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Efficiency of milk proteins in eliminating practical limitations of β-carotene in hydrated polar solution

Abstract : The objective of this work was to study beta-carotene functionalities (color and antioxidant activity) and practical limitations (aggregate formation, poor solubility and low stability) when included in the aqueous systems containing milk proteins. According to the results, self-association constant of beta-carotene in the presence of casein is 1.7-fold of that calculated for WPI. Casein and WPI were capable of conserving beta-carotene against chemical oxidation up to 15 and 12%, respectively, at 1:5 M ratio of beta-carotene to protein. While, WPI reduced its photodegradation quantum yield from 0.03 to 0.012 compared to 0.017 obtained for casein. A 2.7-and 3.6-fold enhancement in beta-carotene solubility was observed in the presence of 1.5 mg/mL of casein and WPI, re-spectively. The study of beta-carotene interaction with proteins showed, on the one hand, a negative effect on electron transfer and, on the other hand, improved hydrogen transfer to the radical species in the solution.
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https://hal.inrae.fr/hal-03154830
Contributor : Olivier Dupre <>
Submitted on : Tuesday, March 2, 2021 - 10:39:46 AM
Last modification on : Tuesday, March 2, 2021 - 10:39:47 AM

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Zahra Allahdad, Mehdi Varidi, Reza Zadmard, Thomas Haertlé, Lindsay Sawyer, et al.. Efficiency of milk proteins in eliminating practical limitations of β-carotene in hydrated polar solution. Food Chemistry, Elsevier, 2020, 330, pp.127218. ⟨10.1016/j.foodchem.2020.127218⟩. ⟨hal-03154830⟩

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