These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Dilatational rheology and foaming properties of sucrose monoesters in the presence of beta-lactoglobulin. Author: Garofalakis G, Murray BS. Journal: Colloids Surf B Biointerfaces; 2001 Jul; 21(1-3):3-17. PubMed ID: 11377930. Abstract: The foaming properties and the dilatational rheology of systems containing purified sucrose caprylate (SM800), caprate (SM1000), laurate (SM1200) and palmitate (SM1600) have been studied. Addition of beta-lactoglobulin (beta-lg) at a low concentration (0.050 wt.%) can aid the foam formation in the cases, where the surfactant concentration is insufficient to support foam formation. However, foams where both species co-existed exhibited poor stability. beta-lg was found to affect the dilatational properties of surfactant films even at low concentrations. It is thought that this could be related to the effect of the protein on the adsorption-desorption relaxation mechanism, or to the possible formation of a protein-surfactant complex in the bulk. The age of the protein film was also found to affect the kinetics of protein displacement by SM1000, as monitored by the change in the dilatational properties (Langmuir trough technique) and the relative reflectivity of the interface (Brewster angle microscopy) with time. An insoluble monolayer of sucrose stearate (Suc18) and beta-lg was also studied and it was found that the presence of small amounts of Suc18 in the protein film lead to a reduction of the interfacial elasticity. This is believed to be due to the disruption of the protein network. A possible mechanism could involve the obstruction of the hydrogen-bond intermolecular protein association by the strongly hydrated sucrose headgroup or the obstruction of the protein-protein hydrophobic interactions by the formation of an interfacial protein-surfactant complex.[Abstract] [Full Text] [Related] [New Search]