Biotechnol. Bioeng., 56, 248-257 (1997)
Sebastião, M. J., Martel, P., Baptista, A., Petersen, S. B., Cabral, J. M. S., Aires-Barros, M. R.
A model for the prediction of protein partition coefficients in aqueous two-phase systems has been developed. This model accounts for both charge-independent and electrostatic effects. The determination of nonelectrostatic effects was based on the model of Eiteman and Gainer for uncharged solutes while the electrostatic contribution was computed using TITRA, a program that uses a continuum electrostatic model to treat charge interactions in proteins and considers the effect of pH and ionic strength. The partition coefficients of Fusarium solani pisi recombinant cutinase have been satisfactorily predicted in polyethylene glycol (PEG) 1000 and phosphate aqueous two-phase systems at a pH range of 6.0-9.0. The model failed to predict the enzyme partitioning behavior at pH 4.5.
Keywords: cutinase; aqueous two-phase systems; partition; modeling; electrostatics
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