On the complexation of whey proteins
(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:
https://lup.lub.lu.se/record/8539878
- author
- Delboni, Lariani A LU and Da Silva, Fernando Luis Barroso LU
- organization
- publishing date
- 2016
- 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
- 2016-04-01 11:07:26
- date last changed
- 2023-01-18 02:10:53
@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}},
keywords = {{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}},
doi = {{10.1016/j.foodhyd.2015.11.010}},
volume = {{55}},
year = {{2016}},
}