Formation and structural heat-stability of β-lactoglobulin/surfactant complexes

Shlomo Magdassi, Yelena Vinetsky, Perla Relkin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

67 Scopus citations


The binding of two model surfactants, sodium dodecyl sulfate and dodecyltrimethyhlmmonium bromide to β-lactoglobulin was studied at room temperature and the thermal stability of the resulting complexes was evaluated by differential scanning calorimetry (DSC) measurements. Binding isotherms indicated both ionic and hydrophobic interactions depending on both the charge of the protein and surfactant at different pHs and on the binding molar ratios of surfactant to the globular protein. Zeta potential measurements indicated charge neutralisation of the protein, under suitable conditions, which also lead to aggregation and precipitation of the proteins. Surface tension measurements indicated similarity between the two types of oppositely charged protein-surfactant complexes and a difference between them when protein and surfactants are similarly charged. DSC measurements revealed different behavior in protein conformation in the presence of the two surfactants. The results obtained at room temperature and upon heating are discussed in terms of the nature of the surfactant/protein interactions involved in the complex formation.

Original languageAmerican English
Pages (from-to)353-362
Number of pages10
JournalColloids and Surfaces B: Biointerfaces
Issue number6
StatePublished - 20 Jun 1996

Bibliographical note

Funding Information:
Financial support from the Ministry of Science and Arts (Israel), Le Minist6re des Affaires Etrang6res (France) and La Conf6rence des Grandes Ecoles (France/Israel) is highly appreciated.


  • Differential scanning calorimetry
  • Dodecyltrimetylammonium bromide
  • Sodium dodecyl sulfate
  • Structural stability
  • Surfactant globular protein complexes
  • β- lactoglobulin


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