Foams Stabilized by β‑Lactoglobulin Amyloid Fibrils: Effect of pH
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. R...
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Published in | Journal of agricultural and food chemistry Vol. 65; no. 48; pp. 10658 - 10665 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
06.12.2017
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Subjects | |
Online Access | Get full text |
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Summary: | 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 (t 1/2) 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 (t 1/2 ≈ 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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ISSN: | 0021-8561 1520-5118 |
DOI: | 10.1021/acs.jafc.7b03669 |