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Several members of the order Thermotogales in the domain Bacteria, viz., Thermotoga neapolitana, Thermotoga maritima, Thermosipho africanus, Fervidobacterium islandicum, and Thermotoga strain SEBR 2665, an isolate from an oil well, reduced thiosulfate to sulfide. This reductive process enhanced cellular yields and growth rates of all the members but was more significant with the two hyperthermophiles T. neapolitana and T. maritima. This is the first report of such an occurrence in this group of thermophilic and hyperthermophilic anaerobic bacteria. The results suggest that thiosulfate reduction is important in the geochemical cycling of sulfur in anaerobic thermal environments such as the slightly acidic and neutral-pH volcanic hot springs and oil reservoirs

Економічні засади покращення інвестиційного клімату України

Розглянуто тенденцію основних прямих та непрямих інвестицій в країну за певний період та виявлено основну низку системних вад економіко - правового середовища, які заважають припливу іноземних інвестицій. Представлені можливі шляхи покращення інвестиційного клімату України.Considered the main trend of direct and indirect investment in the country for a certain period and found a number of major systemic defects economic and legal environment that hinder foreign investment. Courtesy of the main factors that affect the volume of investment, presents possible ways of improving the investment climate in Ukraine

FAST TCP: From Theory to Experiments

We describe a variant of TCP, called FAST, that can sustain high throughput and utilization at multi-Gbps over large distance. We present the motivation, review the background theory, summarize key features of FAST TCP, and report our first experimental results

Structural characterization of diabolic acid-based tetraester, tetraether and mixed ether/ester, membrane-spanning lipids of bacteria from the order Thermotogales

The distribution of core lipids in the membranes of nine different species of the order Thermotogales, one of the early and deep branching lineages in the Bacteria, were examined by HPLC/MS and demonstrated to consist of membrane-spanning diglycerol lipids comprised of diabolic acid-derived alkyl moieties. In the Thermotoga species the core membrane lipids are characterized by the presence of both ester and ether bonds, whereas in the phylogenetically more distinct Thermosipho and Fervidobacterium spp. only ester bonds occur. A tentative biosynthetic route for the biosynthesis of these membrane-spanning lipids is proposed. Since species of the order Thermotogales are assumed to have occurred early during the evolution of life on Earth, as suggested by its position in the phylogenetic tree of life, these data suggest that the ability to produce both ether and ester glycerol membrane lipids developed relatively early during microbial evolution

Observation of a new boson at a mass of 125 GeV with the CMS experiment at the LHC

Results are presented from searches for the standard model Higgs boson in proton–proton collisions at √s = 7 and 8 TeV in the Compact Muon Solenoid experiment at the LHC, using data samples corresponding to integrated luminosities of up to 5.1 fb^(−1) at 7 TeV and 5.3 fb^(−1) at 8 TeV. The search is performed in five decay modes: γγ, ZZ, W^+W^−, τ^+τ^−, and bb. An excess of events is observed above the expected background, with a local significance of 5.0 standard deviations, at a mass near 125 GeV, signalling the production of a new particle. The expected significance for a standard model Higgs boson of that mass is 5.8 standard deviations. The excess is most significant in the two decay modes with the best mass resolution, γγ and ZZ; a fit to these signals gives a mass of 125.3±0.4(stat.)±0.5(syst.) GeV. The decay to two photons indicates that the new particle is a boson with spin different from one

How Molecular Evolution Technologies can Provide Bespoke Industrial Enzymes: Application to Biofuels

International audienceEnzymatic hydrolysis of lignocellulose is one of the major bottlenecks in the development of biological conversion of lignocellulosic biomass to biofuels. One of the most efficient organisms for the production of cellulolytic enzymes is the fungus Trichoderma reesei, mainly thanks to its high secretion capacity. The conversion of cellulose to glucose involves three types of cellulases working in synergy: endoglucanases (EC 3.2.1.4) randomly cleave b-1,4 glycosidic linkages of cellulose, cellobiohydrolases (EC 3.2.1.91) attack cellulose chain ends to produce cellobiose dimers which are converted into glucose by the b-glucosidases (EC 3.2.1 21). Unexpectedly, the amount of b-glucosidase (BGL1) from T. reesei hyperproducing strains represents a very low percentage of the total secreted proteins. A suboptimal content of this enzyme limits the performance of commercial cellulase preparations as cellobiose represents the main inhibitor of the cellulolysis reaction by cellobiohydrolases. This bottleneck can be alleviated either by overexpressing the b-glucosidase in T. reesei or optimized its specific activity. After giving a brief overview of the main available technologies, this example will be used to illustrate the potential of directed evolution technologies to devolop enzymes tailored to fit industrial needs. We describe the L-ShufflingTM strategy implemented with three parental genes originating from microbial biodiversity leading to identification of an efficient b-glucosidase showing a 242-fold increase in specific activity for the pNPGlc substrate compared to WT (Wild Type) Cel3a beta-glucosidase of T. reesei. After expression of the best improved b-glucosidase in T. reesei and secretion of a new enzymatic cocktail, improvement of the glucosidase activity allows a 4-fold decrease of cellulase loading for the saccharification of an industrial pretreated biomass compared to the parental cocktail

How Molecular Evolution Technologies can Provide Bespoke Industrial Enzymes: Application to Biofuels Comment les technologies d’évolution moléculaire peuvent fournir des enzymes industrielles sur mesure : application aux biocarburants

