The effect of high temperature and high hydrostatic pressure on the residua
l hydrolytic activity of a commercial Rhizomucor miehei lipase has been stu
died. Inactivation at high temperature and/or high pressure was carried out
. Under non-denaturing pressure conditions, results showed that pressurisat
ion protects enzymes against thermal deactivation. This is in accordance wi
th previous results obtained with enzymes from mesophilic sources, such as
invertase and galactosidases.