FINITE BATH ADSORPTION OF β-GALACTOSIDASE ONTO MONOCLONAL ANTIBODY LIGAND IMMOBILIZED ON NONPOROUS GLASS COATED BEADS

Abstract

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-galactosidase 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 (ΔH > 0). The fact that ΔH > 0, whereas the adsorption proceeds spontaneously ( ΔH < 0), indicates that the adsorption of β-galaclosidasc onto monoclonal anti-β-galactosidase immobilized on nonporous glass coated beads, is entropically driven ( ΔS > 0).

KEYWORDS:

• Adsorption
• β-Galactosidase
• immobilized ligand
• Biospecific adsorption
• Affinity chromatography
• Modeling

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