µl/hr/ml (5) and glucose oxidation to 0.36 ± 0.02 µmole/hr/ml. Lactic acid production was increased from 1 .5 ± 0.06 µmole/hr/ml (7) to 1.7 ± 0.11 µmole/hr/ml (7) in the presence of methylene blue. Comparison of the yields of [14C]carbon dioxide from [1-14C]glucose and uniformly labelled [14C]glucose indicated that when stimulated by methylene blue 80–100% of glycolysis proceeded by the pentose phosphate pathway, but in the unstimulated system the alternative aerobic pathway accounted for only about 15% of total glycolysis.

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.

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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