Enzymatic hydrolysis of lignocellulose is one of the major bottlenecks in the development of biological conversion of lignocellulosic biomass to biofuels. One of the most efficient organisms for the production of cellulolytic enzymes is the fungus Trichoderma reesei, mainly thanks to its high secretion capacity. The conversion of cellulose to glucose involves three types of cellulases working in synergy: endoglucanases (EC 3.2.1.4) randomly cleave 13-1,4 glycosidic linkages of cellulose, cellobiohydrolases (EC 3.2.1.91) attack cellulose chain ends to produce cellobiose dimers which are converted into glucose by the 13-glucosidases (EC 3.2.1 21). Unexpectedly, the amount of l3-glucosidase (BGLI) from T. reesei hyperproducing strains represents a very low percentage of the total secreted proteins. A suboptimal content of this enzyme limits the performance of commercial cellulase preparations as cellobiose represents the main inhibitor of the cellulolysis reaction by cellobiohydrolases. This bottleneck can be alleviated either by overexpressing the f3-glucosidase in T. reesei or optimized its specific activity. After giving a brief overview of the main available technologies, this example will be used to illustrate the potential of directed evolution technologies to devolop enzymes tailored to fit industrial needs. We describe the L-ShuffiingTM strategy implemented with three parental genes originating from microbial biodiversity leading to identification of an efficient 13-glucosidase showing a 242 fold increase in specific activity for the pNPGIc substrate compared to WT (Wild Type) Cel3a beta-glucosidase of T. reesei. After expression of the best improved 13-glucosidase in T. reesei and secretion of a new enzymatic cocktail, improvement of the glucosidase activity allows a 4-fold decrease of cellulase loading for the saccharification of an industrial pretreated biomass compared to the parental cocktail. L’hydrolyse enzymatique de la lignocellulose est l’un des principaux goulets d’étranglement dans le développement de la conversion biologique de la biomasse lignocellulosique en biocarburants. L’un des organismes les plus efficaces pour la production d’enzymes cellulolytiques est le champignon Trichoderma reesei, principalement grâce à sa capacité importante de sécrétion. La conversion de la cellulose en glucose implique trois types de cellulases travaillant en synergie : les endoglucanases (EC 3.2.1.4) clivant de façon aléatoire les liaisons glycosidiques en (3-1,4, les cellobiohydrolases (EC 3.2.1.91) attaquant la chaîne de cellulose aux deux extrémités afin de produire le cellobiose, dimère qui sera converti en glucose par l’action des (3-glucosidases (EC 3.2.1.21). De façon inattendue, la quantité de 3-glucosidase (BGL1) sécrétée par les souches de T. reesei représente un très faible pourcentage de la quantité totale des protéines sécrétées qui en fait donc une activité limitante du cocktail. Cette faible activité limite d’autant plus les performances du cocktail que le cellobiose représente le principal inhibiteur de la réaction cellulolyse par les cellobiohydrolases. Ce goulot d’étranglement peut être atténué soit par une surexpression de la (3-glucosidase chez T. reesei, soit par une amélioration de son activité spécifique. Après un bref aperçu des principales technologies existantes, cet exemple sera utilisé dans cette revue pour illustrer le potentiel des technologies d’évolution dirigée pour développer des enzymes répondant aux besoins de l’industrie des biotechnologies. Nous décrivons comment la mise en oeuvre d’une stratégie d’évolution dirigée par le L-ShufflingTM avec trois gènes parentaux provenant de la biodiversité microbienne permet d’obtenir des activités (3-glucosidases très améliorées par rapport à la Cel3a (3-glucosidase de T. reesei (activité spécifique 242 fois plus élevée pour le substrat pNPGIc). Cette amélioration de l’activité glucosidasique, après expression du gène codant pour la 3-glucosidase améliorée chez T. reesei et sécrétion du nouveau cocktail, permet une diminution d’un facteur 4 de la quantité de cocktail nécessaire à la saccharification d’une biomasse industrielle prétraitée (paille de blé)

How Molecular Evolution Technologies can Provide Bespoke Industrial Enzymes: Application to Biofuels

Enzymatic hydrolysis of lignocellulose is one of the major bottlenecks in the development of biological conversion of lignocellulosic biomass to biofuels. One of the most efficient organisms for the production of cellulolytic enzymes is the fungus Trichoderma reesei, mainly thanks to its high secretion capacity. The conversion of cellulose to glucose involves three types of cellulases working in synergy: endoglucanases (EC 3.2.1.4) randomly cleave 13-1,4 glycosidic linkages of cellulose, cellobiohydrolases (EC 3.2.1.91) attack cellulose chain ends to produce cellobiose dimers which are converted into glucose by the 13-glucosidases (EC 3.2.1 21). Unexpectedly, the amount of l3-glucosidase (BGLI) from T. reesei hyperproducing strains represents a very low percentage of the total secreted proteins. A suboptimal content of this enzyme limits the performance of commercial cellulase preparations as cellobiose represents the main inhibitor of the cellulolysis reaction by cellobiohydrolases. This bottleneck can be alleviated either by overexpressing the f3-glucosidase in T. reesei or optimized its specific activity. After giving a brief overview of the main available technologies, this example will be used to illustrate the potential of directed evolution technologies to devolop enzymes tailored to fit industrial needs. We describe the L-ShuffiingTM strategy implemented with three parental genes originating from microbial biodiversity leading to identification of an efficient 13-glucosidase showing a 242 fold increase in specific activity for the pNPGIc substrate compared to WT (Wild Type) Cel3a beta-glucosidase of T. reesei. After expression of the best improved 13-glucosidase in T. reesei and secretion of a new enzymatic cocktail, improvement of the glucosidase activity allows a 4-fold decrease of cellulase loading for the saccharification of an industrial pretreated biomass compared to the parental cocktail