Advanced

On the complexation of whey proteins

Delboni, Lariani A LU and Da Silva, Fernando Luis Barroso LU (2016) In Food Hydrocolloids 55. p.89-99
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Milk proteins, Electrostatic interactions, pH, Ionic strength, Molecular, modeling, Heteroprotein association
in
Food Hydrocolloids
volume
55
pages
89 - 99
publisher
Elsevier
external identifiers
  • wos:000366930200011
  • scopus:84947556525
ISSN
0268-005X
DOI
10.1016/j.foodhyd.2015.11.010
language
English
LU publication?
yes
id
3198a118-2feb-4845-8243-1be65fb82839 (old id 8539878)
date added to LUP
2016-01-26 10:45:35
date last changed
2017-11-05 03:24:34
@article{3198a118-2feb-4845-8243-1be65fb82839,
  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.},
  author       = {Delboni, Lariani A and Da Silva, Fernando Luis Barroso},
  issn         = {0268-005X},
  keyword      = {Milk proteins,Electrostatic interactions,pH,Ionic strength,Molecular,modeling,Heteroprotein association},
  language     = {eng},
  pages        = {89--99},
  publisher    = {Elsevier},
  series       = {Food Hydrocolloids},
  title        = {On the complexation of whey proteins},
  url          = {http://dx.doi.org/10.1016/j.foodhyd.2015.11.010},
  volume       = {55},
  year         = {2016},
}