Premium
Effect of surface active additives on partitioning of proteins and enzymes in poly(ethylene glycol)/dextran aqueous two‐phase systems
Author(s) -
Bodhankar Sangita S.,
Gaikar Vilas G.
Publication year - 1998
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/(sici)1097-4660(1998110)73:3<251::aid-jctb958>3.0.co;2-1
Subject(s) - chemistry , aqueous solution , amphiphile , ammonium bromide , polyethylene glycol , ethylene glycol , aqueous two phase system , bromide , sodium dodecyl sulfate , dextran , organic chemistry , hydrophobic effect , micelle , polymer chemistry , pulmonary surfactant , polymer , biochemistry , copolymer
The effect of anionic (sodium butylbenzene sulfonate, sodium butylmonoglycol sulfate), cationic (tetrabutyl ammonium bromide), nonionic(Tween 20) and amphoteric (proline) surface active additives on the partitioning of proteins and enzymes, such as BSA, lysozyme, glucose oxidase and β‐lactoglobulin, in a bipolymeric aqueous two‐phase system of polyethylene glycol and dextran has been studied. The partitioning of proteins and enzymes in the aqueous two‐phase system is influenced by surface active additives depending upon their structure and charge. The amphiphiles themselves partition unevenly between the two phases. Their effect on protein partitioning can be explained on the basis of electrostatic and hydrophobic interactions. In the presence of ionic amphiphiles, proteins have an affinity for the other phase if an amphiphile carrying a charge of the same sign partitions to that phase. The hydrophobic effect contributes to protein partitioning if the proteins have significant members of surface hydrophobic amino acid residues. © 1998 Society of Chemical Industry