Spectroscopic and Calorimetric Study of 2,2′-Dibipyridin Cu(II) Chloride Binding to Bovine β-Lactoglobulin

2013 ◽  
Vol 42 (4) ◽  
pp. 705-715 ◽  
Author(s):  
Adeleh Divsalar ◽  
Ali A. Saboury ◽  
Thomas Haertlé ◽  
Lindsay Sawyer ◽  
Hassan Mansouri-Torshizi ◽  
...  
Keyword(s):  
Calorimetric Study ◽  
Chloride Binding ◽  
Β Lactoglobulin

scholarly journals A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate

1977 ◽  
Vol 44 (3) ◽  
pp. 509-520 ◽  
Author(s):  
M. Rüegg ◽  
Ursula Moor ◽  
B. Blanc
Keyword(s):  
Heat Treatment ◽  
Xanthine Oxidase ◽  
Conformational Changes ◽  
Thermal Denaturation ◽  
Whey Proteins ◽  
Calorimetric Study ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Β Lactoglobulin ◽  
Dsc Thermograms

SummaryDifferential scanning calorimetry (DSC) was used to study thermal transitions of the following whey proteins and enzymes in milk ultrafiltrate solution: β-lactoglobulin, α-lactalbumin, serum albumin, γ-globulin, apo- and Fe-lactoferrin, lysozyme, ribonuclease, α-chymotrypsin and xanthine oxidase. Denaturation enthalpies (ΔHD), denaturation temperatures (TD) and the half width of the denaturation peaks in DSC thermograms (ΔT½D) were determined and the degree of renaturation was estimated by rescanning previously denatured samples. A fair correlation between the results obtained by DSC and other more classical methods was found in general. However, for some proteins (α-lactalbumin, lysozyme, ribonuclease and xanthine oxidase), which have so far been considered relatively thermostable, calorimetry reveals conformational changes starting at temperatures as low as about 45 °C. In these cases thermostability observed after heat treatment of milk should be interpreted in terms of renaturation and not of high temperatures of denaturation.

A differential scanning calorimetric study of β-lactoglobulin and vitamin D3 complexes

2012 ◽  
Vol 110 (1) ◽  
pp. 473-477 ◽  
Author(s):  
Agata Górska ◽  
Ewa Ostrowska-Ligęza ◽  
Karolina Szulc ◽  
Magdalena Wirkowska
Keyword(s):  
Vitamin D3 ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Β Lactoglobulin

scholarly journals Differential Scanning Calorimetric Study of Different Genetic Variants of β-Lactoglobulin

1991 ◽  
Vol 74 (8) ◽  
pp. 2416-2422 ◽  
Author(s):  
Gilbert Idolo Imafidon ◽  
K.F. Ng-Kwai-Hang ◽  
V.R. Harwalkar ◽  
C.-Y. Ma
Keyword(s):  
Genetic Variants ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Β Lactoglobulin

A differential scanning calorimetric study of the thermal behaviour of bovine β-lactoglobulin at temperatures up to 160 °C

1981 ◽  
Vol 48 (2) ◽  
pp. 293-302 ◽  
Author(s):  
Jacob N. de Wit ◽  
Gijsbert Klarenbeek
Keyword(s):  
Thermal Behaviour ◽  
Conformational Changes ◽  
Temperature Shift ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Scanning Calorimetry ◽  
Maximum Heat ◽  
Β Lactoglobulin ◽  
Endothermal Peak ◽  
Dsc Curves

SummaryThe thermal behaviour of β-lactoglobulin was studied by differential scanning calorimetry (DSC) in the temperature range 40–160 °C. The DSC curves revealed, in addition to the usually observed denaturation peak near 80 °C, a distinct endothermal peak between 130 and 150 °C. When the pH was increased from 6·5, the area under the peak near 80 °C (denaturation heat) decreased significantly, whereas the peak area near 140 °C increased. The temperature of maximum heat absorption in the peaks near both 80 and 140 °C gradually increased as the pH decreased. Addition of sugars and variation of the heating rate both caused a temperature shift of the endothermal heat effect at 140 °C, similar to that at 80 °C. No peak near 140 °C was observed when β-mercapto-ethanol was added to the β-lactoglobulin solution before scanning. The origin and nature of the high temperature denaturation peak is discussed in terms of conformational changes of the protein.

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