Picture of a sphere with binary code

Making Strathclyde research discoverable to the world...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs. It exposes Strathclyde's world leading Open Access research to many of the world's leading resource discovery tools, and from there onto the screens of researchers around the world.

Explore Strathclyde Open Access research content

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

Vant, Stewart C. and Glen, Norman and Kontopidis, George and Sawyer, Lindsay and Schaschke, Carl J. (2002) Volumetric changes to the molecular structure of beta-lactoglobulin processed at high pressure. High Temperature High Pressure, 34 (6). pp. 705-712. ISSN 0018-1544

Full text not available in this repository. (Request a copy from the Strathclyde author)

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.