Thermodynamic parameters of β-lactoglobulin and α-lactalbumin. A DSC study of denaturation by heating

The thermodynamic parameters of β-lactoglobulin and α-lactalbumin heat denaturation, at acid and neutral pH respectively, were determined by differential scanning calorimetry using heating rates ranging from 2.5 to 15°C min −1. At the high heating rates, the heat denaturation of bovine β-lactoglobul...

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Bibliographic Details
Published in:Thermochimica acta 1992-07, Vol.204 (1), p.111-121
Main Authors: Relkin, P., Eynard, L., Launay, B.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Glycoproteins
Proteins
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Summary:The thermodynamic parameters of β-lactoglobulin and α-lactalbumin heat denaturation, at acid and neutral pH respectively, were determined by differential scanning calorimetry using heating rates ranging from 2.5 to 15°C min −1. At the high heating rates, the heat denaturation of bovine β-lactoglobulin (crystallized three times or obtained by microfiltration) at about 2–3 mM protein concentration, was found to be partly reversible. The corresponding temperatures and enthalpy changes are protein-concentration-dependent. α-Lactalbumin, in both free and bound Ca 2+ forms, shows total reversibility. The effect of adding Ca 2+ to the Ca 2+-free form was studied, and the thermodynamic parameters of the transition were determined and compared with published results obtained at lower protein concentrations.
ISSN:0040-6031
1872-762X
DOI:10.1016/0040-6031(92)80320-V