Concentration effects on the kinetics of β-lactoglobulin heat denaturation: a differential scanning calorimetric study

1990 ◽  
Vol 4 (1) ◽  
pp. 19-32 ◽  
Author(s):  
P. Relkin ◽  
B. Launay
Keyword(s):  
Heat Denaturation ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Concentration Effects ◽  
Β Lactoglobulin ◽  
Kinetics Of

A differential scanning calorimetric study of the stability of egg white to heat denaturation

1975 ◽  
Vol 26 (1) ◽  
pp. 73-83 ◽  
Author(s):  
John W. Donovan ◽  
Carol J. Mapes ◽  
John Gorton Davis ◽  
John A. Garibaldi
Keyword(s):  
Egg White ◽  
Heat Denaturation ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
The Stability

A Differential Scanning Calorimetric Study of Carbide Transition in 10Cr Tempered Martensitic Steels

2015 ◽  
Vol 1754 ◽  
pp. 37-42
Author(s):  
H.C. Wang
Keyword(s):  
Electron Microscopy ◽  
Carbide Precipitation ◽  
The Other ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Martensitic Steels ◽  
Scanning Calorimetry ◽  
Precise Understanding ◽  
Kinetics Of

ABSTRACTThe process and kinetics of carbide precipitation upon tempering of an Fe-10Cr-0.15C (wt.%) alloy fabricated from high-purity components has been studied. Differential scanning calorimetry reveals three exotherms in a temperature range of 100-700°C. Using advanced electron microscopy and Kissinger analysis, the exothermic processes have been interpreted. Cementite precipitated first upon tempering at temperatures as low as 200°C; M7C3 and M23C6 appear at higher temperatures, precipitating at approximately the same time but on different sites (M7C3 within grains and laths and M23C6 on grain and lath boundaries). Subsequently, the more stable M23C6 coarsens at the expense of M7C3, which dissolves. The first exotherm was interpreted as being related to the precipitation of cementite whilst the other two overlapping exotherms were interpreted as relating to the concurrent precipitation and coarsening of M7C3 and M23C6, respectively. In-situ SEM and TEM observation is being conducted in order to obtain a more precise understanding and further validate the interpretation of the DSC results.

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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