Genome Sequence of the Thermophilic Strain Bacillus coagulans2-6, an Efficient Producer of High-Optical-Purity
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            -Lactic Acid

Su, Fei; Yu, Bo; Sun, Jibin; Ou, Hong‐Yu; Zhao, Bo; Wang, Limin; Qin, Jiayang; Tang, Hongzhi; Tao, Fei; Jarek, Michael; Scharfe, Maren; Ma, Cuiqing; Ma, Yanhe; Xu, Ping

doi:10.1128/jb.05378-11

Cited by 21 publications

(17 citation statements)

References 14 publications

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“…B. coagulans 2-6 was isolated by our laboratory and was used in this study. It is a homofermentative producer of L-lactic acid with an optical purity of 99% (20,21). L. delbrueckii subsp.…”

Section: Methodsmentioning

confidence: 99%

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

Wang

Cai

Zhu

et al. 2014

Appl Environ Microbiol

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Bacillus coagulans 2-6 is an excellent producer of optically pure L-lactic acid. However, little is known about the mechanism of synthesis of the highly optically pure L-lactic acid produced by this strain. Three enzymes responsible for lactic acid production-NAD-dependent L-lactate dehydrogenase (L-nLDH; encoded by ldhL), NAD-dependent D-lactate dehydrogenase (D-nLDH; encoded by ldhD), and glycolate oxidase (GOX)-were systematically investigated in order to study the relationship between these enzymes and the optical purity of lactic acid. Lactobacillus delbrueckii subsp. bulgaricus DSM 20081 (a D-lactic acid producer) and Lactobacillus plantarum subsp. plantarum DSM 20174 (a DL-lactic acid producer) were also examined in this study as comparative strains, in addition to B. coagulans. The specific activities of key enzymes for lactic acid production in the three strains were characterized in vivo and in vitro, and the levels of transcription of the ldhL, ldhD, and GOX genes during fermentation were also analyzed. The catalytic activities of L-nLDH and D-nLDH were different in L-, D-, and DL-lactic acid producers. Only L-nLDH activity was detected in B. coagulans 2-6 under native conditions, and the level of transcription of ldhL in B. coagulans 2-6 was much higher than that of ldhD or the GOX gene at all growth phases. However, for the two Lactobacillus strains used in this study, ldhD transcription levels were higher than those of ldhL. The high catalytic efficiency of L-nLDH toward pyruvate and the high transcription ratios of ldhL to ldhD and ldhL to the GOX gene provide the key explanations for the high optical purity of L-lactic acid produced by B. coagulans 2-6.

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“…B. coagulans 2-6 was isolated by our laboratory and was used in this study. It is a homofermentative producer of L-lactic acid with an optical purity of 99% (20,21). L. delbrueckii subsp.…”

Section: Methodsmentioning

confidence: 99%

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

Wang

Cai

Zhu

et al. 2014

Appl Environ Microbiol

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“…Using the annotated genome sequence of two related B. coagulans strains, 36D1 (GenBank accession number: CP003056) and 2–6 (GenBank accession number: CP002472), as a refs 15, 16, 17, we determined that the enzyme encoded by ldh L3 was a leucine dehydrogenase (for strain 36D1) or a glutamate/leucine/phenylalanine/valine dehydrogenase (for strain 2–6). Based on these results, only the first two ldh L genes and one ldh D gene were chosen for subsequent experiments.…”

Section: Resultsmentioning

confidence: 99%

“…As the genetic manipulation of parent strain, such as B. coagulans 2–6, is currently not available, its phylogenetically close type strain B. coagulans DSM1 was used in this study since the genome sequence of B. coagulans 2–6 shares a high similarity (>99%) with B. coagulans DSM11516. Deletion of ldh L1 led to alteration of the main product of B. coagulans DSM1 from L-lactic acid to acetic acid and other byproducts.…”

Section: Discussionmentioning

confidence: 99%

“…As the genetic manipulation of strain B. coagulans 2–6 is currently not available, its phylogenetically close type strain B. coagulans DSM1 was used in this study1516. B. coagulans DSM1 is a homofermentative producer of L-lactic acid to an optical purity of 99.8%, which was purchased from Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH (DSMZ, Braunschweig, Germany).…”

Section: Methodsmentioning

confidence: 99%

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Contributory roles of two l-lactate dehydrogenases for l-lactic acid production in thermotolerant Bacillus coagulans

Sun

Zhang

Lyu

et al. 2016

Sci Rep

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Thermotolerant Bacillus coagulans is considered to be a more promising producer for bio-chemicals, due to its capacity to withstand harsh conditions. Two L-lactate dehydrogenase (LDH) encoding genes (ldhL1 and ldhL2) and one D-LDH encoding gene (ldhD) were annotated from the B. coagulans DSM1 genome. Transcriptional analysis revealed that the expression of ldhL2 was undetectable while the ldhL1 transcription level was much higher than that of ldhD at all growth phases. Deletion of the ldhL2 gene revealed no difference in fermentation profile compared to the wild-type strain, while ldhL1 single deletion or ldhL1ldhL2 double deletion completely blocked L-lactic acid production. Complementation of ldhL1 in the above knockout strains restored fermentation profiles to those observed in the wild-type strain. This study demonstrates ldhL1 is crucial for L-lactic acid production and NADH balance in B. coagulans DSM1 and lays the fundamental for engineering the thermotolerant B. coagulans strain as a platform chemicals producer.

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“…Interestingly, we found that NusA purified from the Gram-positive, non-γ-proteobacteria strains Lactobacillus delbrueckii subsp. bulgaricus ATCC 1184223 and Bacillus coagulans 2–624 also formed oligomers (Fig. S2) despite their sequence heterology.…”

Section: Resultsmentioning

confidence: 99%

Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity

Jiang

et al. 2013

Sci Rep

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Escherichia coli NusA, an essential component of the RNA polymerase elongation complex, is involved in transcriptional elongation, termination, anti-termination, cold shock and stress-induced mutagenesis. In this study, we demonstrated that NusA can self-assemble into oligomers under heat shock conditions and that this property is largely determined by the C-terminal domain. In parallel with the self-assembly process, NusA also acquires chaperone activity. Furthermore, NusA overexpression results in the enhanced heat shock resistance of host cells, which may be due to the chaperone activity of NusA. Our results suggest that E. coli NusA can act as a protector to prevent protein aggregation under heat stress conditions in vitro and in the NusA-overexpressing strain. We propose a new hypothesis that NusA could serve as a molecular chaperone in addition to its functions as a transcription factor. However, it remains to be further investigated whether NusA has the same function under normal physiological conditions.

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Genome Sequence of the Thermophilic Strain Bacillus coagulans2-6, an Efficient Producer of High-Optical-Purity l -Lactic Acid

Cited by 21 publications

References 14 publications

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

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

Contributory roles of two l-lactate dehydrogenases for l-lactic acid production in thermotolerant Bacillus coagulans

Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity

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