Phase Diagrams for Liquid–Liquid Equilibrium of Aqueous Two-Phase System Containing Poly(ethylene glycol) (4000, 6000, or 10 000 g mol^–1 + Sodium Hydrogen Sulfite + Water) at Different Temperatures

Abstract

The liquid–liquid equilibrium for the mixtures of poly­(ethylene glycol) (PEG) with mass-average molar of 4000, 6000, or 10 000 g mol–1 + sodium hydrogen sulfite (NaHSO3) + water systems has been determined experimentally at T = 288.15, 298.15, 308.15, and 318.15 K. The temperature, PEG mass molar, mixture composition, and nature of anion effects on phase equilibrium were studied. The binodal curves at different temperatures were fitted to an empirical equation that correlates the concentrations of polymers and salt. The consistence of experimental data of equilibrium was available through of the Othmer–Tobias and Bancroft equations, and the parameters were reported.

Thermodynamic Investigation of the Aqueous Two-Phase Systems Formed by PEG 400 + Water + Either Sodium Carbonate or Potassium Carbonate at Different Temperatures: Experimental and Correlational Approaches

“…Tables and show the liquid–liquid equilibrium data for the biphasic systems composed of (PEG 400 + potassium carbonate + water) and (PEG 400 + sodium carbonate + water) at temperatures of 283.15, 298.15, and 313.15 K. The data reveal that these systems consist of a top phase enriched in polymer and a bottom phase enriched in salt, with water as the major component of the ATPS. These are typical features of ATPSs, as reported previously. − …”

Liquid–Liquid Equilibrium Data of Ternary Mixture of Polymer, Sodium Thiosulfate, and Water: Effect of Type and Molar Mass of Macromolecule

“…The data for the PEG10k + NaHSO 3, L64 + Na 2 SO 4 and F68 + Na 2 SO 4 systems were collected from the literature and compared with the data obtained in this work (Figure S1). The order of the phase segregation induction capacity is SO 4 2– > S 2 O 3 2– > HSO 3 – .…”

Purification of Pseudomonas sp. proteases through aqueous biphasic systems as an alternative source to obtain bioactive protein hydrolysates

“…proteases to remain in the top phase even when PEG 10,000 g mol −1 was used, yet with lower K values. Since that high molar mass PEG increases the hydrophobic character of the top phase, it is expected that the nature of the proteases also be hydrophobic 33 …”

“…Since that high molar mass PEG increases the hydrophobic character of the top phase, it is expected that the nature of the proteases also be hydrophobic. 33 The activity yield values commonly reported in enzymes extraction using ABS are closed to 100%. 22,34 However, in this study, some activity yields were less than 80% (Figure 1), which would mean that the activity of the enzyme would be negatively affected by some of the components of ABS causing modifications in ionic conformation of the active site or can be attributed to some losses that can occur in the phase separation step.…”