Pressure unfolding facilitates the formation of temperature gels

The formation of protein aggregates after pressure treatment was investigat ed by Fourier Transform Infrared Spectroscopy (FTIR). The results show that the pressure unfolded protein ends in a conformation, after the release of the pressure, which has an increased tendency to aggregate, even at temper atures lower than the denaturation temperature of the untreated protein. Af ter pressure pretreatment the infrared spectrum shows the same intermolecul ar antiparallel beta -structure features as observed after a temperature tr eatment that gives rise to protein gelation. On the other hand, this struct ure can be destabilized by applying moderate pressures, which are significa ntly lower than the corresponding denaturation pressure.