Protein adsorption at liquid/liquid interface with low interfacial tension

Éva Kiss, Réka Borbás

Research output: Contribution to journalArticle

21 Citations (Scopus)


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
Issue number1-4
Publication statusPublished - Sep 1 2003


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

ASJC Scopus subject areas

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

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