• Journal of Environmental Science International
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• v.22 no.9
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• pp.1161-1170
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• 2013

The efficiency of coal-based activated carbon in removing methylene blue (MB) and phenol from aqueous solution was investigated in batch experiments. The batch adsorption kinetics were described by applying pseudo-first-order, pseudo-second-order, and first order reversible reaction. The results showed that the adsorption of MB and phenol occurs complexed process including external mass transfer and intraparticle diffusion. The maximum adsorption capacity obtained from Langmuir isotherm was 461.0 mg/g for MB and 194.6 mg/g for phenol, respectively. The values of activation parameters such as free energy (${\Delta}G^0$), enthalpy (${\Delta}H^0$), and entropy (${\Delta}S^0$) were also determined as -19.0~-14.9 kJ/mol, 25.4 kJ/mol, and 135.2 J/mol K for MB and 51.8~54.1 kJ/mol, -29.0 kJ/mol, and -76.4 kJ/mol K for phenol, respectively. The MB adsorption was found to be endothermic and spontaneous process. However, the CV adsorption was found to be exothermic and non-spontaneous process.

• Advances in environmental research
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• v.4 no.1
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• pp.49-68
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• 2015

Chemically activated and carbonized adsorbents were prepared from Moringa oleifera pod husks (MOP), characterized and evaluated for their ability to remove a common antibiotic - ofloxacin (OFX) from aqueous solution. The pulverized precursor was steeped in a saturated ammonium chloride solution for a day to give the chemically activated adsorbent (AMOP). A portion of AMOP was pyrolyzed in a muffle furnace at 623 K for 30 min to furnish its carbonized analogue (CMOP). The adsorbents showed favorable physicochemical attributes. The effects of operational parameters such as initial OFX solution pH and concentration, adsorbent dosage, temperature and contact time on OFX removal were investigated. At equilibrium, optimal removal efficiencies of 90.98% and 99.84% were achieved at solution pH 5 for AMOP and CMOP, respectively. The equilibrium adsorption data fitted into both the Langmuir and Freundlich isotherms. Gibbs free energy change (${\Delta}G^o$), enthalpy change (${\Delta}H^o$) and entropy change (${\Delta}S^o$) indicated that the adsorption of OFX was feasible, spontaneous, exothermic and occurred via the physisorption mode. Adsorption kinetics obeyed the Blanchard pseudo-second-order model. The results may find applications in the adsorptive removal of micro-contaminants of pharmaceutical origin from wastewater.

• Bulletin of the Korean Chemical Society
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• v.6 no.4
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• pp.186-191
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• 1985

The effect of pressure and temperature on the stabilities of the charge transfer complexes of hexamethyl benzene with iodine in n-hexane has been investigated by UV-spectrophotometric measurements. In this experiment the absorption spectra of mixed solutions of hexamethyl benzene and iodine in n-hexane were measured at 25, 40 and $60^{\circ}C$ under 1,200, 600, 1200 and 1600 bar. The equilibrium constant of the complex formation was increased with pressure while being decreased with temperature raising. Changes of volume, enthalpy, free energy and entropy for the formation of the complexes were obtained from the equilibrium constants. The red shift at higher pressure, the blue shift at higher temperature and the relation between pressure and oscillator strength were discussed by means of thermodynamic functions. In comparison with the results in the previous studies, it can be seen that the pressure dependence of oscillator strength has a extremum behavior in durene as the variation of ${\Delta}H$ or ${\Delta}S$ with the number of methyl groups of polymethyl benzene near atmospheric pressure in the previous study. The shift or deformation of the potential in the ground state and in the excited state of the complexes formed between polymethyl benzene and iodine was considered from the correlation between the differences of the electron transfer energies and the differences of free energies of the complex formation for the pressure variation.

• BMB Reports
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• v.45 no.8
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• pp.476-481
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• 2012

Flavodoxin (Fld) has been demonstrated to bind to ferredoxin-NADP$^+$ reductase A (FprA) in Pseudomonas putida. Two residues ($Phe^{256}$, $Lys^{259}$) of FprA are likely to be important for interacting with Fld based on homology modeling. Site-directed mutagenesis and pH-dependent enzyme kinetics were performed to further examine the role of these residues. The catalytic efficiencies of FprA-$Ala^{259}$ and FprA-$Asp^{259}$ proteins were two-fold lower than those of the wild-type FprA. Homology modeling also strongly suggested that these two residues are important for electron transfer. Thermodynamic properties such as entropy, enthalpy, and heat capacity changes of FprA-$Ala^{259}$ and FprA-$Asp^{259}$ were examined by isothermal titration calorimetry. We demonstrated, for the first time, that $Phe^{256}$ and $Lys^{259}$ are critical residues for the interaction between FprA and Fld. Van der Waals interactions and hydrogen bonding were also more important than ionic interactions for forming the FprA-Fld complex.

• Journal of the Korean Applied Science and Technology
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• v.17 no.2
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• pp.105-112
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• 2000

Surface tension as a function of concentration and temperature was measured for aquous solution of sodium N-acyl sarcosinate, $RCON(CH_{3})CH_{2}$ COONa, From the intersection points in the (${\gamma}-logC$) curves, the critical micelle concentration (cmc) was determined at 20, 30, 40, and $50^{\circ}C$. Structural effects on the cmc maximum and the minimum area per molecule at the aquous solution/air interface were discussed. The free energy, enthalpy, and entropy of micellization and adsorption of surfactant solution also were investigated. Numberous investigators have dealt with sodium N-acyl sarcosinates and their applications as wettings, flooding and reducing agents and as corrosion inhibitors.

