Electrostimulation of hyperthermophile Thermotoga neapolitana cultures

2021 ◽  
Vol 319 ◽  
pp. 124078 ◽  
Author(s):  
G. d'Ippolito ◽  
G. Squadrito ◽  
M. Tucci ◽  
N. Esercizio ◽  
A. Sardo ◽  
...  
Keyword(s):  
Thermotoga Neapolitana

scholarly journals Chromosome Evolution in the Thermotogales: Large-Scale Inversions and Strain Diversification of CRISPR Sequences

2006 ◽  
Vol 188 (7) ◽  
pp. 2364-2374 ◽  
Author(s):  
Robert T. DeBoy ◽  
Emmanuel F. Mongodin ◽  
Joanne B. Emerson ◽  
Karen E. Nelson
Keyword(s):  
Sequence Analysis ◽  
Large Scale ◽  
Thermotoga Maritima ◽  
Chromosomal Rearrangements ◽  
Pcr Amplification ◽  
Trna Genes ◽  
Thermotoga Neapolitana ◽  
Dna Repeats ◽  
Dna Rearrangements ◽  
Dna Repeat

ABSTRACT In the present study, the chromosomes of two members of the Thermotogales were compared. A whole-genome alignment of Thermotoga maritima MSB8 and Thermotoga neapolitana NS-E has revealed numerous large-scale DNA rearrangements, most of which are associated with CRISPR DNA repeats and/or tRNA genes. These DNA rearrangements do not include the putative origin of DNA replication but move within the same replichore, i.e., the same replicating half of the chromosome (delimited by the replication origin and terminus). Based on cumulative GC skew analysis, both the T. maritima and T. neapolitana lineages contain one or two major inverted DNA segments. Also, based on PCR amplification and sequence analysis of the DNA joints that are associated with the major rearrangements, the overall chromosome architecture was found to be conserved at most DNA joints for other strains of T. neapolitana. Taken together, the results from this analysis suggest that the observed chromosomal rearrangements in the Thermotogales likely occurred by successive inversions after their divergence from a common ancestor and before strain diversification. Finally, sequence analysis shows that size polymorphisms in the DNA joints associated with CRISPRs can be explained by expansion and possibly contraction of the DNA repeat and spacer unit, providing a tool for discerning the relatedness of strains from different geographic locations.

Probing the Solvent Accessibility of the [4Fe–4S] Cluster of the Hydrogenase Maturation Protein HydF from Thermotoga neapolitana by HYSCORE and 3p-ESEEM

2015 ◽  
Vol 119 (43) ◽  
pp. 13680-13689 ◽  
Author(s):  
Marco Albertini ◽  
Paola Berto ◽  
Francesca Vallese ◽  
Marilena Di Valentin ◽  
Paola Costantini ◽  
...  
Keyword(s):  
Solvent Accessibility ◽  
Thermotoga Neapolitana ◽  
Hydrogenase Maturation ◽  
Maturation Protein

scholarly journals Biochemical characterisation of four rhamnosidases from thermophilic bacteria of the genera Thermotoga, Caldicellulosiruptor and Thermoclostridium

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Melanie Baudrexl ◽  
Wolfgang H. Schwarz ◽  
Vladimir V. Zverlov ◽  
Wolfgang Liebl
Keyword(s):  
Thermophilic Bacteria ◽  
Thermotoga Maritima ◽  
Physiological Role ◽  
Structural Similarity ◽  
Glycoside Hydrolase Family ◽  
Thermotoga Neapolitana ◽  
Cobalt Nickel ◽  
Biochemical Characterisation ◽  
Hydrolase Family ◽  
Nickel Manganese

Abstract Carbohydrate active enzymes are classified in databases based on sequence and structural similarity. However, their function can vary considerably within a similarity-based enzyme family, which makes biochemical characterisation indispensable to unravel their physiological role and to arrive at a meaningful annotation of the corresponding genes. In this study, we biochemically characterised the four related enzymes Tm_Ram106B, Tn_Ram106B, Cb_Ram106B and Ts_Ram106B from the thermophilic bacteria Thermotoga maritima MSB8, Thermotoga neapolitana Z2706-MC24, Caldicellulosiruptor bescii DSM 6725 and Thermoclostridium stercorarium DSM 8532, respectively, as α-l-rhamnosidases. Cobalt, nickel, manganese and magnesium ions stimulated while EDTA and EGTA inhibited all four enzymes. The kinetic parameters such as Km, Vmax and kcat were about average compared to other rhamnosidases. The enzymes were inhibited by rhamnose, with half-maximal inhibitory concentrations (IC50) between 5 mM and 8 mM. The α-l-rhamnosidases removed the terminal rhamnose moiety from the rutinoside in naringin, a natural flavonone glycoside. The Thermotoga sp. enzymes displayed the highest optimum temperatures and thermostabilities of all rhamnosidases reported to date. The four thermophilic and divalent ion-dependent rhamnosidases are the first biochemically characterised orthologous enzymes recently assigned to glycoside hydrolase family 106.

