Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 369495
Title Protein adsorption at air-water interfaces: A combination of details
Author(s) Jongh, H.H.J. de; Kosters, H.A.; Kudryashova, E.; Meinders, M.B.J.; Trofimova, D.; Wierenga, P.A.
Source Biopolymers 74 (2004)1-2. - ISSN 0006-3525 - p. 131 - 135.
DOI https://doi.org/10.1002/bip.20036
Department(s) Food Chemistry Group
WU Agrotechnology and Food SciencesDepartment of Agrotechnology and Food Sciences
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2004
Keyword(s) air/water interface - ovalbumin - stability
Abstract Using a variety of spectroscopic techniques, a number of molecular functionalities have been studied in relation to the adsorption process of proteins to air-water interfaces. While ellipsometry and drop tensiometry are used to derive information on adsorbed amount and exerted surface pressure, external reflection circular dichroism, infrared, and fluorescence spectroscopy provide, next to insight in layer thickness and surface layer concentration, molecular details like structural (un)folding, local mobility, and degree of protonation of carboxylates. It is shown that the exposed hydrophobicity of the protein or chemical reactivity of solvent-exposed groups may accelerate adsorption, while increased electrostatic repulsion slows down the process. Also aggregate formation enhances the fast development of a surface pressure. A more bulky appearance of proteins lowers the collision intensity in the surface layer, and thereby the surface pressure, while it is shown to be difficult to affect protein interactions within the surface layer on basis of electrostatic interactions. This work illustrates that the adsorption properties of a protein are a combination of molecular details, rather than determined by a single one
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