Abstract
The partition of proteins (bovine serum albumin, β-lactoglobulin, micellar casein) has been examined in the guar/dextran aqueous two-phase system. The influence of parameters like pH, ionic strength (NaCl), and polymer concentration has been investigated while the protein concentration was increased up to 2% w/w. For globular proteins (bovine serum albumin, β-lactoglobulin) the general trends of partitioning established in the literature with other systems like polyethyleneoxide/dextran were nearly verified. The dextran-rich bottom phase was found to be slightly more concentrated in protein than the guar-enriched top one. However, micellar casein displayed a different behavior, giving a more uneven partition and phase separation phenomena at concentrations above 0.5% w/w. This difference has been attributed to the larger size of the particle. Meanwhile, the modifications of the guar/dextran phase diagram have been investigated. It was shown that the addition of globular protein or micellar casein up to 2% w/w did not affect the thermodynamic features of this system.
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