Experimental determination and thermodynamic modeling of phase equilibrium and protein partitioning in aqueous two-phase systems containing biodegradable salts

摘要: Abstract Phase diagrams of sustainable aqueous two-phase systems (ATPSs) formed by polyethyleneglycols (PEGs) different average molar masses (4000, 6000, and 8000) sodium succinate are reported in this work. Partition coefficients ( Kp s) seven model proteins: bovine serum albumin, catalase, beta-lactoglobulin, alpha-amylase, lysozyme, pepsin, urease trypsin were experimentally determined these ATPSs the former PEGs other biodegradable salts: citrate tartrate. An extension Pitzer comprising long short-range term contributions to excess Gibbs free energy was used describe (liquid + liquid) equilibrium. Comparison between experimental calculated tie line data showed mean deviations always lower than 3%, thus indicating a good correlation. The partition modeled using same thermodynamic approach. Predicted correlated quite successfully. Mean found be uncertainty for most assayed proteins.