Thermodynamic Studies of Bovine Serum Albumin (BSA) Adsorption on Nylon Membrane

Abstract

The aim of this study was to investigate the nylon membrane’s characteristics and thermodynamic aspects for adsorption of Bovine Serum Albumin (BSA) as a model protein on nylon membrane. The morphology characteristics analyzed by FESEM and wetting and weighting technique showed the nylon membrane possessed micro-pore size (0.159±0.039 µm) with high porosity (74.2820±0.0411 %) respectively. Thermodynamic studies indicated that the adsorption reaction was endothermic with positive value of standard enthalpy (∆rHθ = 107.7 kJ/mole) and dominated by chemical adsorption. The results were supported with the analysis of functional groups of the nylon membrane with FTIR-ATR. Bands corresponding to the NH bonds stretching were generally detected in the 3500-3100 cm-1 range. The existence of C=O stretching vibration of carbonyl group was further confirmed with the observation of peak at 1632. 42 cm-1. The water contact angle analysis showed the hydrophilicity nature of nylon membrane with contact angle of 55.6°. These findings are expected to be used in the modification of nylon membrane for an optimum adsorption of protein.