Interactive Effects of Pressure, Temperature and Time on the Molecular Structure of β-Lactoglobulin |
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Authors: | L-A. Tedford S.M. Kelly N.C. Price C.J. Schaschke |
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Affiliation: | Authors Tedford and Schaschke are affiliated with the Dept. of Chemical &Process Engineering, Univ. of Strathclyde, Glasgow, G1 1XJ, UK.;Authors Kelly and Price are affiliated with the Dept. of Biological &Molecular Sciences, Univ. of Stirling, Stirling, UK. |
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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. |
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Keywords: | high pressure β-lactoglobulin tertiary structure circular dichroism |
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