Abstract
We studied the combined effects of several variables, using temperatures up to 79°C and pressures up to 105 MPa, on β-lactoglobulin at pH 7.0 and pH 5.6 by examination of circular dichroism spectra and application of experimental design methodology. The higher pressures were not sufficient to impart the energy necessary to disrupt the protein structure. When used in combination with temperature and holding time, the applied energy was sufficient to disrupt the tertiary structure of the protein. Processing conditions applied at specific pH therefore could act in combination to cause structural changes.
| Original language | English |
|---|---|
| Pages (from-to) | 396-399 |
| Number of pages | 4 |
| Journal | Journal of Food Science |
| Volume | 64 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - May 1999 |
Keywords
- high pressure
- β-lactoglobulin
- tertiary structure
- circular dichroism
ASJC Scopus subject areas
- Food Science