The senú-continuous and continuous extraction of a model enzyme, xylanase, in spray, sieve plates and packed columns were investigated using aqueous two-phase systems composed by polyethylene glycol (PEG) 4000 and potassium phosphate. For the spray colunm, the dispersed phase hold-up and overall mass transfer coefficients (Koa) were evaluated for different superficial ve!ocities o f the dispersed phase (light phase ). Resu!ts indicated that an increase in superficial velocity in the range of O -0.18 mm/s of the dispersed phase had a positive effect on Kn a and on hold-up in all co!umn heights studied, 75, 161 and 246mm. For the sieve plate colunm, the effect ofthe superficial velocity ofthe dispersed phase and number o f plates were also studied. Results showed that the Kn a and hold-up increased with an increase in both parameters. The selectivity of separation of xylanase and BSA (mode! contaminant) was very high, since 60% of the enzyme was extracted in the light phase, whereas no significant amount of BSA was extracted. The possibility o f using the sieve plate and packed column in continuous operations for enzyme extraction was studied. The influence of several kinds of packings, Raschig rings, glass spheres and polyestirene rings was studied as well as the superficial ve!ocity ratio of the salt and PEG phases. The best selectivity was obtained with the polyestirene ring whith 94% of xylanase recovery in the polimeric phase and just 3% of contaminant was recovery to this phase. In a second part of this work a system cornposed by a thermoseparating hydrophobically modified polymers (HM-EOPO) has been used in one-polymer extraction systems, where the top phase is enriched by water and the bottom phase is enriched by the polymer (about 6-8%, w/w). The best separation ofDNA from plasnúd was obtained using a low ionic system at pH 8 when the polymer is positively charged. By using salts that do not produce electrochenúcal driving force in the system contained HM-EOPO copolymer it is possible to distinguish other driving forces acting on the partitioning of biomolecules.One salt used in this study, K2S04, has this property. The partition coefficient of the proteins studied in this work, showed an independence of the pH of the system, but at extreme pH variation in K with the protein charge would indicate structural changes in the proteic molecule.