Protein adsorption at liquid/liquid interface with low interfacial tension

Éva Kiss, Réka Borbás

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Adsorption of proteins at the interface of two-liquid systems composed of aqueous ammonium sulfate solution and tert-butanol by phase separation was investigated by drop shape tensiometry. The change of interfacial tension with time and protein concentration as well as upon compression of the adsorbed layer were compared for bovine serum albumin, ovalbumin, β-lactoglobulin, lysozyme, trypsin and horse radish peroxidase. A correlation between the dilatational moduli of various protein films and the partitioning of proteins in the two-liquid system was found, which provides evidence to the role of emulsion stability in protein separation by three-phase partitioning.

Original languageEnglish
Pages (from-to)169-176
Number of pages8
JournalColloids and Surfaces B: Biointerfaces
Volume31
Issue number1-4
DOIs
Publication statusPublished - Sep 1 2003

Fingerprint

liquid-liquid interfaces
Surface Tension
Adsorption
Surface tension
interfacial tension
proteins
Proteins
adsorption
Liquids
tert-Butyl Alcohol
Raphanus
Lactoglobulins
Protein Stability
Ovalbumin
Ammonium Sulfate
Muramidase
trypsin
Bovine Serum Albumin
Emulsions
horses

Keywords

  • Dilatational rheology
  • Emulsion stability
  • Protein adsorption
  • Three-phase partitioning

ASJC Scopus subject areas

  • Biotechnology
  • Colloid and Surface Chemistry
  • Physical and Theoretical Chemistry
  • Surfaces and Interfaces

Cite this

Protein adsorption at liquid/liquid interface with low interfacial tension. / Kiss, Éva; Borbás, Réka.

In: Colloids and Surfaces B: Biointerfaces, Vol. 31, No. 1-4, 01.09.2003, p. 169-176.

Research output: Contribution to journalArticle

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