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Open Access research with a European policy impact...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by Strathclyde researchers, including by researchers from the European Policies Research Centre (EPRC).

EPRC is a leading institute in Europe for comparative research on public policy, with a particular focus on regional development policies. Spanning 30 European countries, EPRC research programmes have a strong emphasis on applied research and knowledge exchange, including the provision of policy advice to EU institutions and national and sub-national government authorities throughout Europe.

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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

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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.