Measurements of residual enzyme activity and FTIR-spectroscopy reveale
d that mushroom polyphenoloxidase is a thermosensitive enzyme readily
inactivated by temperatures exceeding 50 degrees C. The enzyme is, how
ever, very pressure stable. At room temperature no enzyme inactivation
occurred at pressures up to 6 kbar. FTIR-spectroscopy revealed that a
modification in enzyme conformation occurred below 9 kbar. Kinetic st
udies showed that pressure and temperature did not always act synergis
tically with respect to enzyme inactivation. FTIR-spectroscopy showed
that pressure- or temperature-induced changes were considerably differ
ent. Both temperature and pressure-temperature inactivation were only
slightly influenced by pH (in the pH-range 5.5-7.5).