Rheological properties, protein-stabilized foam

The term food colloids can be applied to all edible multi-phase systems such as foams, gels, dispersions and emulsions. Therefore, most manufactured foodstuffs can be classified as food colloids, and some natural ones also (notably milk). One of the key features of such systems is that they require the addition of a combination of surface-active molecules and thickeners for control of their texture and shelf-life. To achieve the requirements of consumers and food technologists, various combinations of proteins and polysaccharides are routinely used. The structures formed by these biopolymers in the bulk aqueous phase and at the surface of droplets and bubbles determine the long-term stability and rheological properties of food colloids. These structures are determined by the nature of the various kinds of biopolymer-biopolymer interactions, as well as by the interactions of the biopolymers with other food ingredients such as low-molecular-weight surfactants (emulsifiers). 

The behavior of proteins at interfaces influences the formation of foams and emulsions (32). Stabilization of foams and emulsions depends, to a great extent, on the formation, rheological, and mechanical properties of the interfacial film ( ). Factors which ensure optimum film properties in simple systems may retard film formation or cause destabilization in foams or emulsions (3 ) for example, many rheological properties of films are maximum in the isoelectric pH range of specific proteins, yet most proteins have minimum solubility in this pH range (34). Thus, environmental and processing factors which... 

In the case of the major cytoplasmic protein of leaves, ribulose 1,5-biphosphate carboxylase (RUBISCO), the surface rheological properties and foam stability were maximum at pH 5.5, close to the isoelectric point (pH 4.8) and all parameters measured were greater than any other protein studied (2 ). This may be related to the large molecular size of RUBISCO, i.e. 560 000 daltons, and its disulfide stabilized globular structure. 

Adsorption of protein at mobil surfaces as compared with adsorption of proteins from solutions on sohd adsorbents reveals additional phenomena adsorption layers aquire specific rheological properties indicating formation of a new middle phase adsorption can be accompanied by an extension and or stacking of rigid monolayer with nearly ultimate packing by protein and in the case of two liquid immiscible phases by a protein distribution between these phases, evidently in a form of associates of protein with other components of the system. These phenomena remain poorely investigated. Adsorption of a protein on mobil interfaces results in the formation adsorption layer with strong abihty to stabihze foams or emulsions, respectively, and their elements- free and emulsion films, which can be as ultimately thin, black (thickness of such films is of about lOnm). Thermodynamics of black films determines the stability of... 

The interfacial rheology of protein adsorption layers has been intensively studied in relation to the properties of foams and emulsions stabilized by proteins and their mixtures with lipids or surfactants. Detailed information on the investigated systems, experimental techniques, and theoretical models can be found in Refs. [762-769]. The shear rheology of the adsorption layers of many proteins follows the viscoelastic thixotropic model [770-772], in which the surface shear elasticity and viscosity depend on the surface shear rate. The surface rheology of saponin adsorption layers has been investigated in Ref. [773]. 

As already mentioned, the surfactants are used to stabilize the liquid films in foams, in emulsions, on solid surfaces, and so forth. We will first consider the equilibrium and kinetic properties of surfactant adsorption monolayers. Various two-dimensional equations of state are discussed. The kinetics of surfactant adsorption is described in the cases of dijfusion and barrier control. Special attention is paid to the process of adsorption from ionic surfactant solutions. Theoretical models of the adsorption from micellar surfactant solutions are also presented. The rheological properties of the surfactant adsorption mono-layers, such as dilatational and shear surface viscosity and suiface elasticity, are introduced. The specificity of the proteins as high-molecular-weight surfactants is also discussed. 

The most important functional properties of proteins are solubility, water absorption and binding, rheology modification, emulsifying activity and emulsion stabilization, gel formation, foam formation and stabilization, and fat absorption [1-6]. They reflect the inherent properties of proteins as well as the manner of interaction with other components of the system under investigation. 

Because protein-ba sed foams depend upon the intrinsic molecular properties (extent and nature of protein-protein interactions) of the protein, foaming properties (formation and stabilization) can vary immensely between different proteins. The intrinsic properties of the protein together with extrinsic factors (temperature, pH, salts, and viscosity of the continuous phase) determine the physical stability of the film. Films with enhanced mechanical strength (greater protein-protein interactions), and better rheological and viscoelastic properties (flexible residual tertiary structure) are more stable (12,15), and this is reflected in more stable foams/emulsions (14,33). Such films have better viscoelastic properties (dilatational modulus) ( ) and can adapt to physical perturbations without rupture. This is illustrated by -lactoglobulin which forms strong viscous films while casein films show limited viscosity due to diminished protein-protein (electrostatic) interactions and lack of bulky structure (steric effects) which apparently improves interactions at the interface (7,13 19). 

Adsorbed protein molecules interact at the interfaces to form viscoelastic films. The viscoelastic properties of protein films adsorbed at fluid interfaces in food emulsions and foams are important in relation to the stability of such systems with respect to film rupture and coalescence. Interfacial rheology techniques are very sensitive methods to measure the viscoelastic properties of proteins, thereby evaluating the protein-protein or protein-surfactant interactions at the interfaces. There was an excellent review about the principal and methods of interfacial rheology [17]. 

Firstly, the stability of the foam formed by P-casein and whole casein appears very different, the former being more stable. In order to further investigate this issne, we evalnate several surface properties of these two proteins. The surface tension and surface rheology do not seem to be accurate enough to account for this large difference in foam stability, since they show very similar values. However, the thickness of the foam films stabilized by the two proteins respectively seems to determine the ultimate behavior of the foam. Hence, the thicker foam film measured for P-casein probably prevents coalesce of air bubbles resulting in more stable foam formed by this protein as compared to whole casein. 

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