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

 
 
 
  • Abstract
  • Keywords
  • References
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  • 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.  

     


  • Keywords


    Nylon membrane, BSA, morphology, thermodynamic.

  • References


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Article ID: 27668
 
DOI: 10.14419/ijet.v7i4.14.27668




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