Biosorption of oxybenzene using biosorbent prepared by raw wastes of Zea mays and comparative study by using commercially available activated carbon

Organic pollutants present in waste water have undesirable effect on the environment. Industry activities are the key sources of organic pollutants. Prime pollutants released from various sources react instantly with the environment and become derived (secondary) pollutants, which stay for an elongated time. The present research work has been carried out using biosorbent prepared from various Zea mays wastes for elimination of oxybenzene. Different parameters viz contact time, initial concentration; adsorbent dose, temperature and pH were optimized for the biosorption of oxybenzene on to the biosorbent samples. BCS (Baby corn silk) showed higher percentage of biosorption at optimum contact time of 3 h, pH between 5 and 6 and temperature at 25 °C. Analysis of equilibrium biosorption data in terms of several isotherm models revealed that Langmuir isotherm and Freundlich isotherm indicates better agreement with the experimental data. The kinetics of oxybenzene biosorption on to the biosorbents was described with the pseudo-first-order model. Thermodynamic parameters indicated that biosorption onto biosorbent was feasible in nature, spontaneous, and endothermic for some biosorbents, but on contrary not feasible, exothermic and non spontaneous for other biosorbents. The result of this study showed that the biosorbent derived from Zea mays can be used as a prospective biosorbent for oxybenzene in wastewater and also can be an alternative for the commercially activated carbon.     

Transient-phase studies on the creatine kinase reaction. The analysis of a reaction pathway with three intermediates.

1. The initial formation of creatine phosphate by creatine kinase was studied in the millisecond range and the effect of temperature on the transient and steady-state phases exploited. 2. At 25 degrees C and 35 degrees C there was no transient phase. This is in agreement with the results of Gutfreund [Engelborghs, Y., Marsh, A., and Gutfreund, H. (1975) Biochem. J. 151, 47--50]. 3. At 4 degrees C the time course of creatine phosphate formation was complex and consisted of three transient phases: a lag phase, a burst phase and a steady-state phase. Based on this result a reaction scheme for creatine kinase which includes three intermediates was proposed. Despite the completeness of the time course, the extraction of estimates for the rate constants was difficult and computer simulation and iterative methods had to be resorted to. 4. Attempts were made to provide evidence for the complex enzyme.ADP.metaphosphate.creatine on the creatine kinase reaction pathway [cf. Milner-White, E.J. and Watts, D.C. (1971) Biochem. J. 122, 727--740]. Under the conditions used these attempts were unsuccessful at times down to 2.5 ms, at 4 degrees C or 35 degrees C.     

Studies on the Effect of Dust–Ion Collision on Dust–Ion Acoustic Solitary Waves in a Magnetized Dusty Plasma in the Framework of Damped KP Equation and Modified Damped KP Equation

Plasma Physics Reports - The influence of the dust–ion collision effect on the propagation of ion–acoustic waves (IAWs) in a collisional magnetized dusty plasma containing positive...     

Thermodynamics of the two step formation of horseradish peroxidase compound I

The effects of temperature (20 to -38 degrees C), pressure (normal pressures to 1.2 kbar) and solvent (water, 60% DMSO and 50% methanol) on the reaction of hydrogen peroxide or ethyl peroxide with horseradish peroxidase were studied. The formation of compound I was followed at 403 nm in a stopped flow apparatus adapted for high pressure and low temperature work. As with the alkaline form (Job and Dunford 1978), the neutral form of the peroxidase binds peroxide substrates in two steps. It was the combined use of organic solvents and low temperatures which revealed saturation kinetics: (Formula: see text) compound I, where E = horseradish peroxidase and S peroxide substrate. In water and organic solvents at temperatures above -10 degrees C, K1 was too small and k2 too large to be measured, here K1 X k2 was obtained. k-2 was too small for measurement under all conditions. Whereas K1 was insensitive to the peroxide substrate and solvent composition, k2 was very sensitive. The thermodynamic parameters delta H, delta S and delta V for K1 and k2 were obtained under different experimental conditions and the data are interpreted within the available thermodynamic theories.     

Substituents effects on activity of kynureninase from Homo sapiens and Pseudomonas fluorescens

A series of substituted kynurenines (3-bromo-dl, 3-chloro-dl, 3-fluoro-dl, 3-methyl-dl, 5-bromo-l, 5-chloro-l, 3,5-dibromo-l and 5-bromo-3-chloro-dl) have been synthesized and tested for their substrate activity with human and Pseudomonas fluorescens kynureninase. All of the substituted kynurenines examined have substrate activity with both human as well as P. fluorescens kynureninase. For the human enzyme, 3- and 5-substituted kynurenines have k_cat and k_cat/K_m values higher than l-kynurenine, but less than that of the physiological substrate, 3-hydroxykynurenine. However, 3,5-dibromo- and 5-bromo-3-chlorokynurenine have k_cat and k_cat/K_m values close to that of 3-hydroxykynurenine with human kynureninase. The effects of the 3-halo substituents on the reactivity with human kynureninase may be due to electronic effects and/or halogen bonding. In contrast, for the bacterial enzyme, 3-methyl, 3-halo and 3,5-dihalokynurenines are much poorer substrates, while 3-fluoro, 5-bromo, and 5-chlorokynurenine have k_cat and k_cat/K_m values comparable to that of its physiological substrate, l-kynurenine. Thus, 5-bromo and 5-chloro-l-kynurenine are good substrates for both human as well as bacterial enzyme, indicating that both enzymes have space for substituents in the active site near C-5. The increased activity of the 5-halokynurenines may be due to van der Waals contacts or hydrophobic effects. These results may be useful in the design of potent and/or selective inhibitors of human and bacterial kynureninase.     

Relative preference of Lygus hesperus (Hemiptera: Miridae) to selected host plants in the field

Abstract Information on host plant preference of agriculturally important insect pests, such as Lygus hesperus (Knight), can be helpful in predicting its occurrence and future movement among crop and non-crop host plants. A field study was conducted during 2005 and 2006 to evaluate the host preference of Lygus to cotton and four other host plants in the Texas High Plains, including alfalfa (Medicago sativa L.), wild sunflower (Helianthus annuus L.), Russian thistle (Salsola iberica L.) and pigweed (Amaranthus palmeri L.). Sampling for both nymphs and adults during 2005 (July to November) and 2006 (June to November) showed that alfalfa and Russian thistle were the two most preferred hosts out of the five hosts evaluated. Abundance of nymphs (numbers per 50 sweeps per host plant) during the sampling period also indicated the superior reproductive suitability of alfalfa and Russian thistle. Cotton appeared to be the least attractive host plant for Lygus when Russian thistle and alfalfa were available in the host mosaic. Seasonal abundance of Lygus was found to be lower during 2006 compared to 2005, which may be explained by the difference in rainfall patterns during these two years. In terms of species dominance, L. hesperus was the most dominant species in the sampled population followed by an inconsiderable fraction of L. elisus and L. lineolaris.     

Stay-green trait serves as yield stability attribute under combined heat and drought stress in wheat (Triticum aestivum L.)

Plant Growth Regulation - The present study was conducted to evaluate the effect of a stay-green trait to stabilize the yield responses under combined heat and drought stress on wheat. Ten...