Abstract
The effect of hydrostatic pressure treatment (150 and 250 MPa) on the structure and foaming characteristics of dimeric β-lactoglobulin (β-LG) at pH 7.0 is investigated. Angle- and concentration-dependent dynamic light scattering is used to probe pressure-induced changes in size under ambient conditions. The cumulant method is used to analyze correlation functions of the dynamic light scattering experiments and to estimate hydrodynamic radii and the width of their distribution. Instead of a decrease, hydrodynamic radii slightly increase after pressure treatment and depend on protein concentration. Both native and pressurized samples are almost free of aggregates as indicated by a small polydispersity index, PDI < 0.25. A small fraction of larger aggregates in the native sample is not affected by the pressure treatment and only bias the scattering signal at low scattering angles. Circular dichroism measurements indicate transformation of the secondary structure into a random coil for the pressurized samples. Only slightly unfolded β-LG stabilizes foam best because the largest effect is observed for samples treated with 150 MPa. Pressure-modified β-LG could have the potential to be used as a stabilizer in the food industry because of the low pressure needed during processing.
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