Stabilisation of protein adsorbed layers in foams and emulsions by cross-linking.

Description

Dipak K. Sarker School of Chemical Sciences, The University of East Anglia, Norwich NR4 7TJ . Abstract Foams and emulsions which are stabilised by proteins e.g. beer foams and meringues remain stable in the absence of small molecular weight surface active components (lipids, emulsifiers and surfactants). In the presence of surfactants the stabilising visco-elastic layer of protein surrounding each particle is compromised due to competitive adsorption of the surfactant. One strategy to overcome these partially stable dispersions is to unite the 'mobilised' regions of protein adsorbed at the air-water or oil-water interface and produce a more continuous layer of adsorbed protein. A model foam composed of precise amounts of surface active protein, ß-lactoglobulin (ß-lg) and an emulsifier, Tween 20, to mimic the destabilistion of food foams and emulsions was used as a test sample to assess the effectiveness of various potential cross-linking agents. Addition of micromolar concentrations of the polyphenol, (+)catechin and a trivalent cation, AI3+ were found to increase the foam formation and foam stability (reduced liquid drainage from the foam). Behaviour of the model foams has been related to the (+)catechin and trivalent cation mediated cross-linking of protein adsorbed at the interface in thin liquid films (foam lamellae). Event: The Third UK Colloid & Surface Science Student Meeting. The Lawns, University of Hull, 16-18 July 1995 Number of pages: 1 Publication status: Published - 16 Jul 1995

Period	16 Jul 1995 - 18 Jul 1995
Event title	The Third UK Colloid & Surface Science Student Meeting
Event type	Conference
Location	Hull, United Kingdom
Degree of Recognition	National