Finite Bath Adsorption Of 0-galactosidase Onto Monoclonal Antibody Ligand Immobilized On Nonporous Glass Coated Beads
The dynamic experimental data of the finite bath adsorption of β-galactosidase onto monoclonal anti-β-galactosidase ligand immobilized on nonporous glass coated beads, are presented for four different temperatures. Mathematical models that describe the finite bath adsorption of a single adsorbate onto ligand immobilized on nonporous particles, are constructed, and it is found that the overall adsorption rate of β-galactosidase is controlled by film mass transfer and the dynamics of the interaction mechanism (adsorption step). The agreement between experiment and theory is reasonable when the dynamics of the interaction mechanism are described by a second-order reversible kinetic model. Also, the estimated values of the association constant of specific adsorption (interaction of β-gaIactosidase with immobilized anti-β-galactosidase) were significantly larger than those of nonspecific adsorption (interaction of β-galactosidase with a control adsorbent). Furthermore, the values of the association constant of specific adsorption are increasing with increasing temperature, and the heat of adsorption is positive (AH > 0). The fact that AH > 0, whereas the adsorption proceeds spontaneously (AG<0), indicates that the adsorption of β-galactosidase onto monoclonal anti-β-galactosidase immobilized on nonporous glass coated beads, is entropically driven. © 1991, Taylor & Francis Group, LLC. All rights reserved.
M. A. Mccoy et al., "Finite Bath Adsorption Of 0-galactosidase Onto Monoclonal Antibody Ligand Immobilized On Nonporous Glass Coated Beads," Chemical Engineering Communications, vol. 108, no. 1, pp. 225 - 242, Taylor and Francis Group; Taylor and Francis, Sep 1991.
The definitive version is available at https://doi.org/10.1080/00986449108910960
Chemical and Biochemical Engineering
Keywords and Phrases
Adsorption β; Affinity chromatography; Biospecific adsorption; Galactosidase immobilized ligand; Modeling
International Standard Serial Number (ISSN)
Article - Journal
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01 Sep 1991