Hydrocolloids at interfaces and the influence on the properties of dispersed systems

A positive temperature coefficient is the term which has been used to indicate that an increase in solubility occurs as the temperature is raised, whereas a negative coefficient indicates a decrease in solubility with rise in temperature.

Effect of Temperature

https://www.zora.uzh.ch/id/eprint/44154/1/Rabe1.pdf

Understanding protein adsorption phenomena at solid surfaces

The Martini model, a coarse-grained force field for biomolecular simulations, has found a broad range of applications since its release a decade ago. Based on a building block principle, the model combines speed and versatility while maintaining chemical specificity. Here we review the current state of the model. We describe recent highlights as well as shortcomings, and our ideas on the further development of the model.

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Perspective on the Martini model.

Food proteins and polysaccharides are the two key structural entities in food materials. Generally, interactions between proteins and polysaccharides in aqueous media can lead to one- or two-phase systems, the latter being generally observed. In some cases of protein-polysaccharide net attraction, mainly mediated through electrostatic interactions, complex coac-ervation or associative phase separation occurs, giving rise to the formation of protein-polysac-charide complexes. Physicochemical factors such as pH, ionic strength, ratio of protein to polysaccharide, polysaccharide and protein charge, and molecular weight affect the formation and stability of such complexes. Additionally, the temperature and mechanical factors (pressure, shearing rate, and time) have an influence on phase separation and time stability of the system. The protein-polysacchaide complexes exhibit better functional properties than that of the proteins and polysaccharides alone. This improvement could be attributed to the simultaneou...

Structure and Technofunctional Properties of Protein-Polysaccharide Complexes: A Review

Egg-white proteins are extensively utilised as food ingredients due to their unique functional properties. Several attempts have been made in order to improve the functional properties of egg-white proteins and to identify the optimal formulations for unique food products. Experimental data proves that controlled denaturation of egg-white proteins can have a beneficial impact on various functional applications in the food industry such as emulsifying ability, heat stability, and gelation. This review describes the effect of heat-induced denaturation on protein structure and functionality. Studies on the impact of Maillard reaction, which aim to elucidate the structure-function relationship of egg-white proteins, are presented. A novel approach which could be the basis for the development of new methods aiming to improve the functional properties of egg-white proteins is also discussed.

Stephen R. Euston

Papers

Modification of functional properties of egg‐white proteins

Aggregation kinetics of heated whey protein-stabilized emulsions.

Effects of sucrose and sodium chloride on foaming properties of egg white proteins

Rheology and texture of hen's egg protein heat-set gels as affected by pH and the addition of sugar and/or salt

Effects of heat treatment and glucono-δ-lactone-induced acidification on characteristics of soy protein isolate