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  • Title: Foams Stabilized by β-Lactoglobulin Amyloid Fibrils: Effect of pH.
    Author: Peng D, Yang J, Li J, Tang C, Li B.
    Journal: J Agric Food Chem; 2017 Dec 06; 65(48):10658-10665. PubMed ID: 29135243.
    Abstract:
    β-Lactoglobulin fibrils could serve as a surface-active component and form adsorption layers at the air/water interface. In this study, the physical parameters related to the surface adsorption, foaming, and surface properties of β-lactoglobulin fibrils as a function of pH (2-8) were investigated. Results showed that an increase of pH from 2 to 5 led to a rise of the viscoelastic modulus of the surface adsorption layer and half-life time (t1/2) of foams, but it decreased foamability. When the pH was close to its isoelectric point (5.2), fibrils had the lowest electrostatic repulsion and entangled at the air/water interface resulting in a tightly packaged adsorption layer around bubbles to prevent coalescence and coarsening. When the pH (7-8) was higher than the pI of fibrils, the negatively charged β-lactoglobulin fibrils possessed good foamability (∼80%) and high foam stability (t1/2 ≈ 8 h) simultaneously even at low concentration (1 mg/mL). It demonstrated that β-lactoglobulin fibrils with negative charges presented a good foaming behavior and could be a potential new foaming agent in the food industry.
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