135 resultados para Sodium Dodecyl Sulfate


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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Moringa oleifera Lam, is a leguminous plant, originally from Asia, which is cultivated in Brazil because of its low production cost. Although some people have used this plant as food, there is little information about its chemical and nutritional characteristics. The objective of this study was to characterise the leaves of M. oleifera in terms of their chemical composition, protein fractions obtained by solubility in different systems and also to assess their nutritional quality and presence of bioactive substances. The whole leaf flour contained 28.7% crude protein, 7.1% fat, 10.9% ashes, 44.4% carbohydrate and 3.0 mg 100 g(-1) calcium and 103.1 mg 100 g(-1) iron. The protein profile revealed levels of 3.1% albumin, 0.3% globulins, 2.2% prolamin, 3.5% glutelin and 70.1% insoluble proteins. The hydrolysis of the protein from leaf flour employing sodium dodecyl sulfate (SDS) and 2-mercaptoethanol (ME) resulted in 39.5% and 29.5%, respectively. The total protein showed low in vitro digestibility (31.8%). The antinutritional substances tested were tannins (20.7 mg g(-1)), trypsin inhibitor (1.45 TIU mg g(-1)), nitrate (17 mg g(-1)) and oxalic acid (10.5 mg g(-1)), besides the absence of cyanogenic compounds. beta-Carotene and lutein stood out as major carotenoids, with concentrations of 161.0 and 47.0 mu g g(-1) leaf, respectively. Although M. oleifera leaves contain considerable amount of crude protein, this is mostly insoluble and has low in vitro digestibility, even after heat treatment and chemical attack. In vivo studies are needed to better assess the use of this leaf as a protein source in human feed. (C) 2013 Elsevier Ltd. All rights reserved.

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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

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An extracellular pectin lyase secreted by Fusarium decemcellulare MTCC 2079 under solid state fermentation condition has been purified to electrophoretic homogeniety by using ammonium sulfate fractionation, carboxymethyl cellulose and gel filtration (Sephadex G-100) column chromatographies. The purified enzyme showed single protein band corresponding to molecular mass 45 +/- 01 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme had maximum activity at pH 9.0 and showed maximum stability in the pH range of 9.0-12.0. The optimum temperature of the purified enzyme was 50 degrees C and it showed maximum stability upto 40 degrees C. The energy of activation for the thermal denaturation (Ea) was 59.06 kJ mol(-1) K-1. The K-m and k(cat) values using citrus pectin as the substrate were 0.125mgml(-1) and 72.9 s(-1) in 100mM sodium carbonate buffer pH 9.0 at 50 degrees C. The biophysical studies on pectin lyase showed that its secondary structure belongs to alpha+beta class of protein with comparatively less of beta-sheets. Purified pectin lyase showed efficient retting of Crotolaria juncea fibers.

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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This work aims to study the structural characteristics of silica gels obtained from the acid hydrolysis of tetraethoxysilane (TEOS) in water solutions with different concentrations of sodium dodecyl sulfate (SDS). The structural characteristics were studied in stages ranging from the wet gel to the dry stages of the gels (aerogels and xerogels). Aerogels were obtained by ambient pressure drying (APD) after silylation process using trimethylchlorosilane (TMCS) as silylating agent. Xerogels were obtained by conventional evaporating the liquid phase from non silylated gels. The samples were characterized by nitrogen adsorption and small angle X-ray scattering (SAXS). The structure of the wet gels and of the aerogels prepared with the surfactant exhibited characteristics of mass-fractal structures with fractal dimension D in the range 2.1-2.2 for the wet gels and 2.3-2.4 for the aerogels. The characteristic size  of the fractal domain reduces while the size a0 of the primary silica particle composing the fractal structure increases with the drying of the gels, in a process in which share of the porosity is eliminated. Aerogels exhibited typical values for the specific surface of 900 m2g-1 and of 3.5 cm3.g-1 for the total pore volume. These values are correspondingly comparable to those of the aerogels prepared by supercritical drying, since the silylation process replaces hydrophilic –OH groups by hydrophobic –Si-R3 ones, inhibiting the porosity elimination on drying. The silica particle size also increases lightly with the silylation because the attachment of the –Si-R3 groups on the silica surface. The pore size distribution curves of the aerogels are similar for all samples exhibiting a maximum in around 40 nm, independent the concentration of surfactant. This suggests that the characteristic size of 40 nm is due to the association of surfactant micelles... (Complete abstract click electronic access below)

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Pós-graduação em Medicina Veterinária - FCAV

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)