Temperature influence on the dynamic binding capacity of a monolithic ion-exchange column.
This work investigates the influence of temperature on the binding capacity of bovine serum albumin (BSA), soybean trypsin inhibitor and L-glutamic acid to a CIM (DEAE) weak anion-exchange disk monolithic column. The binding capacity was determined experimentally under dynamic conditions using frontal analysis. The effect on the dynamic binding capacity of dimers present in the BSA solution has been evaluated and a closed-loop frontal analysis was used to determine the equilibrium binding capacities. The binding capacity for both BSA and soybean trypsin inhibitor increased with increasing temperature. In the case of L-glutamic acid, an increase in the binding capacity was observed with temperature up to 20 degrees C. A further increase in temperature caused a decrease of the dynamic binding capacity.
Mihelic
Igor
I
Faculty of Chemistry and Chemical Technology, University of Ljubljana, Askerceva 5, SI-1000 Ljubljana, Slovenia.
Podgornik
Ales
A
Koloini
Tine
T
D000837:Anion Exchange Resins; D002852:Chromatography, Ion Exchange / Q000295:instrumentation*; D018698:Glutamic Acid / Q000378:metabolism; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013696:Temperature; D014361:Trypsin Inhibitors / Q000378:metabolism
D000837:Anion Exchange Resins; D014361:Trypsin Inhibitors; D012710:Serum Albumin, Bovine; D018698:Glutamic Acid