210 resultados para 2289


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The effects of soybean and castorbean meals were evaluated separately, and in combinations at different ratios, as substrates for lipase production by Botryosphaeria ribis EC-01 in submerged fermentation using only distilled water. The addition of glycerol analytical grade (AG) and glycerol crude (CG) to soybean and castorbean meals separately and in combination, were also examined for lipase production. Glycerol-AG increased enzyme production, whereas glycerol-CG decreased it. A 24 factorial design was developed to determine the best concentrations of soybean meal, castorbean meal, glycerol-AG, and KH2PO4 to optimize lipase production by B. ribis EC-01. Soybean meal and glycerol-AG had a significant effect on lipase production, whereas castorbean meal did not. A second treatment (22 factorial design central composite) was developed, and optimal lipase production (4,820 U/g of dry solids content (ds)) was obtained when B. ribis EC-01 was grown on 0.5 % (w/v) soybean meal and 5.2 % (v/v) glycerol in distilled water, which was in agreement with the predicted value (4,892 U/g ds) calculated by the model. The unitary cost of lipase production determined under the optimized conditions developed ranged from US$0.42 to 0.44 based on nutrient costs. The fungal lipase was immobilized onto Celite and showed high thermal stability and was used for transesterification of soybean oil in methanol (1:3) resulting in 36 % of fatty acyl alkyl ester content. The apparent K m and V max were determined and were 1.86 mM and 14.29 μmol min -1 mg-1, respectively. © 2013 Springer Science+Business Media New York.

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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An extracellular ethanol-tolerant β-glucosidase from Sporidiobolus pararoseus was purified to homogeneity and characterized, and its potential use for the enhancement of wine aroma was investigated. The crude enzymatic extract was purified in four steps (concentration, dialysis, ultrafiltration, and chromatography) with a yield of around 40 % for total activity. The purified enzyme (designated Sp-βgl-P) showed a specific activity of approximately 20.0 U/mg, an estimated molecular mass of 63 kDa after sodium dodecyl sulfate polyacrylamide gel electrophoresis, and isoelectric point of 5.0 by isoelectric focusing. Sp-βgl-P has optimal activity at pH 4.0 and at 55 °C. It was stable in a broad pH range at low temperatures and it was tolerant to ethanol and glucose, indicating suitable properties for winemaking. The hydrolysis of glycosidic terpenes was analyzed by adding Sp-βgl-P directly to the wines. The released terpene compounds were evaluated by gas chromatography/mass spectrometry. The enzymatic treatment significantly increased the amount of free terpenes, suggesting that this enzyme could potentially be applicable in wine aroma improvement. © 2013 Springer Science+Business Media New York.

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Vigencia de los aportes de Celso Furtado al estructuralismo / Ricardo Bielschowsky. -- Obsolescencia de la protección a los inversores extranjeros después de la crisis argentina / Michael Mortimore y Leonardo Stanley. -- Una aproximación al enfoque de derechos en las estrategias y políticas de desarrollo / Víctor Abramovich. -- ¿Pueden los países de América Latina y el Caribe emular el modelo irlandés para atraer inversión extranjera directa? / Ruth Ríos-Morales y David O ’Donovan. -- El lento retorno de las políticas industriales en América Latina y el Caribe / Wilson Peres. -- Un modelo de bajo crecimiento: la informalidad como restricción structural / Mario Cimoli, Annalisa Primi y Maurizio Pugno. -- El mercado de trabajo argentino en la globalización financier / Mario Damill y Roberto Frenkel. -- Precariedad social en México y Argentina: tendencias, expresiones y trayectorias nacionales / María Cristina Bayón. -- Pacto Fiscal en Guatemala: lecciones de una negociación / Juan Alberto Fuentes K. y Maynor Cabrera. -- Cambio de la estructura productiva en Chile, 1986-1996: producción e interdependencia industrial / José Miguel Albala-Bertrand. -- Orientaciones para los colaboradores de la Revista de la CEPAL. -- La Revista de la CEPAL en Internet. -- Publicaciones recientes de la CEPAL.

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Celso Furtado’s contributions to structuralism and their relevance today / Ricardo Bielschowsky. -- Has investor protection been rendered obsolete by the Argentine crisis? / Michael Mortimore and Leonardo Stanley. -- The rights-based approach in development policies and strategies / Victor Abramovich. -- Can the Latin American and Caribbean countries emulate the Irish model of FDI attraction? / Ruth Rios-Morales and David O’Donovan. -- The slow comeback of industrial policies in Latin America and the Caribbean / Wilson Peres. -- A low-growth model: informality as a structural constraint / Mario Cimoli, Annalisa Primi and Maurizio Pugno. -- The Argentine labour market in a financially globalized world / Mario Damill and Roberto Frenkel. -- Social precarity in Mexico and Argentina: trends, manifestations and national trajectories / María Cristina Bayón. -- The Fiscal Covenant in Guatemala: lessons learned from the negotiations / Juan Alberto Fuentes K. and Maynor Cabrera. -- Changes in Chile’s production structure, 1986-1996: output and industrial interdependence / José Miguel Albala-Bertrand. -- Guidelines for contributors to the CEPAL Review. -- CEPAL Review on the Internet. -- Recent ECLAC publications.

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Streblin, a serine proteinase from plant Streblus asper, has been used to investigate the conformational changes induced by pH, temperature, and chaotropes. The near/far UV circular dichroism activities under fluorescence emission spectroscopy and 8-aniline-1-naphthalene sulfonate (ANS) binding have been carried out to understand the unfolding of the protein in the presence of denaturants. Spectroscopic studies reveal that streblin belongs to the alpha+beta class of proteins and exhibits stability towards chemical denaturants, guanidine hydrochloride (GuHCl). The pH-induced transition of this protein is noncooperative for transition phases between pH 0.5 and 2.5 (midpoint, 1.5) and pH 2.5 and 10.0 (midpoint, 6.5). At pH 1.0 or lower, the protein unfolds to form acid-unfolded state, and for pH 7.5 and above, protein turns into an alkaline denatured state characterized by the absence of ANS binding. At pH 2.0 (1M GuHCl), streblin exists in a partially unfolded state with characteristics of amolten globule state. The protein is found to exhibit strong and predominant ANS binding. In total, six different intermediate states has been identified to show protein folding pathways.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)