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

Published online by Cambridge University Press:  01 June 2009

M. Rüegg ,
Ursula Moor  and
B. Blanc
M. Rüegg
Affiliation:
Federal Dairy Research Institute, 3097 Liebefeld, Bern, Switzerland
Ursula Moor
Affiliation:
Federal Dairy Research Institute, 3097 Liebefeld, Bern, Switzerland
B. Blanc
Affiliation:
Federal Dairy Research Institute, 3097 Liebefeld, Bern, Switzerland
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Summary

Differential 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.

Type
Original Articles
Information
Journal of Dairy Research , Volume 44 , Issue 3 , October 1977 , pp. 509 - 520
Copyright
Copyright © Proprietors of Journal of Dairy Research 1977

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