Transmission analysis in ultrafiltration of ternary protein mixture through a hydrophilic membrane

One of the main reasons for the underutilization of ultrafiltration has been the lack of experimental data on transmission of proteins for complex systems and its corresponding theoretical analysis. Of course, the presence of fouling coupled with concentration polarization have had their share in making ultrafiltration operation a difficult one to understand. In the present study, the systematic ultrafiltration of 3-protein mixture, namely lysozyme, myoglobin and ovalbumin, has been carried out using a hydrophilic 30,000 molecular weight cut off membrane. The experimental data of individual protein transmission in ternary mixture showed a very low transmission (as low as 3% for ovalbumin) to a very high transmission (as high as 90% for lysozyme) of proteins for different operating conditions. This behaviour of each protein in the mixture was analyzed using combined concentration polarization and irreversible thermodynamics model. The parameters of the modeled values gave a very good fit with experimental data and the resulting analysis indicated some interesting findings, which are discussed in this paper. The comparison of parameters obtained for single protein solution and the ternary protein solution showed some unusual results that point to the presence of the protein–protein and protein–membrane interactions.