β-Carotene and Milk Protein Complexation: a Thermodynamic Approach and a Photo Stabilization Study

The demand for bioactive molecules, such as β-carotene (β-car), has increased, but some characteristics such as low water solubility and low photo stability limit its application in many formulations. The bioactive entrapment into milk proteins may overcome this barrier. Thus, the aim of this work w...

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Bibliographic Details
Published in:Food and bioprocess technology 2018-03, Vol.11 (3), p.610-620
Main Authors: Silva, Carla Eduarda Ladeira, Hudson, Eliara Acipreste, Agudelo, Álvaro Javier Patiño, da Silva, Luis Henrique Mendes, Pinto, Maximiliano Soares, do Carmo Hespanhol, Maria, Barros, Frederico Augusto Ribeiro, dos Santos Pires, Ana Clarissa
Format: Article
Language:English
Subjects:
Agriculture
Biological activity
Biotechnology
Bovine serum albumin
Carotene
Casein
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Complex formation
Entrapment
Entropy
Fluorescence
Fluorescence spectroscopy
Food Science
Free energy
Micelles
Milk
Original Paper
Proteins
Serum albumin
Stability
Stoichiometry
β-Carotene
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Summary:The demand for bioactive molecules, such as β-carotene (β-car), has increased, but some characteristics such as low water solubility and low photo stability limit its application in many formulations. The bioactive entrapment into milk proteins may overcome this barrier. Thus, the aim of this work was to study the interaction between β-car and bovine serum albumin (BSA) or β-casein and the photo stability of this bioactive in the presence of the proteins. Fluorescence spectroscopy showed that at pH 7.0, increasing concentrations of β-carotene reduced the fluorescence intensity of both proteins, and the fluorescence-quenching mechanism is mainly static. The stoichiometry of the β-car/protein complex varied between proteins, being 1:1 to native BSA, 1:3 to denatured BSA (d-BSA), and 1:2 for β-casein. The standard Gibbs-free energy (Δ G °) of complex formation was negative for all systems studied and followed the order Δ G ° BSA  
ISSN:1935-5130
1935-5149
DOI:10.1007/s11947-017-2028-7