2003
DOI: 10.1016/j.memsci.2003.07.020
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Study of ultrafiltration of a single and binary protein solution in a thin spiral channel module

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Cited by 37 publications
(20 citation statements)
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“…Previously, the separation of lysozyme from myoglobin has been investigated by a few groups. Müller et al [40] reported the maximum selectivity of lysozyme against myoglobin through cellulose acetate membrane around 3 at pH 7, low transmembrane pressure and zero ionic strength of the protein solution. For similar conditions, we have determined the selectivity value of 36 through the 1-bilayer PEI-ALG coated PAN-C membrane.…”
Section: Separation Of Proteinsmentioning
confidence: 99%
“…Previously, the separation of lysozyme from myoglobin has been investigated by a few groups. Müller et al [40] reported the maximum selectivity of lysozyme against myoglobin through cellulose acetate membrane around 3 at pH 7, low transmembrane pressure and zero ionic strength of the protein solution. For similar conditions, we have determined the selectivity value of 36 through the 1-bilayer PEI-ALG coated PAN-C membrane.…”
Section: Separation Of Proteinsmentioning
confidence: 99%
“…In addition to the classical filtration parameters, the most important parameters governing such a process are the pH value and the ionic strength. Furthermore, the global transport parameters such as permeability, rejection, selectivity, effective diffusion coefficient and solubility of the protein may play an important role [3]. One of the major difficulties with crossflow filtration research is the black box' nature of the equipment.…”
Section: Introductionmentioning
confidence: 99%
“…Müller et al [3] demonstrated the factors influencing a protein filtration process using single and mixed solutions of lysozyme and myoglobin through a hydrophilic 30 kDa molecular weight cut-off (MWCO) cellulose acetate membrane. The proteins were of similar molar mass and size.…”
Section: Introductionmentioning
confidence: 99%
“…Ghosh and Cui [8] observed greater self-rejection of LYZ at a pH far away from the pI. Müller et al [27] also reported that LYZ forms a positively charged layer at the membrane surface below its pI. The permeate flux was found to be lower for the LYZ experiments compared with the BSA experiments.…”
Section: Protein Filtration Of Lysozymementioning
confidence: 94%
“…Only at pH 4.9 was a slight increase in rejection be observed. At the higher ionic strength, charge-shielding of the proteins results in reduction in the protein effective size [27]. In addition, less self-rejection of LYZ is anticipated in a solution environment where protein charge is shielded.…”
Section: Protein Filtration Of Lysozymementioning
confidence: 99%