219 resultados para AMK22-2289


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This study was carried out to determine the best digestible energy and digestible protein ratio in feeds for Nile tilapia (Oreochromis niloticus) juveniles 30.0 +/- 4.21 g) based on digestible amino acids and the ideal protein concept). Twelve rations were formulated with protein levels 22.0; 26.0; 30.0 and 34.0% of digestible protein and levels 3,000, 3,300 and 3,600 kcal/kg digestible energy. The digestible energy/digestible protein ratio was between 8.94 and 15.19 kcal/g. Three hundred and twenty four tilapias were randomly distributed in thirty six 250 L circular tanks at a density of 9 fish/tank, a total of 12 treatments with three replications. After 60 days, there was no significant difference in weight gain, daily weight gain and feed conversion ratio among the studied treatments. A linear increase was observed in fillet yield with increasing digestible protein. With respect to feed cost/kg weight gain, the treatment with 30.0% DP and 3,000 kcal/kg DE presented low cost and better cost effectiveness index. Therefore, it was concluded that digestible energy did not influence the productive performance parameters and that effective feeds can be formulated with DP levels lower than 34% when feeding juvenile tilapias. The ration should be formulated based on the concept of ideal protein.

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The alkalophilic Bacillus circulans D1 was isolated from decayed wood. It produced high levels of extracellular cellulase-free xylanase. The enzyme was thermally stable up to 60°C, with an optimal hydrolysis temperature of 70°C. It was stable over a wide pH range (5.5-10.5), with an optimum pH at 5.5 and 80% of its activity at pH 9.0. This cellulase-free xylanase preparation was used to biobleach kraft pulp. Enzymatic treatment of kraft pulp decreased chlorine dioxide use by 23 and 37% to obtain the same kappa number (κ number) and brightness, respectively. Separation on Sephadex G-50 isolated three fractions with xylanase activity with distinct molecular weights.

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This article investigates a strain of the yeast Aureobasidium pullulans for cellulase and hemicellulase production in solid state fermentation. Among the substrates analyzed, the wheat bran culture presented the highest enzymatic production (1.05 U/mL endoglucanase, 1.3 U/mL β-glucosidase, and 5.0 U/mL xylanase). Avicelase activity was not detected. The optimum pH and temperature for xylanase, endoglucanase and β-glucosidase were 5.0 and 50, 4.5 and 60, 4.0 and 75°C, respectively. These enzymes remained stable between a wide range of pH. The β-glucosidase was the most thermostable enzyme, remaining 100% active when incubated at 75°C for 1 h. © 2007 Humana Press Inc.

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The texture of concrete blocks is very important and is often the decisive factor when choosing a product, particularly if the building specifications call for high-strength blocks allied to low-cost finish, in which case exposed blocks with a closer texture are often preferred. Furthermore, a closer texture, especially for exteriors, may be a vital factor in ensuring the building's durability. At present, however, there is no standard to quantify the texture of a structural block. Further, when studying masonry blocks compressive strength should never be overlooked. This article discusses a procedure to produce concrete block textures with and without the addition of lime, but still to achieve the required compressive strength. The method used in this study, to evaluate texture, proved to be simpler and cheaper than methods reported by other authors in the literature. The addition of small quantities of lime proved beneficial for both texture and compressive strength. Increasing the amount of lime further, however, only improved texture.

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The purpose of this work was to purify a protease from Penicillium waksmanii and to determine its biochemical characteristics and specificity. The extracellular protease isolated that was produced by P. waksmanii is a serine protease that is essential for the reproduction and growth of the fungus. The protease isolated showed 32 kDa, and has optimal activity at pH 8.0 and 35 C towards the substrate Abz-KLRSSKQ-EDDnp. The protease is active in the presence of CaCl2, KCl, and BaCl, and partially inhibited by CuCl2, CoCl2 and totally inhibited by AlCl3 and LiCl. In the presence of 1 M urea, the protease remains 50 % active. The activity of the protease increases 60 % when it is exposed to 0.4 % nonionic surfactant-Triton X-100 and loses 10 % activity in the presence of 0.4 % Tween-80. Using fluorescence resonance energy transfer analysis, the protease showed the most specificity for the peptide Abz-KIRSSKQ-EDDnp with k cat/K m of 10,666 mM-1 s-1, followed by the peptide Abz-GLRSSKQ-EDDnp with a k cat/K m of 7,500 mM -1 s-1. Basic and acidic side chain-containing amino acids performed best at subsite S1. Subsites S2, S3, S′ 2, and S′ 1, S ′ 3 showed a preference for binding for amino acids with hydrophobic and basic amino acid side chain, respectively. High values of k cat/K m were observed for the subsites S2, S3, and S′ 2. The sequence of the N-terminus (ANVVQSNVPSWGLARLSSKKTGTTDYTYD) showed high similarity to the fungi Penicillium citrinum and Penicillium chrysogenum, with 89 % of identity at the amino acid level. © 2012 Springer Science+Business Media New York.

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Microbial β-glucosidases have been used for the enhancement of wine aroma. Nevertheless, few enzymes are active in the conditions of winemaking. In this work, the production of a β-glucosidase by an Aureobasidium pullulans strain (Ap-β-gl) isolated from grape ecosystems was evaluated. The maximum enzymatic synthesis using submerged fermentation was after 96 h of growth in complex media containing 20 g/L of cellobiose as the sole carbon source. The crude enzyme (Ap-β-gl) showed optimal pH at 5.5 and two peaks of optimum temperature (at 45 and 70 C). It showed a wide range of pH stability, stability at low temperatures, and tolerance to ethanol, showing suitable characteristics for winemaking conditions. The hydrolysis of glycosidic terpenes by Ap-β-gl was studied, and its ability to efficiently release free terpenols was demonstrated by gas chromatography/mass spectrometry. The enzymatic treatment notably increased the amount of monoterpenes, showing good prospects for its potential application for the development of aroma in wines. © 2012 Springer Science+Business Media New York.

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