On the complexation of whey proteins

Author(s)

Delboni, Lariani Aparecida ^{[1, 2]} ; Barroso da Silva, Fernando Luis ^{[1, 2]}

Affiliation

^[1] Univ Sao Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Dept Fis & Quim, BR-14040903 Ribeirao Preto, SP - Brazil

^[2] Lund Univ, Dept Theoret Chem, S-22100 Lund - Sweden

• Document type: Journal article
• Source: FOOD HYDROCOLLOIDS; v. 55, p. 89-99, APR 2016.
• Web of Science Citations: 11

Abstract

Milk proteins have a rich diversity of physical chemistry and biodegradable properties which makes them appealing for different food and pharmaceutical applications. Theoretical coarse grained models and numerical simulations were employed here in order to gain novel insight into the understanding of the fundamental mechanisms of the process of milk proteins complexation in a diversity of environmental conditions. The interactions between alpha-lactalbumin, beta-lactoglobulin and lactoferrin were investigated by means of Monte Carlo simulations. The comparison between the free energies associated with the complexation of alpha-lactalbumine-lactoferrin and beta-lactoglobuline-lactoferrin at different pH and ionic strengths let us to explain why is experimentally observed the later complex and not the alpha-lactalbumine-lactoferrin complex. (C) 2015 Elsevier Ltd. All rights reserved. (AU)