Adsorption of Unstructured Protein beta-Casein to Hydrophobic and Charged Surfaces
Evers, Chris H. J. ; Andersson, Thorbjorn ; Lund, Mikael LU
and Skepö, Marie
LU
(2012)
In Langmuir
28(32).
p.11852-11858
- Abstract
- In this Monte Carlo simulation study we use mesoscopic modeling to show that beta-casein, an unstructured milk protein, adsorbs to surfaces not only due to direct electrostatic and hydrophobic interactions but also due to structural rearrangement and charge regulation due to proton uptake and release. beta-casein acts as an amphiphilic chameleon, changing properties according to the chemical environment, and binding is observed to both positively and negatively charged surfaces. The binding mechanisms, however, are fundamentally different. A detailed, per-residue-level analysis shows that the adsorption process is controlled by a few very specific regions of the protein and that these change dramatically with pH. Caseins, being the most... (More)
- In this Monte Carlo simulation study we use mesoscopic modeling to show that beta-casein, an unstructured milk protein, adsorbs to surfaces not only due to direct electrostatic and hydrophobic interactions but also due to structural rearrangement and charge regulation due to proton uptake and release. beta-casein acts as an amphiphilic chameleon, changing properties according to the chemical environment, and binding is observed to both positively and negatively charged surfaces. The binding mechanisms, however, are fundamentally different. A detailed, per-residue-level analysis shows that the adsorption process is controlled by a few very specific regions of the protein and that these change dramatically with pH. Caseins, being the most abundant proteins in milk, are crucial for the properties of fermented dairy products, such as nutrition, texture, and viscosity, but may also influence adhesion to packaging materials. The latter leads to product losses of about 10%, leading to economical and environmental problems. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3059327
- author
- Evers, Chris H. J.
; Andersson, Thorbjorn
; Lund, Mikael
LU
and Skepö, Marie
LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 28
- issue
- 32
- pages
- 11852 - 11858
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000307479000021
- scopus:84865179049
- pmid:22783871
- ISSN
- 0743-7463
- DOI
- 10.1021/la300892p
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- 307baa66-5067-42ff-bd38-4ef02e3c6c4f (old id 3059327)
- date added to LUP
- 2016-04-01 11:14:17
- date last changed
- 2023-04-03 22:58:57
@article{307baa66-5067-42ff-bd38-4ef02e3c6c4f,
abstract = {{In this Monte Carlo simulation study we use mesoscopic modeling to show that beta-casein, an unstructured milk protein, adsorbs to surfaces not only due to direct electrostatic and hydrophobic interactions but also due to structural rearrangement and charge regulation due to proton uptake and release. beta-casein acts as an amphiphilic chameleon, changing properties according to the chemical environment, and binding is observed to both positively and negatively charged surfaces. The binding mechanisms, however, are fundamentally different. A detailed, per-residue-level analysis shows that the adsorption process is controlled by a few very specific regions of the protein and that these change dramatically with pH. Caseins, being the most abundant proteins in milk, are crucial for the properties of fermented dairy products, such as nutrition, texture, and viscosity, but may also influence adhesion to packaging materials. The latter leads to product losses of about 10%, leading to economical and environmental problems.}},
author = {{Evers, Chris H. J. and Andersson, Thorbjorn and Lund, Mikael and Skepö, Marie}},
issn = {{0743-7463}},
language = {{eng}},
number = {{32}},
pages = {{11852--11858}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Langmuir}},
title = {{Adsorption of Unstructured Protein beta-Casein to Hydrophobic and Charged Surfaces}},
url = {{http://dx.doi.org/10.1021/la300892p}},
doi = {{10.1021/la300892p}},
volume = {{28}},
year = {{2012}},
}