Adsorption of Unstructured Protein beta-Casein to Hydrophobic and Charged Surfaces

Summary, in English

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: Chris H. J. Evers; Thorbjorn Andersson; Mikael Lund; Marie Skepö
• Department/s: Computational Chemistry; eSSENCE: The e-Science Collaboration
• Publishing year: 2012
• Language: English
• Pages: 11852-11858
• Publication/Series: Langmuir
• Volume: 28
• Issue: 32
• Links: http://dx.doi.org/10.1021/la300892p
• Document type: Journal article
• Publisher: The American Chemical Society (ACS)
• Topic: Theoretical Chemistry (including Computational Chemistry)
• Status: Published
• ISBN/ISSN/Other: ISSN: 0743-7463