The potential for cations to cross-link protein molecules through electrostatic interaction and thereby enhance foaming properties was investigated using aluminium chloride, β-lactoglobulin and Tween 20 as a model system. The addition of the trivalent cations resulted in a noticable improvement in the foamability and foam stability. Optimal behaviour, specific to the protein and emulsifier concentrations used, was observed at 4–5 μM added aluminium ions. The mode of action of the cations was investigated further using isolated foam lamellae (thin liquid films). The appearance of aggregates in the thin liquid films, non-uniformity of the film, and an increase in the dilational viscosity/elastic modulus of the surface associated with the addi...
Bubbles are the vital component of many aerated food products which improves the properties like tex...
In food industry, protein isolates are often used to help in the formation and stabilisation of food...
The foam stability of protein–surfactant mixtures strongly depends on the charge of the protein and ...
Foams and emulsions which are stabilised by proteins e.g. beer foams and meringues remain stable in ...
The stabilization of foam by proteins has been mostly studied in relation to the food industry. The ...
The action of propylene glycol alginate in the enhancement of foam stability of a destabilised Tween...
To understand the properties of protein stabilized foam, quantitative parameters, such as the concen...
The effectiveness of (+)-catechin in the control of foam stability of a deliberately destabilized Tw...
The main destabilisation processes in aqueous foams are liquid drainage, coalescence and disproporti...
The foam stability properties of a defined mixed solution of Tween 20 and bovine serum albumin was e...
Foam film’s properties have a high impact on the properties of the macroscopic foams. This work focu...
This thesis shows the effects that the addition of low molecular weight surfactants (LWMS) to protei...
β-Lactoglobulin fibrils could serve as a surface-active component and form adsorption layers at the...
This study aimed at evaluating the effect of three independent variables: biopolymer concentration (...
This thesis aims to advance the knowledge on the effect that particulates of dairy (whey protein) an...
Bubbles are the vital component of many aerated food products which improves the properties like tex...
In food industry, protein isolates are often used to help in the formation and stabilisation of food...
The foam stability of protein–surfactant mixtures strongly depends on the charge of the protein and ...
Foams and emulsions which are stabilised by proteins e.g. beer foams and meringues remain stable in ...
The stabilization of foam by proteins has been mostly studied in relation to the food industry. The ...
The action of propylene glycol alginate in the enhancement of foam stability of a destabilised Tween...
To understand the properties of protein stabilized foam, quantitative parameters, such as the concen...
The effectiveness of (+)-catechin in the control of foam stability of a deliberately destabilized Tw...
The main destabilisation processes in aqueous foams are liquid drainage, coalescence and disproporti...
The foam stability properties of a defined mixed solution of Tween 20 and bovine serum albumin was e...
Foam film’s properties have a high impact on the properties of the macroscopic foams. This work focu...
This thesis shows the effects that the addition of low molecular weight surfactants (LWMS) to protei...
β-Lactoglobulin fibrils could serve as a surface-active component and form adsorption layers at the...
This study aimed at evaluating the effect of three independent variables: biopolymer concentration (...
This thesis aims to advance the knowledge on the effect that particulates of dairy (whey protein) an...
Bubbles are the vital component of many aerated food products which improves the properties like tex...
In food industry, protein isolates are often used to help in the formation and stabilisation of food...
The foam stability of protein–surfactant mixtures strongly depends on the charge of the protein and ...