Molecular studies of pressure & temperature induced structural changes in protein

-lactoglobulin in Tris-HCl buffer pH 7 50 mM was treated with combined pressure and temperature
treatments using a central composite experimental design. Pressures studied were up to 294 MPa,
temperatures up to 62°C and processing times up to 30 minutes. The molecular structure, at a secondary and
tertiary level, was analysed post-processing using far and near-UV circular dichroism. It was found that,
although the pressures applied were moderate, the far-UV circular dichroism spectra showed important
changes corresponding to an increase in -helical content. The tertiary structure was almost completely lost
for the highest processing intensities. This suggests a transition to the molten globule state. The percentage
change in ellipticities at 293 nm (tertiary structure) were found to be linearly connected to the three
independent variables hence possibly allowing process optimisation for that response. Pressure was found to
be the most important parameter to bring about the molecular changes at the two molecular levels
investigated.

This is the peer reviewed version of the following article: Aouzelleg, A., Bull, L.-A., Price, N.C. and Kelly, S.M. (2004), Molecular studies of pressure/temperature-induced structural changes in bovine β-lactoglobulin. J. Sci. Food Agric., 84: 398-404., which has been published in final form at https://doi.org/10.1002/jsfa.1669 . This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.