Within a restricted range of pH and protein concentration crystalline chymotrypsinogen undergoes thermal denaturation which is wholly reversed upon cooling. At a given temperature an equilibrium exists between native and reversibly denatured protein. Within the pH range 2 to 3 the amount of denatured protein is a function of the third power of the hydrogen ion activity. The presence of small am...

When understanding the mechanisms of HPinduced changes, HP can be used in targeted and unique biomolecule architecture. Thereby, HP offers opportunities to modify structure and interactions within or between biopolymers. This review introduces the principle of HP and its characteristic followed by a description of the pressure effects on meat proteins. Overall, meat protein systems and meat pro...

Proteins denature not only at high, but also at low temperature as well as high pressure. These denatured states are not easily accessible for experiment, because usually heat denaturation causes aggregation, whereas cold or pressure denaturation occurs at temperatures well below the freezing point of water or pressures above 5 kbar, respectively. Here we have obtained atomic details of the pre...

BACKGROUND Chemistry and particularly enzymology at surfaces is a topic of rapidly growing interest, both in terms of its role in biological systems and its application in biocatalysis. Existing protein immobilization approaches, including noncovalent or covalent attachments to solid supports, have difficulties in controlling protein orientation, reducing nonspecific absorption and preventing p...

A fast uptake of the preservative benzoic acid was observed in Saccharomyces cerevisiae, reaching saturation in about two min and then remaining constant at this level. The strong dependence of benzoic acid uptake on pH was due to the relative distribution of molecular and ionic forms in solution and not to the pH itself. The molecular form was the only one taken up by the cells. The specificit...

Urea-induced protein denaturation is widely used to study protein folding and stability; however, the molecular mechanism and driving forces of this process are not yet fully understood. In particular, it is unclear whether either hydrophobic or polar interactions between urea molecules and residues at the protein surface drive denaturation. To address this question, here, many molecular dynami...

Heat treatment of milk signifies a certain degree protein denaturation, which modifies the functional properties dairy products. Traditional methods for detecting and quantifying denaturation whey proteins are slow, complex require sample preparation qualified staff. The world’s current trend is to develop rapid, real-time analytical that do not destroy can be applied on/in-line during processi...

The thermomechanical structuring by extrusion and shear cell processing of plant proteins into meat analogues is discussed in the context phase state behavior proteins, with a focus on soy gluten. water content dependence denaturation temperature major protein fractions from critically analyzed available literature sources, its impact for low-moisture (LMMAs; also known as texturized vegetable ...

We study cold denaturation of proteins at high pressures. Using multicanonical Monte Carlo simulations of a model protein in a water bath, we investigate the effect of water density fluctuations on protein stability. We find that above the pressure where water freezes to the dense ice phase (≈ 2 kbar), the mechanism for cold denaturation with decreasing temperature is the loss of local low-dens...

The viscosity of a protein solution is increased by the denaturation of the protein. This is true both when there is the formation of protein aggregates which occlude water and when there is no aggregation. Under certain conditions, as a result of the aggregation following denaturation, a solution containing only one per cent of protein may be converted into a clear gel. The conditions for obta...