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Limited conformational change of β-lactoglobulin when adsorbed at the air–water interface

✍ Scribed by Marcel B. J. Meinders; Harmen H. J. De Jongh

Publisher
Wiley (John Wiley & Sons)
Year
2002
Tongue
English
Weight
90 KB
Volume
67
Category
Article
ISSN
0006-3525

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✦ Synopsis

Detailed insight can be obtained from proteins at and near the air-water interface using external reflection IR and circular dichroism techniques. Besides information on local protein concentrations and surface layer thickness, it is shown that beta-lactoglobulin displays a limited unfolding at the interface. The conformational change is comparable to that observed upon heat-induced aggregation of the protein and can be understood in view of the high surface concentration of the protein (approximately 40% volume fraction). The layer thickness and the conformational properties of the protein do not depend on the bulk concentration. After adsorption of beta-lactoglobulin to a preformed lipid monomolecular layer a similar conformational change is induced, suggesting that the folding properties of the protein itself determine the extent of conformational changes at the interfaces.

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