JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES, vol.1203, 2022 (SCI-Expanded)
In the study, purification of ovalbumin was performed by modifying polyamide hollow fiber membranes using immobilized metal affinity chromatography technique. For this purpose, firstly polyethyleneimine (PEI) solutions of different concentrations were attached to hollow fiber membranes. Then, Cu(II), Ni(II) and Zn(II) metal ions were chelated separately to polyethyleneimine attached hollow fiber membranes. Characterization studies of modified hollow fiber membranes were performed with scanning electron microscopy (SEM). Also, the surface area was measured with the Brunner Emmet Teller (BET) method and the porosity was measured with mercury porosimeter. pH, ionic strength, initial ovalbumin concentration, temperature and reusability parameters affecting adsorption capacity were investigated. The maximum ovalbumin adsorption capacities of hollow fiber membranes were found to be 317 mg/g for Cu(II), 169 mg/g for Ni(II) and 101 mg/g for Zn(II), respectively. Desorption ratio of metal ions were calculated as 91.6% for Cu(II), 92.9% for Ni(II) and 91.8% for Zn(II), which are quite high and suitable. When examined in terms of adsorption isotherm models, it was concluded that the Langmuir model is suitable. Purification of ovalbumin from egg white was carried out by fast performance liquid chromatography (FPLC), and the purity of ovalbumin was evaluated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) method.