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

Structuring dairy systems through high pressure processing

“…Further reduction of DH g can be achieved by adding DS into b-lactoglobulin solutions with a ratio of 1:1, without (42.8% reduction) and with (96.1% reduction) HPP application with the same condition. The DH g reduction is larger with: (i) increasing pressure (from 150 to 280 MPa) or temperature (from 40 to 60°C) independently, (ii) combining pressure-heat treatment (280 MPa and 60°C), and (iii) lengthen the holding time from 10 to 30 min (Aouzelleg and Bull, 2004).…”

Physical and Oxidative Stability of Low-Fat Fish Oil-in-Water Emulsions Stabilized with Black Soldier Fly (Hermetia illucens) Larvae Protein Concentrate

“…Unfolding involves the dissociation of intramolecular bonds, which results in an endothermic process. On the other hand, protein aggregation involves the possible reformation of intra- and intermolecular hydrophobic bonds resulting from different treatments, such as sonication [ 31 ]. In this study, there was a decrease in the denaturation temperature for the sample treated with OH, after which sonication occurred.…”

Monitoring protein denaturation using thermal conductivity probe

“…To investigate the physics of conformational change in proteins, various methods have been employed to detect the denaturation state [5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21]. Differential scanning calorimetry (DSC) has been widely used to investigate the thermodynamics of protein denaturation [7][8][9][10]20,21]. DSC can measure the change in heat capacity and enthalpy of protein solutions during denaturation.…”