The structure of three food proteins, ovalbumin, lysozyme and beta-lactoglobulin were investigated when subjected to pressure, temperature and holding time. Structural effects were determined by the examination of circular dichroism spectra. Experiments were performed using pressures of up to 105 MPa, temperatures up to 79degreesC and holding times of 30 minutes using experimental design methodology and compared with ultra high pressures (600 MPa). Examination of the spectra showed that the structure of the three proteins behaved differently to the processing conditions. beta-lactoglobulin was found to be the least stable protein while lysozyme was the most stable protein. The higher pressure of 105 MPa was not sufficient to cause structural change when used at ambient conditions but when used in conjunction with raised temperatures and holding time, the applied energy was found to be sufficient to disrupt the protein structure.
- high pressure
- experimental design
- protein structure
- circular dichroism
Bull, L. A., & Schaschke, C. J. (2002). Interactive effects of pressure, temperature and time on the molecular structure of ovalbumin, lysozyme and beta-lactoglobulin. High Pressure Research, 22(3-4), 689-691. https://doi.org/10.1080/08957950212432