Changes in protein-protein and protein-polysaccharide interactions induced by high pressure

Emulsifying properties of ovalbumin in mixtures with sulphated polysaccharides: effects of pH, ionic strength, heat and high-pressure treatment

“…It is interesting to note that previous studies carried out on b-Lg emulsions have also shown¯occulation, 43 although the effect of high pressure on d 43 and creaming behaviour was somewhat less when the treatment was applied after emulsion formation. 14 On the basis of the experimental results presented in this paper and data from previous studies 10,20,22 we assume that high-pressure processing leads to the dissociation of the electrostatic protein±polysacchar-ide complex(es). During the`holding period' at the set treatment pressure, OVA becomes denatured and so exposes more charged groups.…”

Protein stability function relations: native ?-lactoglobulin sulphhydryl-disulphide exchange with PDS

“…Highpressure treatment induces a b-lactoglobulin conformational change and aggregation partly by SH± disulphide exchange. 20,21 SH group exposure increases the antioxidant effect of b-lactoglobulin against the oxidation of linoleic acid. 22,23 Ureainduced gelation of b-lactoglobulin also occurs via SH±disulphide exchange.…”

Differential scanning calorimetry study of pressure/temperature processed β-lactoglobulin: The effect of dextran sulphate

“…This globular protein is quite sensitive to pressure when processed at relatively high concentration as aggregation occurs. It is believed that the protein is more resistant to pressure at low concentration because of its higher flexibility and due to some refolding occurring post-processing when the protein is not implicated in aggregates (Galazka, Sumner, & Ledward, 1996). It has been shown, using circular dichroism, that a combination of pressure and temperature (maximum of 294 MPa and 62°C) could alter, in an important way, the secondary and tertiary structure of b-lactoglobulin (Aouzelleg, Bull, Price, & Kelly, 2004) even if the pressures used were lower than those required to modify irreversibly the protein structure at low concentration.…”