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