Abstract
Hypothesis
The structural details of foams made with pea albumins are affected by the pH of the initial solution and followed heat treatment.
Experiments
An in situ, time-resolved investigation of foams prepared with pea albumins was conducted using small-angle neutron scattering (SANS) in combination with imaging and conductance measurements. Solutions were tested at pH three pH values (3, 4.5, and 8) before and after heating (90 °C for 1 and 5 min).
Findings
The characteristic structures present in the foam from the nano to the meso-scale differed during drainage depending on solution pH. Foams obtained at pH 3, had the largest bubble radius and thinnest plateau border, as well as the highest extent of liquid drainage. At pH 4.5, close to the isoelectric point of the proteins, foams displayed similar bubbles’ behavior to those at pH 8, but with the largest film thickness. In this case, the proteins were extensively aggregated. Heating of the solutions prior to foaming did not significantly affect the foam aging regardless of pH. The quantification of specific surface areas and film thickness over time without sample disruption shows to be a powerful approach to designing foam structures.
The structural details of foams made with pea albumins are affected by the pH of the initial solution and followed heat treatment.
Experiments
An in situ, time-resolved investigation of foams prepared with pea albumins was conducted using small-angle neutron scattering (SANS) in combination with imaging and conductance measurements. Solutions were tested at pH three pH values (3, 4.5, and 8) before and after heating (90 °C for 1 and 5 min).
Findings
The characteristic structures present in the foam from the nano to the meso-scale differed during drainage depending on solution pH. Foams obtained at pH 3, had the largest bubble radius and thinnest plateau border, as well as the highest extent of liquid drainage. At pH 4.5, close to the isoelectric point of the proteins, foams displayed similar bubbles’ behavior to those at pH 8, but with the largest film thickness. In this case, the proteins were extensively aggregated. Heating of the solutions prior to foaming did not significantly affect the foam aging regardless of pH. The quantification of specific surface areas and film thickness over time without sample disruption shows to be a powerful approach to designing foam structures.
| Original language | English |
|---|---|
| Journal | Journal of Colloid and Interface Science |
| Volume | 678 |
| Issue | Part B |
| Pages (from-to) | 1049-1060 |
| Number of pages | 12 |
| ISSN | 0021-9797 |
| DOIs | |
| Publication status | Published - 15 Jan 2025 |
Keywords
- Albumins
- Conductance
- Image analysis
- Liquid foam
- Pea proteins
- Plateau border
- SANS
- Thin film