Functional analysis of lactate dehydrogenase during hypoxic stress in Arabidopsis

During waterlogging conditions plants switch from aerobic respiration to anaerobic fermentation to cope with the lack of available oxygen. Plants have two main fermentation pathways: ethanol and lactic acid fermentation. In this paper we carry out a functional analysis of the Arabidopsis lactate dehydrogenase gene, LDH1. Our results indicate that LDH1, like some other anaerobic genes, is expressed in a root-specific manner and is affected by a variety of abiotic stresses (hypoxia, drought, cold) and mechanical wounding. Functional analysis of LDH1 was carried out using transgenic Arabidopsis overexpressing the gene (35S promoter) and a T-DNA knockout line. Overexpression of LDH1 resulted in improved survival of low oxygen stress conditions in roots but not in shoots. Increased lactic acid fermentation also resulted in significantly higher activities of pyruvate decarboxylase (PDC). Knockout mutants of LDH1 showed reduced survival under low oxygen conditions and PDC activity levels were not changed compared with the wild type. Our data suggest that there is an interdependency between the lactic and ethanol fermentation pathways and that lactic acid fermentation may play a role in stimulating ethanol fermentation and improving plant survival. We show also that Arabidopsis plants are able to exude lactate efficiently into the medium, preventing it accumulating to toxic levels in the cells.

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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

Applied and Environmental Microbiology ◽

10.1128/aem.00573-09 ◽

2009 ◽

Vol 75 (15) ◽

pp. 5175-5178 ◽

Cited By ~ 45

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.

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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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In Vivo Regulation of Alcohol Dehydrogenase and Lactate Dehydrogenase in Rhizopus Oryzae to Improve l-Lactic Acid Fermentation

Applied Biochemistry and Biotechnology ◽

10.1007/s12010-011-9214-2 ◽

2011 ◽

Vol 164 (8) ◽

pp. 1305-1322 ◽

Cited By ~ 13

Author(s):

Sitanan Thitiprasert ◽

Sarintip Sooksai ◽

Nuttha Thongchul

Keyword(s):

Lactic Acid ◽

Lactate Dehydrogenase ◽

Alcohol Dehydrogenase ◽

Rhizopus Oryzae ◽

Lactic Acid Fermentation ◽

Acid Fermentation

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Solid And Liquid Pineapple Waste Utilization For Lactic Acid Fermentation

REAKTOR ◽

10.14710/reaktor.11.1.50-52 ◽

2017 ◽

Vol 11 (1) ◽

pp. 50 ◽

Cited By ~ 5

Author(s):

Abdullah Abdullah

Keyword(s):

Lactic Acid ◽

Carbon Source ◽

Batch Fermentation ◽

Anaerobic Fermentation ◽

Waste Utilization ◽

Lactic Acid Fermentation ◽

Lactobacillus Delbrueckii ◽

Raw Material ◽

Acid Fermentation ◽

Pineapple Waste

The liquid and solid pineapple waste contain mainly sucrose, glucose,fructose, and other nutrients. It therefore can potentially be used as carbon source for fermentation to produce organic acid. Recently, lactic acid has been considered to be an important raw material for production of biodegradable lactate polymer, the experiments were carried out in batch fermentation using the liquid and solid pineapple waste to produce lactic acid. The anaerobic fermentation of lactic acis were performed at 40 0C, ph 6, 5% inocolum, and 50 rpm. Initially results show that the liquid pineapple waste by using Lactobacillus delbrueckii can be used as carbon source for lactic acid fermentation. The production of lactic acid are found to be 79% yield, while only 56% yield was produced y using solid waste.Keywords : Lactic acid fermentation, Pineapple waste, Lactobacillus delbrueckii

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Modification of metabolic pathways of Saccharomyces cerevisiae by the expression of lactate dehydrogenase and deletion of pyruvate decarboxylase genes for the lactic acid fermentation at low pH value

Journal of Fermentation and Bioengineering ◽

10.1016/s0922-338x(98)80131-1 ◽

1998 ◽

Vol 86 (3) ◽

pp. 284-289 ◽

Cited By ~ 78

Author(s):

Eri Adachi ◽

Mikiko Torigoe ◽

Minetaka Sugiyama ◽

Jun-Ichi Nikawa ◽

Kazuyuki Shimizu

Keyword(s):

Saccharomyces Cerevisiae ◽

Lactic Acid ◽

Lactate Dehydrogenase ◽

Metabolic Pathways ◽

Ph Value ◽

Pyruvate Decarboxylase ◽

Low Ph ◽

Lactic Acid Fermentation ◽

Acid Fermentation

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Lactic Acid Fermentation Is Required for NLRP3 Inflammasome Activation

Frontiers in Immunology ◽

10.3389/fimmu.2021.630380 ◽

2021 ◽

Vol 12 ◽

Author(s):

Hsin-Chung Lin ◽

Yu-Jen Chen ◽

Yau-Huei Wei ◽

Hsin-An Lin ◽

Chien-Chou Chen ◽

...

Keyword(s):

Lactic Acid ◽

Lactate Dehydrogenase ◽

Nlrp3 Inflammasome ◽

Lactate Production ◽

Lactic Acid Fermentation ◽

Inflammasome Activation ◽

Acid Fermentation ◽

Potassium Efflux ◽

Pyruvate Oxidation ◽

Nlrp3 Inflammasome Activation

Activation of the Nod-like receptor 3 (NLRP3) inflammasome is important for activation of innate immune responses, but improper and excessive activation can cause inflammatory disease. We previously showed that glycolysis, a metabolic pathway that converts glucose into pyruvate, is essential for NLRP3 inflammasome activation in macrophages. Here, we investigated the role of metabolic pathways downstream glycolysis – lactic acid fermentation and pyruvate oxidation—in activation of the NLRP3 inflammasome. Using pharmacological or genetic approaches, we show that decreasing lactic acid fermentation by inhibiting lactate dehydrogenase reduced caspase-1 activation and IL-1β maturation in response to various NLRP3 inflammasome agonists such as nigericin, ATP, monosodium urate (MSU) crystals, or alum, indicating that lactic acid fermentation is required for NLRP3 inflammasome activation. Inhibition of lactate dehydrogenase with GSK2837808A reduced lactate production and activity of the NLRP3 inflammasome regulator, phosphorylated protein kinase R (PKR), but did not reduce the common trigger of NLRP3 inflammasome, potassium efflux, or reactive oxygen species (ROS) production. By contrast, decreasing the activity of pyruvate oxidation by depletion of either mitochondrial pyruvate carrier 2 (MPC2) or pyruvate dehydrogenase E1 subunit alpha 1 (PDHA1) enhanced NLRP3 inflammasome activation, suggesting that inhibition of mitochondrial pyruvate transport enhanced lactic acid fermentation. Moreover, treatment with GSK2837808A reduced MSU-mediated peritonitis in mice, a disease model used for studying the consequences of NLRP3 inflammasome activation. Our results suggest that lactic acid fermentation is important for NLRP3 inflammasome activation, while pyruvate oxidation is not. Thus, reprograming pyruvate metabolism in mitochondria and in the cytoplasm should be considered as a novel strategy for the treatment of NLRP3 inflammasome-associated diseases.

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