Thermotoga neapolitana sp. nov. of the extremely thermophilic, eubacterial genus Thermotoga

1988 ◽  
Vol 150 (1) ◽  
pp. 103-104 ◽  
Author(s):  
Holger W. Jannasch ◽  
Robert Huber ◽  
Shimshon Belkin ◽  
Karl O. Stetter
Keyword(s):  
Thermotoga Neapolitana

Quantitative real-time PCR monitoring dynamics of Thermotoga neapolitana in synthetic co-culture for biohydrogen production

2018 ◽  
Vol 43 (6) ◽  
pp. 3133-3141 ◽  
Author(s):  
Onyinye Okonkwo ◽  
Aino-Maija Lakaniemi ◽  
Ville Santala ◽  
Matti Karp ◽  
Rahul Mangayil
Keyword(s):  
Real Time ◽  
Real Time Pcr ◽  
Biohydrogen Production ◽  
Thermotoga Neapolitana ◽  
Quantitative Real Time Pcr

Thermotoga neapolitana Homotetrameric Xylose Isomerase Is Expressed as a Catalytically Active and Thermostable Dimer in Escherichia coli

1998 ◽  
Vol 64 (7) ◽  
pp. 2357-2360 ◽  
Author(s):  
J. Michael Hess ◽  
Vladimir Tchernajenko ◽  
Claire Vieille ◽  
J. Gregory Zeikus ◽  
Robert M. Kelly
Keyword(s):  
Escherichia Coli ◽  
Differential Scanning Calorimetry ◽  
Gel Filtration ◽  
Xylose Isomerase ◽  
Thermotoga Neapolitana ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Catalytically Active ◽  
The Stability ◽  
Tetrameric Form

ABSTRACT The xylA gene from Thermotoga neapolitana5068 was expressed in Escherichia coli. Gel filtration chromatography showed that the recombinant enzyme was both a homodimer and a homotetramer, with the dimer being the more abundant form. The purified native enzyme, however, has been shown to be exclusively tetrameric. The two enzyme forms had comparable stabilities when they were thermoinactivated at 95°C. Differential scanning calorimetry revealed thermal transitions at 99 and 109.5°C for both forms, with an additional shoulder at 91°C for the tetramer. These results suggest that the association of the subunits into the tetrameric form may have little impact on the stability and biocatalytic properties of the enzyme.

scholarly journals Capnophilic Lactic Fermentation from Thermotoga neapolitana: A Resourceful Pathway to Obtain Almost Enantiopure L-lactic Acid

Fermentation ◽  
2019 ◽  
Vol 5 (2) ◽  
pp. 34 ◽  
Author(s):  
Genoveffa Nuzzo ◽  
Simone Landi ◽  
Nunzia Esercizio ◽  
Emiliano Manzo ◽  
Angelo Fontana ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Enantiomeric Excess ◽  
Thermophilic Bacterium ◽  
Racemic Mixture ◽  
Thermotoga Neapolitana ◽  
High Concentration ◽  
Lactic Fermentation ◽  
Bacterial Fermentation ◽  
First Time

The industrial production of lactic acid (LA) is mainly based on bacterial fermentation. This process can result in enantiopure or racemic mixture according to the producing organism. Between the enantiomers, L-lactic acid shows superior market value. Recently, we reported a novel anaplerotic pathway called capnophilic lactic fermentation (CLF) that produces a high concentration of LA by fermentation of sugar in the anaerobic thermophilic bacterium Thermotoga neapolitana. The aim of this work was the identification of the enantiomeric characterization of the LA produced by T. neapolitana and identification of the lactate dehydrogenase in T. neapolitana (TnLDH) and related bacteria of the order Thermotogales. Chemical derivatization and GC/MS analysis were applied to define the stereochemistry of LA from T. neapolitana. A bioinformatics study on TnLDH was carried out for the characterization of the enzyme. Chemical analysis showed a 95.2% enantiomeric excess of L-LA produced by T. neapolitana. A phylogenetic approach clearly clustered the TnLDH together with the L-LDH from lactic acid bacteria. We report for the first time that T. neapolitana is able to produce almost enantiopure L-lactic acid. The result was confirmed by bioinformatics analysis on TnLDH, which is a member of the L-LDH sub-family.

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