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

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.

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Production of optically pure l -lactic acid from lignocellulosic hydrolysate by using a newly isolated and d -lactate dehydrogenase gene-deficient Lactobacillus paracasei strain

Bioresource Technology ◽

10.1016/j.biortech.2015.09.071 ◽

2015 ◽

Vol 198 ◽

pp. 651-657 ◽

Cited By ~ 36

Author(s):

Yang-Cheng Kuo ◽

Shuo-Fu Yuan ◽

Chun-An Wang ◽

Yin-Jung Huang ◽

Gia-Luen Guo ◽

...

Keyword(s):

Lactic Acid ◽

Lactate Dehydrogenase ◽

Lactobacillus Paracasei ◽

Lignocellulosic Hydrolysate ◽

Dehydrogenase Gene ◽

Optically Pure

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

Applied and Environmental Microbiology ◽

10.1128/aem.71.4.1964-1970.2005 ◽

2005 ◽

Vol 71 (4) ◽

pp. 1964-1970 ◽

Cited By ~ 93

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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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

Applied and Environmental Microbiology ◽

10.1128/aem.01514-08 ◽

2008 ◽

Vol 75 (2) ◽

pp. 462-467 ◽

Cited By ~ 68

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.

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Lactic acid production by Saccharomyces cerevisiae expressing a Rhizopus oryzae lactate dehydrogenase gene

Journal of Industrial Microbiology & Biotechnology ◽

10.1007/s10295-002-0004-2 ◽

2003 ◽

Vol 30 (1) ◽

pp. 22-27 ◽

Cited By ~ 63

Author(s):

Christopher D. Skory

Keyword(s):

Saccharomyces Cerevisiae ◽

Lactic Acid ◽

Lactate Dehydrogenase ◽

Acid Production ◽

Rhizopus Oryzae ◽

Lactic Acid Production ◽

Dehydrogenase Gene

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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

Applied and Environmental Microbiology ◽

10.1128/aem.01692-09 ◽

2009 ◽

Vol 75 (24) ◽

pp. 7858-7861 ◽

Cited By ~ 60

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.

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Efficient production of d-lactate from methane in a lactate-tolerant strain of Methylomonas sp. DH-1 generated by adaptive laboratory evolution

Biotechnology for Biofuels ◽

10.1186/s13068-019-1574-9 ◽

2019 ◽

Vol 12 (1) ◽

Cited By ~ 5

Author(s):

Jong Kwan Lee ◽

Sujin Kim ◽

Wonsik Kim ◽

Sungil Kim ◽

Seungwoo Cha ◽

...

Keyword(s):

Transcription Factor ◽

Lactic Acid ◽

Lactate Dehydrogenase ◽

Value Added ◽

Wild Type ◽

Adaptive Laboratory Evolution ◽

Gene Encoding ◽

Laboratory Evolution ◽

Tolerant Strain ◽

Dehydrogenase Gene

Abstract Background Methane, a main component of natural gas and biogas, has gained much attention as an abundant and low-cost carbon source. Methanotrophs, which can use methane as a sole carbon and energy source, are promising hosts to produce value-added chemicals from methane, but their metabolic engineering is still challenging. In previous attempts to produce lactic acid (LA) from methane, LA production levels were limited in part due to LA toxicity. We solved this problem by generating an LA-tolerant strain, which also contributes to understanding novel LA tolerance mechanisms. Results In this study, we engineered a methanotroph strain Methylomonas sp. DH-1 to produce d-lactic acid (d-LA) from methane. LA toxicity is one of the limiting factors for high-level production of LA. Therefore, we first performed adaptive laboratory evolution of Methylomonas sp. DH-1, generating an LA-tolerant strain JHM80. Genome sequencing of JHM80 revealed the causal gene watR, encoding a LysR-type transcription factor, whose overexpression due to a 2-bp (TT) deletion in the promoter region is partly responsible for the LA tolerance of JHM80. Overexpression of the watR gene in wild-type strain also led to an increase in LA tolerance. When d form-specific lactate dehydrogenase gene from Leuconostoc mesenteroides subsp. mesenteroides ATCC 8293 was introduced into the genome while deleting the glgA gene encoding glycogen synthase, JHM80 produced about 7.5-fold higher level of d-LA from methane than wild type, suggesting that LA tolerance is a critical limiting factor for LA production in this host. d-LA production was further enhanced by optimization of the medium, resulting in a titer of 1.19 g/L and a yield of 0.245 g/g CH4. Conclusions JHM80, an LA-tolerant strain of Methylomonas sp. DH-1, generated by adaptive laboratory evolution was effective in LA production from methane. Characterization of the mutated genes in JHM80 revealed that overexpression of the watR gene, encoding a LysR-type transcription factor, is responsible for LA tolerance. By introducing a heterologous lactate dehydrogenase gene into the genome of JHM80 strain while deleting the glgA gene, high d-LA production titer and yield were achieved from methane.

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Functional Replacement of the Escherichia colid-(−)-Lactate Dehydrogenase Gene (ldhA) with the l-(+)-Lactate Dehydrogenase Gene (ldhL) from Pediococcus acidilactici

Applied and Environmental Microbiology ◽

10.1128/aem.69.4.2237-2244.2003 ◽

2003 ◽

Vol 69 (4) ◽

pp. 2237-2244 ◽

Cited By ~ 74

Author(s):

Shengde Zhou ◽

K. T. Shanmugam ◽

L. O. Ingram

Keyword(s):

Lactic Acid ◽

Lactate Dehydrogenase ◽

Dehydrogenase Activity ◽

Optical Purity ◽

Pediococcus Acidilactici ◽

Coding Region ◽

Mineral Salts ◽

Lactate Dehydrogenase Activity ◽

Fermentation Products ◽

Dehydrogenase Gene

ABSTRACT The microbial production of l-(+)-lactic acid is rapidly expanding to allow increased production of polylactic acid (PLA), a renewable, biodegradable plastic. The physical properties of PLA can be tailored for specific applications by controlling the ratio of l-(+) and d-(−) isomers. For most uses of PLA, the l-(+) isomer is more abundant. As an approach to reduce costs associated with biocatalysis (complex nutrients, antibiotics, aeration, product purification, and waste disposal), a recombinant derivative of Escherichia coli W3110 was developed that contains five chromosomal deletions (focA-pflB frdBC adhE ackA ldhA). This strain was constructed from a d-(−)-lactic acid-producing strain, SZ63 (focA-pflB frdBC adhE ackA), by replacing part of the chromosomal ldhA coding region with Pediococcus acidilactici ldhL encoding an l-lactate dehydrogenase. Although the initial strain (SZ79) grew and fermented poorly, a mutant (SZ85) was readily isolated by selecting for improved growth. SZ85 exhibited a 30-fold increase in l-lactate dehydrogenase activity in comparison to SZ79, functionally replacing the native d-lactate dehydrogenase activity. Sequencing revealed mutations in the upstream, coding, and terminator regions of ldhL in SZ85, which are presumed to be responsible for increased l-lactate dehydrogenase activity. SZ85 produced l-lactic acid in M9 mineral salts medium containing glucose or xylose with a yield of 93 to 95%, a purity of 98% (based on total fermentation products), and an optical purity greater than 99%. Unlike other recombinant biocatalysts for l-lactic acid, SZ85 remained prototrophic and is devoid of plasmids and antibiotic resistance genes.

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