Relevant bibliographies by topics / Thermotoga maritima Thermotoga maritima Thermus thermophilus

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Academic literature on the topic 'Thermotoga maritima Thermotoga maritima Thermus thermophilus'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Thermotoga maritima Thermotoga maritima Thermus thermophilus"

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Mikhaylina, A. O., O. S. Kostareva, E. Y. Nikonova, M. B. Garber, and S. V. Tishchenko. "Identification of Ribosomal Protein L1-Binding Sites in Thermus thermophilus and Thermotoga maritima mRNAs." Molecular Biology 52, no. 1 (2018): 84–90. http://dx.doi.org/10.1134/s0026893318010132.

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Костарева, О. С., Е. Ю. Никонова, М. Б. Гарбер та С. В. Тищенко. "ИДЕНТИФИКАЦИЯ САЙТОВ СВЯЗЫВАНИЯ РИБОСОМНОГО БЕЛКА L1 НА МРНК THERMUS THERMOPHILUS И THERMOTOGA MARITIMA, "Молекулярная биология"". Молекулярная биология, № 1 (2018): 98–105. http://dx.doi.org/10.7868/s0026898418010135.

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Sharp, Paul M. "Identification of genes encoding ribosomal protein L33 from Bacillus licheniformis, Thermus thermophilus and Thermotoga maritima." Gene 139, no. 1 (1994): 135–36. http://dx.doi.org/10.1016/0378-1119(94)90537-1.

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Abu Al-Soud, Waleed, and Peter Rådström. "Capacity of Nine Thermostable DNA Polymerases To Mediate DNA Amplification in the Presence of PCR-Inhibiting Samples." Applied and Environmental Microbiology 64, no. 10 (1998): 3748–53. http://dx.doi.org/10.1128/aem.64.10.3748-3753.1998.

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ABSTRACT The PCR is an extremely powerful method for detecting microorganisms. However, its full potential as a rapid detection method is limited by the inhibition of the thermostable DNA polymerase fromThermus aquaticus by many components found in complex biological samples. In this study, we have compared the effects of known PCR-inhibiting samples on nine thermostable DNA polymerases. Samples of blood, cheese, feces, and meat, as well as various ions, were added to PCR mixtures containing various thermostable DNA polymerases. The nucleic acid amplification capacity of the nine polymerases,
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Wieteska, Lukasz, Maksim Ionov, Janusz Szemraj, Claudia Feller, Andrzej Kolinski, and Dominik Gront. "Improving thermal stability of thermophilic l -threonine aldolase from Thermotoga maritima." Journal of Biotechnology 199 (April 2015): 69–76. http://dx.doi.org/10.1016/j.jbiotec.2015.02.013.

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KLUSKENS, Leon D., Gert-Jan W. M. van ALEBEEK, Alphons G. J. VORAGEN, Willem M. de VOS, and John van der OOST. "Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima." Biochemical Journal 370, no. 2 (2003): 651–59. http://dx.doi.org/10.1042/bj20021595.

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The ability of the hyperthermophilic bacterium Thermotoga maritima to grow on pectin as a sole carbon source coincides with the secretion of a pectate lyase A (PelA) in the extracellular medium. The pelA gene of T. maritima was functionally expressed in Escherichia coli as the first heterologously produced thermophilic pectinase, and purified to homogeneity. Gel filtration indicated that the native form of PelA is tetrameric. Highest activity (422units/mg, with a Km of 0.06mM) was demonstrated on polygalacturonic acid (PGA), whereas pectins with an increasing degree of methylation were degrade
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Mehmood, Muhammad A., Izzah Shahid, Khadim Hussain, Farooq Latif та Muhammad I. Rajoka. "Thermodynamic Properties of the β-glucosidase from Thermotoga maritima Extend the Upper Limit of Thermophilicity". Protein & Peptide Letters 21, № 12 (2014): 1282–88. http://dx.doi.org/10.2174/0929866521666140616123104.

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Enzymes from thermophilic organisms are believed to be strong candidates for industrial applications due to their ability to withstand temperature-induced enzyme inactivation. The present study demonstrated molecular cloning, over-expression, purification and characterization of β-glucosidase from Thermotoga maritima. The bglA gene with a capacity to encode a 51 kDa enzyme was heterologously expressed in E. coli M15. The enzyme was produced @130 mgL-1 in LB media and @440 mgL-1 in Dubos salt medium accounting 40-47 % of total cellular soluble proteins when lactose was used as an inducer. The e
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Diaz, R. S., and E. C. Sabino. "Accuracy of replication in the polymerase chain reaction. Comparison between Thermotoga maritima DNA polymerase and Thermus aquaticus DNA polymerase." Brazilian Journal of Medical and Biological Research 31, no. 10 (1998): 1239–42. http://dx.doi.org/10.1590/s0100-879x1998001000001.

