Limited conformational change of beta-lactoglobulin when adsorbed at the air-water interface |
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Authors: | Meinders Marcel B J De Jongh Harmen H J |
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Institution: | Wageningen Centre for Food Sciences, Diedenweg 20, Wageningen, The Netherlands. m.b.j.meinders@ato.wag-ur.nl |
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Abstract: | 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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