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• W1568402015 abstract "The purpose of this work was to investigate the effect of genetically engineered charge modifications on the separation behavior of proteins in aqueous two-phase extraction. The proteins used in this study included; P-galactosidase, modified by the fusion of positivelyor negatively-charged peptide tails to the carboxy terminus of the enzyme, and lysozyme, which has been altered by site-directed mutagenesis to replace basic amino acids with acidic ones. The effects of these charge modifications were evaluated in phase systems utilizing two different charge-based mechanisms. Protein net charge was found to be effective in systems where partitioning is driven by a salt induced interfacial potential difference. By varying the system pH, the partitioning of p-galactosidase could be increased by several orders of magnitude, and although the change in partitioning of lysozyme was much smaller, its behavior could be quantitatively described by a simple thermodynamic model. The genetic modifications were less effective in altering partition behavior using this mechanism. The charged fusion tails altered partition behavior through offsetting mechanisms, masking the effect of the additional charge on |3galactosidase. The point mutations had a smaller effect on lysozyme partitioning than that observed for an equivalent pH dependent charge change. Direct ionic interaction between polymers and proteins of opposite charge had an even larger effect on partition behavior. Strong interactions between P-galactosidase and diethylaminoethyl-dextran resulted in the formation of protein/polymer aggregates, causing nearly 100% of the enzyme to partition to the DEAE-rich phase. The effect of the fusions was less clear, since the observed partitioning trends could not be completely explained in terms of charge effects. However, the high positive charge density of the polyarginine tails provided for a localized interaction with dextran sulfate, causing fifteen fold shifts in" @default.
• W1568402015 created "2016-06-24" @default.
• W1568402015 creator A5078152606 @default.
• W1568402015 date "2018-08-13" @default.
• W1568402015 modified "2023-09-24" @default.
• W1568402015 title "Genetically engineered charge modifications to enhance protein separation in aqueous two-phase systems" @default.
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• W1568402015 doi "https://doi.org/10.31274/rtd-180813-11845" @default.
• W1568402015 hasPublicationYear "2018" @default.
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