Protein adsorption using novel carboxymethyl-curdlan microspheres

• Novel carboxymethyl-curdlan (CC) microspheres were synthesized and characterized.
• The CC microspheres were applied to adsorbing Bovine serum albumin (BSA).
• Kinetic analysis and isotherm models of BSA adsorption were investigated.

Carboxymethyl-curdlan as a water soluble curdlan derivative, was synthesized in an aqueous alkaline medium using monochloroacetic acid. Novel carboxymethyl-curdlan (CC) microspheres were prepared by the method of W/O/W emulsion. The chemical and morphological structures of CC microspheres were investigated by scanning electron microscopy (SEM), Fourier-transform infrared spectroscopy (FTIR) and particle size analysis. The CC microspheres were spherical, free flowing, non-aggregated and uniform mono-disperse with diameter of 260 μm. The prepared CC microspheres were applied to adsorbing Bovine serum albumin (BSA) as model protein. Factors influencing the adsorption of BSA such as solution pH, temperature, initial BSA concentration and ionic strength were examined by batch experiments. The maximum adsorption capacity was calculated as 168 mg/g under optimal conditions including BSA initial concentration (4 mg/mL), pH (4.7), adsorption time (9 h) and temperature (35 °C). The adsorption isotherm followed the Langmuir model and the adsorption kinetics fitted the pseudo-second-order model. In addition, the CC microspheres can be also regenerated and re-used.