65 research outputs found

    Іван Франко - публіцист

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    Проаналізовано соціально-економічну і культурно-освітню публіцистику І. Франка, зокрема, його ставлення до податкової політики Австро-Угорщини, діяльності банківської системи, еміграції з Галичини, кооперативного руху, майбутнього української держави.The article analyses social and economic and cultural and educational publications by Ivan Franko, as well as his attitude to tax policies in Austro-Hungarian Empire, banking system activities, emigration from Halychyna, co-operative societies movement, and the future of Ukraine

    Purification, characterization, and cloning of a bifunctional molybdoenzyme with hydratase and alcohol dehydrogenase activity

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    A bifunctional hydratase/alcohol dehydrogenase was isolated from the cyclohexanol degrading bacterium Alicycliphilus denitrificans DSMZ 14773. The enzyme catalyzes the addition of water to α,β-unsaturated carbonyl compounds and the subsequent alcohol oxidation. The purified enzyme showed three subunits in SDS gel, and the gene sequence revealed that this enzyme belongs to the molybdopterin binding oxidoreductase family containing molybdopterins, FAD, and iron-sulfur clusters

    Genome analysis and physiological comparison of Alicycliphilus denitrificans strains BC and K601T

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    The genomes of the Betaproteobacteria Alicycliphilus denitrificans strains BC and K601T have been sequenced to get insight into the physiology of the two strains. Strain BC degrades benzene with chlorate as electron acceptor. The cyclohexanol-degrading denitrifying strain K601T is not able to use chlorate as electron acceptor, while strain BC cannot degrade cyclohexanol. The 16S rRNA sequences of strains BC and K601T are identical and the fatty acid methyl ester patterns of the strains are similar. Basic Local Alignment Search Tool (BLAST) analysis of predicted open reading frames of both strains showed most hits with Acidovorax sp. JS42, a bacterium that degrades nitro-aromatics. The genomes include strain-specific plasmids (pAlide201 in strain K601T and pAlide01 and pAlide02 in strain BC). Key genes of chlorate reduction in strain BC were located on a 120 kb megaplasmid (pAlide01), which was absent in strain K601T. Genes involved in cyclohexanol degradation were only found in strain K601T. Benzene and toluene are degraded via oxygenase-mediated pathways in both strains. Genes involved in the meta-cleavage pathway of catechol are present in the genomes of both strains. Strain BC also contains all genes of the ortho-cleavage pathway. The large number of mono- and dioxygenase genes in the genomes suggests that the two strains have a broader substrate range than known thus far.This research was supported by the Technology Foundation, the Applied Science Division (STW) of the Netherlands Organization for Scientific Research (NWO), project number 08053, the graduate school WIMEK (Wageningen Institute for Environment and Climate Research, which is part of SENSE Research School for Socio-Economic and Natural Sciences of the Environment, www.wimek-new.wur.nl and www.sense.nl), SKB (Dutch Centre for Soil Quality Management and Knowledge Transfer, www.skbodem.nl) and the Consolider project CSD-2007-00055. The research was incorporated in the TRIAS (TRIpartite Approaches 469 toward Soil systems processes) program (http://www.nwo.nl/en/research-and-results/programmes/alw/trias-tripartite-approach-to-soil-system-processes/index. html). Flávia Talarico Saia was supported by a FAPESP (the State of São Paulo Research Foundation) scholarship (2006-01997/5). The work conducted by the DOE JGI is supported by the Office of Science of the United States Department of Energy under contract number DE-AC02-05CH11231. Alfons Stams acknowledges support by an ERC (European Research Counsil) advanced grant (project 323009). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript

    Laccase purification and characterization from Trametes trogii isolated in Tunisia: decolorization of textile dyes by the purified enzyme

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    8 páginas, 3 figuras, 5 tablas -- PAGS nros. 141-148A white-rot basidiomycete, isolated from decayed acacia wood (from Northwest of Tunisia) and identified as Trametes trogii, was selected in a broad plate screening because of its ability to degrade commercial dyes. In liquid cultures using a glucose–peptone medium, the sole ligninolytic activity detected was laccase. The highest laccase levels were obtained in presence of CuSO4 as inducer (around 20000 U/l). Two isoenzymes, were purified using anion-exchange and size-exclusion chromatographies. Both isoenzymes are monomeric proteins, with Mw around 62 kDa and isoelectric points of 4.3 and 4.5, showing similar stability at pH and temperature, optimum pH and substrate specificity. The highest oxidation rate was obtained at pH 2 and 2.5 for ABTS and DMP, respectively. They were stable up to 50 °C for 24 h and the stability was higher at alkaline pH. Activity increased by the addition of 10 mM Ni, Mo or Mn but it was not affected by Cd, Al, Li and Ca. Identical N-terminal sequences were determined in both laccases. The crude enzyme, as well as the purified laccase, was able to decolorize dyes from the textile industryThis research has been funded by a Cooperation project between Spain and Tunisia (31p/02 – Spanish “Ministerio de Asuntos Exteriores” and “MRSTDC”), and in part by a grant from “Contrats Programmes MRSTCD” (Tunisia)Peer reviewe

