Volumetric changes to the molecular structure of β-lactoglobulin processed at high pressure

Stewart C. Vant*, Norman F. Glen, George Kontopidis, Lindsay Sawyer, Carl J. Schaschke

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

We measured in-situ the volumetric changes to the molecular structure of the bovine milk protein β-lactoglobulin in a series of high-pressure processing experiments. We used the so-called μPVT device at hydrostatic pressures up to 500 MPa under isothermal conditions of 25 °, the protein in solution, prepared at both pH 5.0 and 7.0, in a series of compression and decompression cycles. Significant irreversible volumetric changes were found, most notably with a marked step decrease in molar volume of 1.3 litre mol -1 occurring between 10 and 17 MPa. Irreversible molar volume changes of 2.16 litre mol-1 were found when pressures above 17 MPa were applied. This is thought to be due in part to a collapse of the inner calyx. Volume changes were confirmed by measuring the unit-cell volume of the crystalline protein. The effects of pH were indistinguishable. These pressures are considerably less than previously thought necessary for this protein.

Original languageEnglish
Pages (from-to)705-712
Number of pages8
JournalHigh Temperatures - High Pressures
Volume34
Issue number6
DOIs
Publication statusPublished - 4 Aug 2002

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Mechanics of Materials
  • Physical and Theoretical Chemistry

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