Ion-exchanging dialysis as an effective method for protein entrapment in curdlan hydrogel.

The purpose of this study was to determine whether dialysis method allows for efficient protein entrapment in curdlan-based hydrogel. Thus, bovine serum albumin, a model of bioactive protein, was incorporated into curdlan matrix using ion-exchanging dialysis method against two concentrations of CaCl ₂ solution - 2% and 10%, respectively. Then, physicochemical, mechanical, and biological properties of the bovine serum albumin-loaded curdlan hydrogels were evaluated. Received results show that neither the polymer nor the entrapment procedure change the bovine serum albumin conformation (as proven by Fourier transform infrared spectroscopy and circular dichroism spectroscopy) and the process guarantees high protein entrapment efficiency (above 95%). The curdlan-based carrier obtained against 2% of CaCl ₂ solution was found to possess higher swelling ability, release greater amounts of bovine serum albumin (up to 4 weeks), and exhibit superior biocompatibility compared to curdlan-based carrier obtained against 10% of CaCl ₂ solution. Thus, dialysis method enables efficient protein entrapment in curdlan hydrogel and obtained protein carrier via dialysis method into 2% of CaCl ₂ solution may be considered as a promising protein delivery system especially for tissue engineering applications. It should be noted that we are the first who presented effective method for protein entrapment in curdlan hydrogel.
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