UCL logo

UCL Discovery

UCL home » Library Services » Electronic resources » UCL Discovery

Strong improvement of interfacial properties can result from slight structural modifications of proteins: the case of native and dry-heated lysozyme.

Desfougères, Y; Saint-Jalmes, A; Salonen, A; Vié, V; Beaufils, S; Pezennec, S; Desbat, B; ... Nau, F; + view all (2011) Strong improvement of interfacial properties can result from slight structural modifications of proteins: the case of native and dry-heated lysozyme. Langmuir , 27 (24) pp. 14947-14957. 10.1021/la203485y.

Full text not available from this repository.

Abstract

Identification of the key physicochemical parameters of proteins that determine their interfacial properties is still incomplete and represents a real stake challenge, especially for food proteins. Many studies have thus consisted in comparing the interfacial behavior of different proteins, but it is difficult to draw clear conclusions when the molecules are completely different on several levels. Here the adsorption process of a model protein, the hen egg-white lysozyme, and the same protein that underwent a thermal treatment in the dry state, was characterized. The consequences of this treatment have been previously studied: net charge and hydrophobicity increase and lesser protein stability, but no secondary and tertiary structure modification (Desfougères, Y.; Jardin, J.; Lechevalier, V.; Pezennec, S.; Nau, F. Biomacromolecules 2011, 12, 156-166). The present study shows that these slight modifications dramatically increase the interfacial properties of the protein, since the adsorption to the air-water interface is much faster and more efficient (higher surface pressure). Moreover, a thick and strongly viscoelastic multilayer film is created, while native lysozyme adsorbs in a fragile monolayer film. Another striking result is that completely different behaviors were observed between two molecular species, i.e., native and native-like lysozyme, even though these species could not be distinguished by usual spectroscopic methods. This suggests that the air-water interface could be considered as a useful tool to reveal very subtle differences between protein molecules.

Type: Article
Title: Strong improvement of interfacial properties can result from slight structural modifications of proteins: the case of native and dry-heated lysozyme.
Location: United States
DOI: 10.1021/la203485y
Keywords: Adsorption, Air, Animals, Chemistry, Physical, Chickens, Desiccation, Elasticity, Hot Temperature, Hydrophobic and Hydrophilic Interactions, Kinetics, Microscopy, Atomic Force, Molecular Conformation, Muramidase, Pressure, Rheology, Spectrum Analysis, Static Electricity, Surface Properties, Thermodynamics, Viscosity, Water
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
URI: http://discovery.ucl.ac.uk/id/eprint/1521426
Downloads since deposit
0Downloads
Download activity - last month
Download activity - last 12 months
Downloads by country - last 12 months

Archive Staff Only

View Item View Item