Interactive effects of pressure, temperature and time on the molecular structure of beta-lactoglobulin

We studied the combined effects of several variables, using temperatures up to 79 degrees C and pressures up to 105 MPa, on beta-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 s ufficient to disrupt the tertiary structure of the protein. processing cond itions applied at specific pH therefore could act in combination to cause s tructural changes.