The kinetics of adsorption of bovine serum albumin on an anion-exchange resin were measured in a batch system using a flow cell and ultraviolet absorbance, as a function of initial liquid-phase protein concentration and solid-to-liquid phase ratio. A new mathematical model for adsorption kinetics is
Kinetic modeling of proteins adsorption with a methodology of error analysis
✍ Scribed by Leôncio Diógenes Tavares Câmara; Cesar Costapinto Santana; Antônio José da Silva Neto
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 456 KB
- Volume
- 30
- Category
- Article
- ISSN
- 1615-9306
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✦ Synopsis
Abstract
The estimation of adsorption parameters for chromatographic systems is a very important step for column characterization used in the design of continuous separation equipments. The turbulent hydrodynamics aspect of batch procedures makes the kinetic modeling an interesting tool for the process modeling used for the determination of the main parameters that will be considered in the equipment design. The implemented irreversible kinetic model, which depends on both solute and site concentrations, was found to be very effective in the experimental correlation of two different enzyme adsorption systems: adsorption of Inulinases and β‐Galactosidase using two different adsorbents, the CM‐Sepharose CL‐6B and Accell plus QMA, respectively. The implementation of an error analysis methodology associated with an inverse problem approach was successful in determining the kinetic parameters with high accuracy. The simulations indicated a decrease in the kinetic constants with an increase in the solute concentration, which can be related to the increase in the competition by sites of adsorption.
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