On the complexation of whey proteins

Research output: Contribution to journalArticle

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.

Details

Authors
  • Lariani A Delboni
  • Fernando Luis Barroso Da Silva
Organisations
External organisations
  • University of São Paulo
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Theoretical Chemistry

Keywords

  • Milk proteins, Electrostatic interactions, pH, Ionic strength, Molecular, modeling, Heteroprotein association
Original languageEnglish
Pages (from-to)89-99
JournalFood Hydrocolloids
Volume55
Publication statusPublished - 2016
Publication categoryResearch
Peer-reviewedYes