Interfacial behavior of proteins in three-phase partitioning using salt-containing water/tert-butanol systems

E. Kiss, J. Szamos, B. Tamás, R. Borbás

Research output: Article

40 Citations (Scopus)

Abstract

Three-phase partitioning (TPP) was used to investigate the partitioning of four model proteins (bovine serum albumin, ovalbumin, lysozyme and gelatine) in a system containing water, tert-butanol and an inorganic electrolyte ((NH4)2SO4). Phase diagrams of the ternary (protein-free) system and interfacial tensions between the equilibrium upper and lower liquid phases have been determined. The amount of protein precipitated in the middle layer was delineated as a function of the composition of the partitioning system as well as the initial protein concentration. No dependence of the relative amount of protein accumulated in the midlayer on the total amount of protein was observed. The constant partitioning ratio found in TPP emphasizes the partitioning character of the process. The interfacial adsorption of a single protein (indicated by the decreasing interfacial tension between the immiscible liquid phases) shows a good correlation with the accumulation of the same protein in TPP as a middle layer for the various proteins investigated. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)295-302
Number of pages8
JournalColloids and Surfaces A: Physicochemical and Engineering Aspects
Volume142
Issue number2-3
DOIs
Publication statusPublished - dec. 10 1998

Fingerprint

tert-Butyl Alcohol
Butenes
Salts
salts
proteins
Proteins
Water
water
Surface tension
interfacial tension
liquid phases
lysozyme
Ovalbumin
Liquids
Muramidase
Bovine Serum Albumin
albumins
serums
Electrolytes
Phase diagrams

ASJC Scopus subject areas

  • Colloid and Surface Chemistry
  • Physical and Theoretical Chemistry

Cite this

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title = "Interfacial behavior of proteins in three-phase partitioning using salt-containing water/tert-butanol systems",
abstract = "Three-phase partitioning (TPP) was used to investigate the partitioning of four model proteins (bovine serum albumin, ovalbumin, lysozyme and gelatine) in a system containing water, tert-butanol and an inorganic electrolyte ((NH4)2SO4). Phase diagrams of the ternary (protein-free) system and interfacial tensions between the equilibrium upper and lower liquid phases have been determined. The amount of protein precipitated in the middle layer was delineated as a function of the composition of the partitioning system as well as the initial protein concentration. No dependence of the relative amount of protein accumulated in the midlayer on the total amount of protein was observed. The constant partitioning ratio found in TPP emphasizes the partitioning character of the process. The interfacial adsorption of a single protein (indicated by the decreasing interfacial tension between the immiscible liquid phases) shows a good correlation with the accumulation of the same protein in TPP as a middle layer for the various proteins investigated. Copyright (C) 1998 Elsevier Science B.V.",
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T1 - Interfacial behavior of proteins in three-phase partitioning using salt-containing water/tert-butanol systems

AU - Kiss, E.

AU - Szamos, J.

AU - Tamás, B.

AU - Borbás, R.

PY - 1998/12/10

Y1 - 1998/12/10

N2 - Three-phase partitioning (TPP) was used to investigate the partitioning of four model proteins (bovine serum albumin, ovalbumin, lysozyme and gelatine) in a system containing water, tert-butanol and an inorganic electrolyte ((NH4)2SO4). Phase diagrams of the ternary (protein-free) system and interfacial tensions between the equilibrium upper and lower liquid phases have been determined. The amount of protein precipitated in the middle layer was delineated as a function of the composition of the partitioning system as well as the initial protein concentration. No dependence of the relative amount of protein accumulated in the midlayer on the total amount of protein was observed. The constant partitioning ratio found in TPP emphasizes the partitioning character of the process. The interfacial adsorption of a single protein (indicated by the decreasing interfacial tension between the immiscible liquid phases) shows a good correlation with the accumulation of the same protein in TPP as a middle layer for the various proteins investigated. Copyright (C) 1998 Elsevier Science B.V.

AB - Three-phase partitioning (TPP) was used to investigate the partitioning of four model proteins (bovine serum albumin, ovalbumin, lysozyme and gelatine) in a system containing water, tert-butanol and an inorganic electrolyte ((NH4)2SO4). Phase diagrams of the ternary (protein-free) system and interfacial tensions between the equilibrium upper and lower liquid phases have been determined. The amount of protein precipitated in the middle layer was delineated as a function of the composition of the partitioning system as well as the initial protein concentration. No dependence of the relative amount of protein accumulated in the midlayer on the total amount of protein was observed. The constant partitioning ratio found in TPP emphasizes the partitioning character of the process. The interfacial adsorption of a single protein (indicated by the decreasing interfacial tension between the immiscible liquid phases) shows a good correlation with the accumulation of the same protein in TPP as a middle layer for the various proteins investigated. Copyright (C) 1998 Elsevier Science B.V.

KW - Interfacial adsorption of BSA, OVA and LYS

KW - Interfacial tension

KW - Phase behavior of water/tert-butanol/ammonium sulfate ternary system

KW - Precipitation of proteins

KW - Three-phase partitioning

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