Restoration of protein foam stability through electrostatic propylene glycol alginate-mediated protein–protein interactions

Dipak Sarker, Peter J. Wilde

Research output: Contribution to journalArticle

Abstract

The action of propylene glycol alginate in the enhancement of foam stability of a destabilised Tween 20/bovine serum albumin mixed system was evaluated. A significant increase in the foam stability was observed in the presence of low concentrations of propylene glycol alginate. A pseudo-plateau level of foam stability was obtained in the presence of approximately 0.8 μg/ml propylene glycol alginate in the solution used to form the foam. Foam stability enhancement due to bulk viscosity changes and surface effects were elucidated. The increase in foam stability was investigated by reference to the properties of thin liquid films and the macroscopic interface of test solutions. Propylene glycol alginate was found to slow the rate of thin film drainage, increase the equilibrium thickness of the films, slow the lateral diffusion of a fluorescent probe molecule located in the adsorbed layer and increase the elasticity of the interface. Data are consistent with propylene glycol alginate-induced crosslinking of protein in the adsorbed layer. This polysaccharide presents a means for controlling protein foam stability.
Original languageEnglish
Pages (from-to)203-213
Number of pages11
JournalColloids and Surfaces B: Biointerfaces
Volume15
Issue number3-4
DOIs
Publication statusPublished - 13 Sep 1999

Keywords

  • Protein
  • Adsorbed layer
  • Electrostatic
  • Crosslinking
  • Viscosity

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  • Activities

    • 1 Invited talk

    Functional Foods and Food Functionalisation.

    Dipak Sarker (Presenter)

    4 Feb 2015

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