Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study

2000 ◽  
Vol 33 (8) ◽  
pp. 673-682 ◽  
Author(s):  
J.I Boye ◽  
I Alli
1977 ◽  
Vol 44 (3) ◽  
pp. 509-520 ◽  
Author(s):  
M. Rüegg ◽  
Ursula Moor ◽  
B. Blanc

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.


2012 ◽  
Vol 110 (1) ◽  
pp. 473-477 ◽  
Author(s):  
Agata Górska ◽  
Ewa Ostrowska-Ligęza ◽  
Karolina Szulc ◽  
Magdalena Wirkowska

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