http://dns2.asia.edu.tw/~ysho/YSHO-English/1000%20WC/PDF/Pro%20Bio34,%20451.pdf

Pseudo-second order model for sorption processes

http://dns2.asia.edu.tw/~ysho/YSHO-English/Publications/PDF/Che%20Eng%20J70,%20115.pdf

Sorption of dye from aqueous solution by peat

http://repository.ust.hk/ir/bitstream/1783.1-645/1/323k.pdf

A comparison of chemisorption kinetic models applied to pollutant removal on various sorbents

A review of the mechanisms of solute sorption onto various biosorbents has been performed. The mechanisms have been subdivided into reaction based systems and diffusion based systems and the literature has been reviewed in accordance with these two groups. The range of solute-sorbent systems reviewed include metal ions, dyestuffs and several organic substances in aqueous systems onto a wide range of biosorbents and mineral earths. Extensive tables are presented summarising isotherm types, sorption capacities, kinetic models which have been applied particularly to biosorbent systems but also to many other adsorbent materials.

http://dns2.asia.edu.tw/~ysho/YSHO-English/Publications/PDF/Sep%20Pur%20Met29,%20189.pdf

Kinetics of pollutant sorption by biosorbents: review

On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon

Activation Parameters for Kinetics of Protein Adsorption at Silica-Water Interface

Kinetics of Desorption of Proteins from the Surface of Protein-Coated Alumina by Various Desorbing Reagents

Excess adsorption of lysozyme and water at solid-liquid interfacesα

The adsorption of oligomeric protein, hemoglobin from aqueous solution to the surfaces of silica, alumina, chromium, resin (Cl - form), carbon and sephadex have been studied as functions of bulk aqueous protein concentrations at various values of pH, ionic strength and temperature of the system. The shape and monolayer points of the adsorption isotherms have been analysed and factors responsible for positive and negative adsorption of hemoglobin at different surfaces have been discussed. The low values of maximum adsorption of hemoglobin obtained for several types of surfaces indicates that the quaternary structure of four polypeptide chains of the oligomeric protein are probably broken at the interface and the protein is adsorbed as a single polypeptide chain having tertiary structure close to that of myoglobin. Further, using an universal scale of thermodynamics, an attempt has been made to explain and compare the maximum affinities for different surfaces in terms of standard free energies (ΔG 0 ) of adsorption per square meter of the surface. The standard free energy (ΔG 0 B) for the transfer of one mole of protein from bulk water to the surface is observed to be ±40 kJ/mol and this value is independent of pH, ionic strength and temperature.

Deepa Sarkar

Papers

Activation Parameters for Kinetics of Protein Adsorption at Silica-Water Interface

Kinetics of Desorption of Proteins from the Surface of Protein-Coated Alumina by Various Desorbing Reagents

Excess adsorption of lysozyme and water at solid-liquid interfacesα

Excess Adsorption of Hemoglobin at Solid-Liquid Interfaces