Please use this identifier to cite or link to this item:
|Title:||Electrostatic Interactions, Phase Separation Behaviour and Partitioning of Proteins in Polyelectrolyte Based Aqueous Two-Phase Systems|
|Abstract:||Electrostatic interactions play a major role in the purification of proteins by different methods and they tend to be specific in nature in the presence of salts and environmental hydrogen ion concentration (pH). These can be readily exploited as the basis for protein isolation and purification by aqueous two-phase system (ATPS) using a polyelectrolyte as one of the polymeric components. Polyelectrolytes are water-soluble charged polymers and the phase separation in the polyelectrolyte based ATPS is dependent on the ionic composition of the system and the charge density of polymers. This review outlines the mechanism of the phase separation in non-ionic polymers based ATPS on the basis of water structure in polymeric solution and validity of the hypothesis is further discussed for polyelectrolyte-based systems. Partitioning of proteins in polyeletrolyte based A TPS is dominantly controlled by the electrostatic interactions. Several factors that influence the partitioning of proteins include the properties of the polymers, pH, salt type and concentration and the charge on protein molecules. Low polymer concentration requirement for the phase separation and high specificity of protein purification in polyelectrolyte based ATPS holds a great promise for their large scale applications in isolation and purification of proteins.|
|ISSN:||0975-0967 (Online); 0972-5849 (Print)|
|Appears in Collections:|| IJBT Vol.01(1) [January 2002]|
Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.