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Issue Lait
Volume 87, Number 4-5, July-October 2007
27th IDF World Dairy Summit and Congress
Page(s) 301 - 315
DOI http://dx.doi.org/10.1051/lait:2007012
Published online 26 October 2007

Lait 87 (2007) 301-315
DOI: 10.1051/lait:2007012

Reaction kinetic pathway of reversible and irreversible thermal denaturation of $\beta $-lactoglobulin

Alexander Tolkach and Ulrich Kulozik

Institute for Food Process Engineering and Dairy Technology, Technical University Munich, Weihenstephaner Berg 1, 85354 Freising-Weihenstephan, Germany

(Published online: 26 October 2007)

Abstract - A reaction kinetic approach for the description of reversible (unfolding) and irreversible (aggregation) denaturation of $\beta $-lactoglobulin ($\beta $-Lg) was developed in this study. This novel approach allows the calculation of the content of native, partially unfolded and irreversibly denatured $\beta $-Lg as a function of the heat treatment time. Moreover, it is able to give a mathematical interpretation of the sharp bend on the Arrhenius plot of the formal denaturation rate constant which is characteristic of the denaturation behaviour of both major whey proteins, $\alpha$-lactalbumin and $\beta $-lactoglobulin. The developed theoretical backgrounds were applied for the denaturation kinetics of $\beta $-Lg in a protein solution containing 50 g$\cdot$L-1 of the isolated whey protein fraction and verified by means of differential scanning calorimetry.


Résumé - Cinétique de la réaction de dénaturation réversible et irréversible de la $\beta $-lactoglobuline ($\beta $-Lg)
Une approche de la cinétique de réaction pour décrire la dénaturation réversible (dépliement) et irréversible (agrégation) de la $\beta $-Lg a été développée dans cette étude. Ce nouveau modèle cinétique permet de calculer la fraction de $\beta $-Lg native, partiellement dépliée et irréversiblement dénaturée en fonction de la durée de traitement thermique. De plus, l'approche cinétique développée est capable de donner une interprétation mathématique du brusque changement de pente de la constante de dénaturation en fonction de la température, caractéristique du comportement de dénaturation des deux protéines sériques majeures, $\alpha$-lactalbumine et $\beta $-lactoglobuline. Le modèle théorique développé a été appliqué à l'étude de la cinétique de dénaturation de la $\beta $-Lg dans une solution protéique à 50 g$\cdot$L-1 de la fraction de protéine sérique isolée, et vérifié par mesure en calorimétrie différentielle.


Key words: $\beta $-lactoglobulin / thermal denaturation / unfolding / aggregation / reaction kinetic

Mots clés : $\beta $-lactoglobuline / dénaturation thermique / dépliement / agrégation / cinétique de réaction

Corresponding author: Alexander.Tolkach@wzw.tum.de

© INRA, EDP Sciences 2007


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