B. Chaufer et al., Selective extraction of lysozyme from a mixture with lactoferrin by ultrafiltration. Role of the physico-chemical environment, LAIT, 80(1), 2000, pp. 197-203
Variation of the physico-chemical environment was used to optimize the sele
ctive extraction of lysozyme(14 300 g.mol(-1)) from a model protein mixture
with lactoferrin (77 000 g.mol(-1), in monomer form) by ultrafiltration (U
F). The system protein-membrane-electrolyte was studied using electrokineti
c measurements, in order to determine the charge of both free proteins and
fouled membrane, depending on the physico-chemical environment (pH, ionic s
trength, chemical nature of added salts). This paper shows that, in order t
o achieve the extraction of a protein from a mixture, the following strateg
y can be used: the target protein recovered in the permeate has to be uncha
rged, whereas the retained protein has to be charged in order to exploit th
e electrostatic repulsion of the membrane partly fouled by the charged prot
ein. This approach was successfully used to achieve the lysozyme/lactoferri
n separation with a high selectivity (lysozyme transmission/lactoferrin tra
nsmission) using an anionic membrane of pore diameter close to 28 nm. The s
electivity of the separation was studied according to the variation of the
ionic strength, in the range 1 to 150 mmol.L-1, with either sodium chloride
or potassium phosphate. Whereas selectivities were close to 20 in sodium c
hloride, they were always greater in potassium phosphate and increased up t
o 120.