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ABSTRACT: In this work the use of silkworm pupa, which is the waste of silk spinning industries has been investigated as an adsorbent for the removal of C.I. Basic Blue 41. The amino acid nature of the pupa provided a reasonable capability for dye removal. Equilibrium adsorption isotherms and kinetics were investigated. The adsorption equilibrium data were analyzed by using various adsorption isotherm models and the results have shown that adsorption behavior of the dye could be described reasonably well by either Langmuir or Freundlich models. The characteristic parameters for each isotherm have been determined. The monolayer adsorption capacity was determined to be 555 mg/g. Kinetic studies indicated that the adsorption follows pseudo-second-order kinetics with a rate constant of 0.0434 and 0.0572 g/min mg for initial dye concentration of 200 mg/l at 20 and 40 degrees C, respectively. Kinetic studies showed that film diffusion and intra-particle diffusion were simultaneously operating during the adsorption process. The rate constant for intra-particle diffusion was estimated to be 1.985 mg/g min(0.5).
Journal of Hazardous Materials 02/2007; 139(1):167-74. · 4.17 Impact Factor
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ABSTRACT: The interactions between bilirubin and human serum albumin (HSA) were studied by isothermal titration calorimetry (ITC) and UV-vis spectrophotometry at 27 degrees C in 100 mM phosphate buffer pH 7.4 containing 1 mM EDTA. The biphasic shape of the HSA-bilirubin binding curve depicted the existence of two bilirubin binding sets on the HSA structure which had distinct binding interactions. Each binding set contained one or more bilirubin binding site. The first binding set at subdomain IIA included one binding site and had a more hydrophobic microenvironment than the other two binding sites in the second bilirubin binding set (subdomain IIIA). With our method of analysis, the calculated dissociation constant of the first binding site is 1.28 x 10(-6) M and 4.80 x 10(-4) M for the second and third binding sites. Here, the typical Boltzmann's equation was used with a new approach to calculate the dissociation constants as well as the standard free energy changes for the HSA-bilirubin interactions. Interestingly, our calculations obtained using the Wyman binding potential theory confirmed that our analysis method had been correct (especially for the second binding phase). The molar extinction coefficient determined for the first bound bilirubin molecule depicted that the bilirubin molecules (in low concentrations) should interact with the nonpolar microenvironment of the first high affinity binding site. Binding of the bilirubin molecules to the first binding site was endothermic (deltaH > 0) and occurred through the large increase in the binding entropy established when the hydrophobic bilirubin molecules escaped from their surrounding polar water molecules and into the hydrophobic medium of the first binding site. On the other hand, the calculated molar extinction coefficient illustrated that the microenvironment of the second binding set (especially for the third binding site) was less hydrophobic than the first one but still more hydrophobic than the buffer medium. The binding of the third bilirubin molecule to the HSA molecule was established more through exothermic (electrostatic) interactions.
The Protein Journal 04/2006; 25(3):193-201. · 1.04 Impact Factor
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ABSTRACT: This paper presents a novel two-phase flux-reversal permanent magnet generator for application in high speed power generation. The machine structure is like an axial flux generator. To reduce the output frequency and iron losses, the number of rotor and stator poles is chosen equal 2 and 4 respectively. The robustness and simplicity of the rotor structure is suitable for high speeds. By using finite element method, the static characteristic of the proposed generator are given.
Power Electronics and Drives Systems, 2005. PEDS 2005. International Conference on; 12/2005
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ABSTRACT: The reaction kinetics of the Autocatalytic Oxidation of L-asparagine by permanganate ions has been investigated in moderately strong acid medium using the spectrophotometric technique. In all cases studied, an autocatalytic effect due to Mn2+ ions formed as a reaction product was observed. Both catalytic and noncatalytic processes were determined to be first order with respect to the permanganate ions while a first and a fractional order with respect to the amino acid for noncatalytic and catalytic reactions were obtained, respectively. The overall rate equation for this process may be written asd[MO4
–]/dt= k1[MnO4
–]+k2[MnO4
–][Mn+2],where k1 and k2 are rate pseudoconstants for noncatalytic and catalytic reactions, respectively. The influence of some factors such as temperature and reactant concentration on the rate constants has been studied, and the activation parameters have been calculated. Reaction mechanisms satisfying observations for both catalytic and noncatalytic routes have been presented.
Kinetics and Catalysis 04/2004; 45(3):351-358. · 0.64 Impact Factor
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Dyes Pigm. 72:331-338.
