Physical-chemical comparison of cow’s milk proteins versus soy proteins in their calcium-binding capacities

Abstract : In this study, calcium-protein interactions were thermodynamically characterized in cow's milk and in (Non-Hydrolysed, NH, or Hydrolysed, H) soy protein dispersions using Isothermal Titration Calorimetry (ITC). Both systems were compared in order to determine the efficiency of soy proteins as a possible vector for further calcium (Ca) supplementation. Regardless of the system (milk, Non-Hydrolysed and Hydrolysed-soy proteins), the thermodynamic signal from Ca-protein interactions was endothermic in nature, and was fitted by a one set of sites model. Whatever the system, mu(E) variations were clearly indicative of Ca-protein interactions of an electrostatic nature. Hence, the exothermic part of the signal due to electrostatic interactions was completely hidden by a strong endothermic signal. Not the Coulomb interactions but instead water molecule release, either from the hydration shells of the calcium ion and/or dehydration of the hydrophobic core of the proteins may be the driving energy source for the Ca binding onto milk or soy proteins. The nature of the Ca-protein interaction was similar in all three systems. Furthermore, as compared to milk protein, containing less Ca bound to the protein, the NH-soy protein system could be a possible protein vector for further Ca supplementation
Type de document :
Article dans une revue
Colloids and Surface A: Physicochemical and Engineering Aspects. , 2010, 366 (1-3), pp.110-112. 〈10.1016/j.colsurfa.2010.05.030〉
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https://hal.univ-lorraine.fr/hal-01620305
Contributeur : Laetitia Canabady-Rochelle <>
Soumis le : vendredi 20 octobre 2017 - 13:19:31
Dernière modification le : mardi 24 octobre 2017 - 01:11:00

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Laetitia Canabady-Rochelle, Michel Mellema. Physical-chemical comparison of cow’s milk proteins versus soy proteins in their calcium-binding capacities. Colloids and Surface A: Physicochemical and Engineering Aspects. , 2010, 366 (1-3), pp.110-112. 〈10.1016/j.colsurfa.2010.05.030〉. 〈hal-01620305〉

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