    Laccase purification and characterization from Trametes trogii isolated in Tunisia: decolorization of textile dyes by the purified enzyme

    No full text
    8 páginas, 3 figuras, 5 tablas -- PAGS nros. 141-148A white-rot basidiomycete, isolated from decayed acacia wood (from Northwest of Tunisia) and identified as Trametes trogii, was selected in a broad plate screening because of its ability to degrade commercial dyes. In liquid cultures using a glucose–peptone medium, the sole ligninolytic activity detected was laccase. The highest laccase levels were obtained in presence of CuSO4 as inducer (around 20000 U/l). Two isoenzymes, were purified using anion-exchange and size-exclusion chromatographies. Both isoenzymes are monomeric proteins, with Mw around 62 kDa and isoelectric points of 4.3 and 4.5, showing similar stability at pH and temperature, optimum pH and substrate specificity. The highest oxidation rate was obtained at pH 2 and 2.5 for ABTS and DMP, respectively. They were stable up to 50 °C for 24 h and the stability was higher at alkaline pH. Activity increased by the addition of 10 mM Ni, Mo or Mn but it was not affected by Cd, Al, Li and Ca. Identical N-terminal sequences were determined in both laccases. The crude enzyme, as well as the purified laccase, was able to decolorize dyes from the textile industryThis research has been funded by a Cooperation project between Spain and Tunisia (31p/02 – Spanish “Ministerio de Asuntos Exteriores” and “MRSTDC”), and in part by a grant from “Contrats Programmes MRSTCD” (Tunisia)Peer reviewe

    Acceleration of anthraquinone-type dye removal by white-rot fungus under optimized environmental conditions

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    The decolorization of the recalcitrant dye Remazol Brilliant Blue R (RBBR) by the culture filtrate of Polyporus sp. S133 and the effect of various environmental factors were investigated. Both biodegradation and biosorption were playing an important role in bioremoval mechanisms. The highest biosorption of RBBR in Polyporussp. S133 was shown by all carbon sources such as sucrose, glucose, fructose, and starch. No biosorption was shown by the addition of aromatic compounds and metal ions; 97.1 % RBBR decolorization was achieved in 120-rpm culture for 96 h, as compared to 49.5 % decolorization in stationary culture. Increasing the shaking rotation of the culture to more than 120 rpm was proven to give a negative effect on decolorization. The highest production of laccase was shown at pH 4 and constantly decreases when the pH level increases. The addition of glucose, ammonium tartrate, Cu2+, and protocatechuic acid was the suitable environmental condition for RBBR decolorization. There was a positive relationship between all environmental conditions and laccase production in the decolorization of RBBR

    Clostridium methoxybenzovorans sp. nov., a new aromatic o-demethylating homoacetogen from an olive mill wastewater treatment digester

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    A strictly anaerobic, spore-forming bacterium (3.0-5.0 x 0.4-0.8 micrometers), designated strain SR3T (T = type strain), which stained Gram-positive and possessed a Gram-positive type cell wall was isolated from a methanogenic pilot-scale digester fed with olive mill wastewater (Sfax, Tunisia). It utilized a number of carbohydrates (glucose, fructose, sorbose, galactose, myo-inositol, sucrose, lactose, cellobiose), organic compounds (lactate, betaine, sarcosine, dimethylglycine, methanethiol, dimethylsulfide), alcohol (methanol) and all methoxylated aromatic compounds only in the presence of yeast extract (0.1%). The end products from carbohydrate fermentation were H2, CO2, formate, acetate and ethanol, that from lactate was methanol, those from methoxylated aromatics were acetate and butyrate, and that form betaine, sarcosine, dimethylglycine, methanethiol and dimethylsulfide was only acetate. Strain SR3T was non-motile, had a G+C content of 44 mol% and grew optimally at 37°C and pH 7.4 on a glucose-containing medium. Phylogenetically, the closest relatives of strain SR3T were the non-methoxylated aromatic-degrading #Clostridium xylanolyticum, #Clostridium aerotolerans, #Clostridium sphenoides and #Clostridium celerecrescens (mean similarity of 98%). On the basis of the phenotypic, genotypic and phylogenetic characteristics of the isolate, it is proposed to designate strain SR3T as #Clostridium methoxybenzovorans$ sp. nov. The type strain is SR3T (= DSM 12182T). (Résumé d'auteur
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