• Bulletin of the Korean Chemical Society
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• v.31 no.1
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• pp.146-150
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• 2010

A distinguished class of hydrophobic ionic liquids bearing a Br${\o}$nsted acidic character derived from amide-like compounds were prepared by a neutralization reaction of N,N-diethylformamide, N,N-dibutylformamide, 1-formylpiperidine, and $\varepsilon$-caprolactam with trifluoroacetic acid and physical absorptions of $CO_2$ in these ionic liquids were demonstrated and evaluated. $CO_2$ solubilities in these ionic liquids were influenced by the molecular structure of the cation and were apparently increased with the molar volume. Comparison based on a volume unit reveals that $CO_2$ solubilities in these liquids are relatively higher than those in imidazolium-based ionic liquids. Henry's coefficients calculated from low-pressure solubility tests at 313 to 333 K were used to derive the thermodynamics quantities. Enthalpy and entropy of solvation may share equal contributions in solubility.

• BMB Reports
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• v.31 no.4
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• pp.307-327
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• 1998

Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme which catalyzes the reduction of hydrogen peroxide to water using two equivalents of ferrocytochrome c. The CcP/cytochrome c system has many features which make it a very useful model for detailed investigation of heme protein structure/function relationships including activation of hydrogen peroxide, protein-protein interactions, and long-range electron transfer. Both CcP and cytochrome c are single heme, single subunit proteins of modest size. High-resolution crystallographic structures of both proteins, of one-to-one complexes of the two proteins, and a number of active-site mutants are available. Site-directed mutagenesis studies indicate that the distal histidine in CcP is primarily responsible for rapid utilization of hydrogen peroxide implying significantly different properties of the distal histidine in the peroxidases compared to the globins. CcP and cytochrome c bind to form a dynamic one-to-one complex. The binding is largely electrostatic in nature with a small, unfavorable enthalpy of binding and a large positive entropy change upon complex formation. The cytochrome c-binding site on CcP has been mapped in solution by measuring the binding affinities between cytochrome c and a number of CcP surface mutations. The binding site for cytochrome c in solution is consistent with the crystallographic structure of the one-to-one complex. Evidence for the involvement of a second, low-affinity cytochrome c-binding site on CcP in long-range electron transfer between the two proteins is reviewed.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.31 no.1
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• pp.61-71
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• 1999

The study aimed at the theoretical analysis of vapor sorption properties of, pp.rmaking fibers. Water vapor affinity and sorption thermodynamic properties of fiber constituents were evaluated based on Henry's law and Hildebrand's solubility theory. Theoretical equilibrium moisture content(ThEMC) on fiber surface was estimated using functional group contribution. Crystallinity of cellulose in fiber significantly controlled the water vapor solubility. Comparisons of the measured equilibrium moisture content data and the estimated ThEMC data coincidently suggested the fact that crystallinity of cellulose in fibers was around 60% to 70%. Carbohydrates constituents including amorphous cellulose and hemicellulose in fibers showed higher vapor solubility than lignin molecules. High correlation existed between ThEMC and vapor solubility as well as between ThEMC and solubility parameter. In the thermodynamic analysis on water-vapor sorption process in fibers, the sorption enthalpy increased as RH increased, whereas sorption entropy and free energy decreased with increasing RH.

• Textile Coloration and Finishing
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• v.19 no.4
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• pp.18-25
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• 2007

Kinetics and mechanism for alkaline hydrolysis of C. I. Disperse Green 9(G-9) of dinitrothiophene disperse dye were investigated. As soon as G-9 contacted with alkali, instant and continuous decreases of color strength of G-9 followed with increasing time. The hydrolysis rate of G-9 increased with increasing alkali, and it was found that alkali appeared first order dependence. The observed rate constants obtained from hydrolysis of various amount of dye were similar values, and calculation of initial rates showed that G-9 hydrolyzed by first order reaction for dye. Therefore it was confirmed that the overall reaction was second order, $SN_2$ of nucleophilic substitution reaction. Increasing temperature enhanced the hydrolysis of G-9. From the results of hydrolysis performed at various temperatures, it was obtained that activation energy(Ea) was 12.6 kcal/mole, enthalpy of reaction(${\triangle}H$) was 12.0 kcal/mole, and entropy of reaction(${\triangle}S$) was $29.8J/mol{\cdot}K$.

• Bulletin of the Korean Chemical Society
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• v.14 no.4
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• pp.515-519
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• 1993

The retention behavior of proteins was investigated by using hydrophobic interaction chromatography (HIC), comparing to the results obtained in reversed-phase chromatography (RPC) described in the previous paper. A SynChropak propyl column was employed with 0.05 M phosphate buffer (pH 7.0) containing sodium sulfate. Conformational changes were recognized by examining Z values as a function of sodium sulfate concentration over a range of temperature between 5 and 65$^{\circ}C$. Z values did not change significantly at the range of the temperature showing the consistent ${\Delta}H^{\circ}$ and ${\Delta}S^{\circ}$ values. The sign and the magnitude of ${\Delta}H^{\circ}$ and ${\Delta}S^{\circ}$ of proteins in HIC were compared with those obtained in RPC. The signs of ${\Delta}H^{\circ}$ and ${\Delta}S^{\circ}$ of proteins in HIC were all positive, while those of proteins in RPC were all negative. These results suggested that the retention of proteins in HIC and in RPC were entropy-driven and enthalpy-driven process, respectively. From the two different investigations, it was concluded that the retention mechanism of RPC and HIC was based on the same fundamental principle in which separation is dependent on hydrophobicity, but the retention behavior of the proteins in HIC is clearly different from that observed in RPC.