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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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
28
issue
32
pages
11852 - 11858
publisher
The American Chemical Society
external identifiers
  • wos:000307479000021
  • scopus:84865179049
ISSN
0743-7463
DOI
10.1021/la300892p
language
English
LU publication?
yes
id
307baa66-5067-42ff-bd38-4ef02e3c6c4f (old id 3059327)
date added to LUP
2012-09-25 13:59:55
date last changed
2017-09-24 03:26:15
@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},
  series       = {Langmuir},
  title        = {Adsorption of Unstructured Protein beta-Casein to Hydrophobic and Charged Surfaces},
  url          = {http://dx.doi.org/10.1021/la300892p},
  volume       = {28},
  year         = {2012},
}