Open AccessThermodynamic Studies of Bovine Serum Albumin (BSA) Adsorption on Nylon Membrane
Author(s) -
Norhidayah Ideris,
Ahmad Muhaimin Roslan
Publication year - 2019
Publication title -
international journal of engineering and technology
Language(s) - English
Resource type - Journals
ISSN - 2227-524X
DOI - 10.14419/ijet.v7i4.14.27668
Subject(s) - adsorption , nylon 6 , contact angle , bovine serum albumin , membrane , wetting , enthalpy , chemistry , endothermic process , protein adsorption , fourier transform infrared spectroscopy , chromatography , chemical engineering , polymer chemistry , materials science , polymer , organic chemistry , composite material , biochemistry , thermodynamics , physics , engineering
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.