Whey protein nanoparticles prepared with desolvation with ethanol: Characterization, thermal stability and interfacial behavior

Abstract

Whey protein isolate (WPI) nanoparticles were prepared by diluting an alkaline solution of protein in ethanol at concentrations varying between 50 and 80%. The nanoparticles were then immediately diluted in buffer. While the nanoparticles were not stable at pH 7, they showed no changes in size when diluted at pH 3. When 75–80% ethanol was added during preparation, the size of the WPI nanoparticles ranged between 10 and 100 nm, with no change in size after dilution and storage at pH 3 for 96 h at 22 °C. When heating was applied, particle aggregation occurred, and large aggregates (>1 μm) were observed at temperatures > 60 °C. The particle size of the heat-induced aggregates could be reduced by homogenization. The nanoparticles prepared by desolvation showed interfacial pressure values similar to those of the corresponding protein solutions, indicating similar interfacial properties and the potential to be used to stabilize emulsions but as supramolecular aggregates of WPI.