Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system
A relationship is proposed for the interfacial partitioning of protein in poly(ethylene glycol) (PEG)-phosphate aqueous two-phase system (ATPS). The relationship relates the natural logarithm of interfacial partition coefficient, ln G to the PEG concentration difference between the top and bottom ph...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English English |
| Published: |
Elsevier
2013
|
| Online Access: | http://psasir.upm.edu.my/id/eprint/30119/ http://psasir.upm.edu.my/id/eprint/30119/1/Interfacial%20partitioning%20behaviour%20of%20bovine%20serum%20albumin%20in%20polymer.pdf |
| _version_ | 1848846587924578304 |
|---|---|
| author | Chow, Yin Hui Yap, Yee Jiun Anuar, Mohd. Shamsul Tejo, Bimo Ario Ariff, Arbakariya Show, Pau Loke Ng, Eng Poh Tau, Chuan Ling |
| author_facet | Chow, Yin Hui Yap, Yee Jiun Anuar, Mohd. Shamsul Tejo, Bimo Ario Ariff, Arbakariya Show, Pau Loke Ng, Eng Poh Tau, Chuan Ling |
| author_sort | Chow, Yin Hui |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | A relationship is proposed for the interfacial partitioning of protein in poly(ethylene glycol) (PEG)-phosphate aqueous two-phase system (ATPS). The relationship relates the natural logarithm of interfacial partition coefficient, ln G to the PEG concentration difference between the top and bottom phases, Δ[PEG], with the equation ln G = AΔ[PEG] + B. Results showed that this relationship provides good fits to the partition of bovine serum albumin (BSA) in ATPS which is comprised of phosphate and PEG of four different molecular weight 1450 g/mol, 2000 g/mol, 3350 g/mol and 4000 g/mol, with the tie-line length (TLL) in the range of 44–60% (w/w) at pH 7.0. The decrease of A values with the increase of PEG molecular weight indicates that the correlation between ln G and Δ[PEG] decreases with the increase in PEG molecular weight and the presence of protein–polymer hydrophobic interaction. When temperature was increased, a non-linear relationship of ln G inversely proportional to temperature was observed. The amount of proteins adsorbed at the interface increased proportionally with the amount of BSA loaded whereas the partition coefficient, K remained relatively constant. The relationship proposed could be applied to elucidate interfacial partitioning behaviour of other biomolecules in polymer-salt ATPS. |
| first_indexed | 2025-11-15T09:05:05Z |
| format | Article |
| id | upm-30119 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English English |
| last_indexed | 2025-11-15T09:05:05Z |
| publishDate | 2013 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-301192015-09-08T04:20:05Z http://psasir.upm.edu.my/id/eprint/30119/ Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system Chow, Yin Hui Yap, Yee Jiun Anuar, Mohd. Shamsul Tejo, Bimo Ario Ariff, Arbakariya Show, Pau Loke Ng, Eng Poh Tau, Chuan Ling A relationship is proposed for the interfacial partitioning of protein in poly(ethylene glycol) (PEG)-phosphate aqueous two-phase system (ATPS). The relationship relates the natural logarithm of interfacial partition coefficient, ln G to the PEG concentration difference between the top and bottom phases, Δ[PEG], with the equation ln G = AΔ[PEG] + B. Results showed that this relationship provides good fits to the partition of bovine serum albumin (BSA) in ATPS which is comprised of phosphate and PEG of four different molecular weight 1450 g/mol, 2000 g/mol, 3350 g/mol and 4000 g/mol, with the tie-line length (TLL) in the range of 44–60% (w/w) at pH 7.0. The decrease of A values with the increase of PEG molecular weight indicates that the correlation between ln G and Δ[PEG] decreases with the increase in PEG molecular weight and the presence of protein–polymer hydrophobic interaction. When temperature was increased, a non-linear relationship of ln G inversely proportional to temperature was observed. The amount of proteins adsorbed at the interface increased proportionally with the amount of BSA loaded whereas the partition coefficient, K remained relatively constant. The relationship proposed could be applied to elucidate interfacial partitioning behaviour of other biomolecules in polymer-salt ATPS. Elsevier 2013-09-01 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/30119/1/Interfacial%20partitioning%20behaviour%20of%20bovine%20serum%20albumin%20in%20polymer.pdf Chow, Yin Hui and Yap, Yee Jiun and Anuar, Mohd. Shamsul and Tejo, Bimo Ario and Ariff, Arbakariya and Show, Pau Loke and Ng, Eng Poh and Tau, Chuan Ling (2013) Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system. Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, 934. pp. 71-78. ISSN 1570-0232 10.1016/j.jchromb.2013.06.034 English |
| spellingShingle | Chow, Yin Hui Yap, Yee Jiun Anuar, Mohd. Shamsul Tejo, Bimo Ario Ariff, Arbakariya Show, Pau Loke Ng, Eng Poh Tau, Chuan Ling Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system |
| title | Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system |
| title_full | Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system |
| title_fullStr | Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system |
| title_full_unstemmed | Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system |
| title_short | Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system |
| title_sort | interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system |
| url | http://psasir.upm.edu.my/id/eprint/30119/ http://psasir.upm.edu.my/id/eprint/30119/ http://psasir.upm.edu.my/id/eprint/30119/1/Interfacial%20partitioning%20behaviour%20of%20bovine%20serum%20albumin%20in%20polymer.pdf |