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Tiboni, O., A. M. Sanangelantoni, P. Cammarano, L. Cimino, G. Di Pasquale, and S. Sora. "Expression in Escherichia coli of the tuf Gene from the Extremely Thermophilic Eubacterium Thermotoga maritima: Purification of the Thermotoga Elongation Factor Tu by Thermal Denaturation of the Mesophile Host Cell Proteins." Systematic and Applied Microbiology 12, no. 2 (1989): 127–33. http://dx.doi.org/10.1016/s0723-2020(89)80002-5.

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10

Bertoldo, Costanzo, Fiona Duffner, Per L. Jorgensen, and Garabed Antranikian. "Pullulanase Type I from Fervidobacterium pennavorans Ven5: Cloning, Sequencing, and Expression of the Gene and Biochemical Characterization of the Recombinant Enzyme." Applied and Environmental Microbiology 65, no. 5 (1999): 2084–91. http://dx.doi.org/10.1128/aem.65.5.2084-2091.1999.

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ABSTRACT The gene encoding the type I pullulanase from the extremely thermophilic anaerobic bacterium Fervidobacterium pennavorans Ven5 was cloned and sequenced in Escherichia coli. The pulA gene from F. pennavoransVen5 had 50.1% pairwise amino acid identity with pulA from the anaerobic hyperthermophile Thermotoga maritima and contained the four regions conserved among all amylolytic enzymes. The pullulanase gene (pulA) encodes a protein of 849 amino acids with a 28-residue signal peptide. The pulA gene was subcloned without its signal sequence and overexpressed in E. coli under the control of
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Dissertations / Theses on the topic "Thermotoga maritima Thermotoga maritima Thermus thermophilus"

1

Hettwer, Stefan. "Tryptophansynthasen bei hohen Temperaturen Charakterisierung der thermostabilen Enzyme aus Thermotoga maritima und Etablierung eines Selektionssystems zur Stabilisierung thermolabiler Enzyme in Thermus thermophilus /." [S.l. : s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=964136716.

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Drone, Jullien. "Synthèse sélective d'oligosaccharides : utilisation de glycosidases obtenues par mutagenèse ponctuelle et par évolution dirigée : tentatives de création d'une activité hydratase à partir d'une pectate lyase." Nantes, 2006. http://www.theses.fr/2006NANT2038.

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L'objectif de cette thèse est, d'une part, axée sur les glycosidases modifiées pour la synthèse d'analogues de l'antigène H-1 et, d'autre part, de créer une activité hydratase à partir d'une pectate lyase. A cet effet, nous avons évalué trois glycosynthases et des transglycosidases. Nos résultats montrent que les glycosynthases permettent d'obtenir des disaccharides avec des rendements quasi quantitatifs. De plus, les transglycosidases permettent la synthèse de composés de transglycosylation avec des rendements de 60 à 75% selon l'accepteur utilisé. La modification de la pectate lyase de Therm
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Uzzell, Jamar. "STRUCTURAL BASIS FOR THERMAL STABILITY OF THERMOPHILIC TRMD PROTEINS." VCU Scholars Compass, 2011. http://scholarscompass.vcu.edu/etd/2539.

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Thermal stability of theG37 tRNA methyltransferase proteins from Thermotoga maritima and Aquifex aeolicus have been compared using Differential Scanning Calorimetry. It was shown that the Thermotoga protein is remarkably stable and is denatured at temperatures in excess of 100 degrees Centigrade. The Aquifex aeolicus protein was less stable, denaturing broadly at temperatures between 55oC and 100oC. In contrast, the mesophilic E. coli protein was completely denatured at 55oC. Enzymatic activity of the proteins was measured at various temperatures. Both the Thermotoga and Aquifex enzymes are
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4

Hettwer, Stefan [Verfasser]. "Tryptophansynthasen bei hohen Temperaturen : Charakterisierung der thermostabilen Enzyme aus Thermotoga maritima und Etablierung eines Selektionssystems zur Stabilisierung thermolabiler Enzyme in Thermus thermophilus / Stefan Hettwer." 2001. http://d-nb.info/964136716/34.

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