Study of hydrodynamic and protein-adsorptive properties of gigaporous materials

MIRNA SANCHEZ; GAVARA POONDI; MARCELO FERNANDEZ LAHORE; MARIANO GRASSELLI

Salta

Congreso; XXXIX Annual Meeting of the Argentinean Biophysical Society; 2010

Modern biotechnology heavily depends on the availability of efficient processes, which should be able to generate competitive products in terms of quality and cost. The strategy elected for this project is via direct product process, improve separation by development of novel adsorbents. In previous work we obtained micro-hydrogels supported onto foams. Preliminary studies showed that adsorption properties of these hydrogels allow adsorbing proteins in a reversible fashion, as an ion exchanger. The purpose of this work is to explore the hydrodynamic and adsorptive properties of this new gigaporous material capable of interact with proteins for bioprocess applications. Gigaporous structure is based onto polymeric foams with pore sizes in the range of 100-2000 um and apparent density of 0.15 g/ml. Polymeric foams are grafted with glycidylmethacrylate (GMA) by radiation-induced polymerization and subsequently derivatized with sulfonic groups. Lysozyme is used as a model protein. Adsorptive foams were able to reversible adsorb between 17 to 60 (+/-6) mg lysozyme/g for different pore sizes, in batch adsorption experiments. The hydrodynamic behavior was similar, measured at two different flow-rates, independently of pore size. Dynamic protein adsorption capacities were from 1.3 to 3.4 mg lysozyme / ml for foams with pore sizes from 2000 to 100 um respectively. Breakthrough points were determined at 10%. Functional hydrogels supported onto polymeric foams are promising chromatographic matrices for protein purification from non-clarified samples.