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

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

Research output: Contribution to journalArticle

6 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 °C, 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.
LanguageEnglish
Pages705-712
Number of pages7
JournalHigh Temperature High Pressure
Volume34
Issue number6
DOIs
Publication statusPublished - 4 Aug 2002

Fingerprint

Lactoglobulins
Molecular structure
molecular structure
proteins
Proteins
Density (specific gravity)
Milk Proteins
Hydrostatic pressure
Protein C
milk
pressure reduction
hydrostatic pressure
Crystalline materials
Processing
cycles
cells
Experiments

Keywords

  • volumetric changes
  • molecular structure
  • beta-lactoglobulin
  • high pressure
  • high temperature

Cite this

Vant, Stewart C. ; Glen, Norman ; Kontopidis, George ; Sawyer, Lindsay ; Schaschke, Carl J. / Volumetric changes to the molecular structure of beta-lactoglobulin processed at high pressure. In: High Temperature High Pressure. 2002 ; Vol. 34, No. 6. pp. 705-712.
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Volumetric changes to the molecular structure of beta-lactoglobulin processed at high pressure. / Vant, Stewart C.; Glen, Norman; Kontopidis, George; Sawyer, Lindsay; Schaschke, Carl J.

In: High Temperature High Pressure, Vol. 34, No. 6, 04.08.2002, p. 705-712.

Research output: Contribution to journalArticle

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T1 - Volumetric changes to the molecular structure of beta-lactoglobulin processed at high pressure

AU - Vant, Stewart C.

AU - Glen, Norman

AU - Kontopidis, George

AU - Sawyer, Lindsay

AU - Schaschke, Carl J.

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AB - 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 °C, 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.

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KW - molecular structure

KW - beta-lactoglobulin

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KW - high temperature

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