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Abstract
In this study, poly(glycidyl methacrylate) [PGMA] microbeads with surface modified iminodiacetic acid (IDA) were used for myoglobin (Mb) adsorption from buffer solutions at different pHs and ionic strengths in a packed-bed column. Attenuated Total Reflectance Fourier Transformed Infrared (ATR-FTIR) spectroscopy and scanning electron microscopy (SEM) measurements before and after the adsorption process confirmed the structural stability of adsorbed Mb. The effects of initial concentration, flow-rate, pH and ionic strength on the adsorption were investigated. The results showed that the maximum amount of protein was adsorbed at a pH 7.0, which is the protein isoelectric point. The adsorption is rationalized in terms of local electrostatic forces acting between the protein and the IDA modified PGMA surface as well as hydrophobic interactions close to the protein isoelectric point, whereas at low pH the global changes give rise to protein–protein repulsion and at high pH protein-support material repulsion.
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