Effects of medium and chemical modification on thermal characteristics of Β-lactoglobulin

Effect of pectin adsorption on the hydrophobic binding sites of β-lactoglobulin in solution and in emulsion systems

“…The experiments were carried out at pH 4.0 to confirm the conformational change observed with S 0 measurements. The T m of bLG at pH 4.0 in the absence of pectin was 86.1 C. This relatively high T m agrees with a previous study where the increase in T m upon folding is correlated with less repulsive forces near the iso-electric point of bLG (Ma & Harwalkar, 1996). A decrease can be observed in the exothermic peak with a lower T m of 82.7 C for the complex of bLG and pectin.…”

Effect of high pressure treatment on thermal and rheological properties of lentil flour slurry

“…The residual denaturation enthalpy provides a net value from a combination of endothermic reactions like the disruption of hydrogen bonds, and exothermic processes, including the break-up of hydrophobic interactions and protein aggregation (Ma & Harwalkar, 1991;Privalov & Khechinashvili, 1974). Thus, DSC thermograms of the pressure treated lentil slurry exhibit the subsequent thermal denaturation of the proteins remaining in a native-like conformation.…”

Effects of High Hydrostatic Pressure Treatment on Physicochemical Characteristics of Sea Cucumber

“…Results indicated that the sea cucumber protein was significantly affected by the HHP treatment, complete denaturation occurred when the treatment pressure level increased to 400 MPa. The decrease of enthalpy with pressure level has been reported in the literature for various proteins [25][26][27].…”

“…These changes could be attributed by cleavage of hydrogen bonds between surface of the protein and the surroundings, protecting water molecules. The residual denaturation enthalpy provides a net value from a combination of endothermic reactions like the disruption of hydrogen bonds, and exothermic processes, including the break-up of hydrophobic interactions and protein aggregation [27,29]. As a result, DSC-thermograms of the pressure-treated sea cucumber exhibited subsequent thermal denaturation of the proteins remaining in a nativelike conformation.…”