Interactive effects of pressure, temperature and time on the molecular structure of β-lactoglobulin

L. A. Tedford, S. M. Kelly, N. C. Price, C. J. Schaschke

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

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 languageEnglish
Pages (from-to)396-399
Number of pages4
JournalJournal of Food Science
Volume64
Issue number3
DOIs
Publication statusPublished - May 1999

Keywords

  • high pressure
  • β-lactoglobulin
  • tertiary structure
  • circular dichroism

ASJC Scopus subject areas

  • Food Science

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