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

Published online by Cambridge University Press:  01 June 2009

Jacob N. de Wit  and
Gijsbert Klarenbeek
Jacob N. de Wit
Affiliation:
Netherlands Institute for Dairy Research (NIZO), Ede, The Netherlands
Gijsbert Klarenbeek
Affiliation:
Netherlands Institute for Dairy Research (NIZO), Ede, The Netherlands
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Summary

The 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.

Type
Original Articles
Information
Journal of Dairy Research , Volume 48 , Issue 2 , June 1981 , pp. 293 - 302
Copyright
Copyright © Proprietors of Journal of Dairy Research 1981

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