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Modification of β-lactoglobulin by oligofructose: Impact on protein adsorption at the air-water interface

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Author: Trofimova, D. · Jongh,
Institution: TNO Voeding
Source:Langmuir, 13, 20, 5544-5552
Identifier: 237845
doi: doi:10.1021/la049390j
Keywords: Nutrition · Food technology · Adsorption · Chemical modification · Contacts (fluid mechanics) · Differential scanning calorimetry · Elastic moduli · Fluorescence · Proteins · β-lactoglobulin · Drop tensiometry · Oligofructose · Fructose · Adsorption · Calorimetry · Circular Dichroism · Elastic Strength · Fluorescence · Fructose · Globulins · Oligosaccharides · Proteins · lactoglobulin · oligofructose · oligosaccharide · water · adsorption · air · article · chemistry · elasticity · ion exchange chromatography · metabolism · pH · phase transition · protein folding · protein secondary structure · spectroscopy · thermodynamics · time · viscosity · Adsorption · Air · Chromatography, Ion Exchange · Elasticity · Hydrogen-Ion Concentration · Lactoglobulins · Oligosaccharides · Phase Transition · Protein Folding · Protein Structure, Secondary · Spectrum Analysis · Thermodynamics · Time Factors · Viscosity · Water


Maillard products of β-lactoglobulin (βLg) and fructose oligosaccharide (FOS) were obtained in different degrees of modification depending on incubation time and pH. By use of a variety of biochemical and spectroscopic tools, it was demonstrated that the modification at limited degrees does not significantly affect the secondary, tertiary, and quaternary structure of βLg. The consequence of the modification on the thermodynamics of the protein was studied using differential scanning calorimetry, circular dichroism, and by monitoring the fluorescence intensity of protein samples with different concentrations of guanidine-HCl. The modification leads to lowering of the denaturation temperature by 5°C and a reduction of the free energy of stabilization of about 30%, Ellipsometry and drop tensiometry demonstrated that upon adsorption to air-water interfaces in equilibrium modified βLg exerts a lower surface pressure than native βLg (16 versus 22 mN/m). Moreover, the surface elastic modulus increased with increasing surface pressure but reached significantly smaller values in the case of FOS-βLg. Compared to native βLg, modification of the protein with oligofructose moieties results in higher surface loads and thicker surface layers. The consequences of these altered surface rheological properties are discussed in view of the functional behavior in technological applications.