Optimization of multiple parameters for adsorption of arsenic (III) from aqueous solution using Psidium guajava leaf powder.

The conventional method of water treatment using activated carbon from several sources has been focused on extensively in the last two decades. However, rare attention has been noticed on natural adsorbents such as plant leaves. Therefore, the Psidium guajava (guava) leaf has been investigated to understand its adsorption efficacy for Arsenic (III) [As(III)] in this study. The effect of process variables, e.g., pH, concentration of metal ion, adsorbent's particle size, and dosages, are evaluated. Experiments are carried out in batch mode, and the individual and combined parameter's impact on adsorption have been discussed. Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM) is used to characterize the adsorbent's surface. Freundlich and Langmuir's isotherms are used for adsorption equilibrium study. The adsorption parameters are optimized by establishing a regression correlation using central composite design (CCD) of response surface methodology (RSM). The analysis of variance (ANOVA) suggests a high regression coefficient (R2 = 0.9249) for the removal of As(III). Particle size of 0.39 mm; adsorbent's height of 10 cm; metal ion concentration of 30 ppm, and pH 6 are optimized to remove 90.88% As(III) from aqueous solution. HCl is evaluated as a potential solvent for desorption of arsenic from the desorption study.

Lipase catalyzed transesterification of ethyl butyrate synthesis in n-hexane- a kinetic study.

Kinetics of lipase catalyzed transesterification of ethyl caprate and butyric acid was investigated. The objective of this work was to propose a reaction mechanism and develop a rate equation for the synthesis of ethyl butyrate by transesterification using surfactant coated lipase from Candida rugosa. The reaction rate could be described in terms of Michaelis-Menten equation with a Ping-Pong Bi-Bi mechanism and competitive inhibition by both the substrates. The values of kinetic parameters computed were Vmax = 2.861 µmol/min/mg; Km(acid) = 0.0746 M; Km(ester) = 0.125 M; Ki acid = 0.450 M. This study indicated a competitive enzyme inhibition by butyric acid during lipase catalyzed transesterification reaction. Experimental observations had clearly indicated that the substrates as well as product act as dead-end inhibitors.