STABILITY OF IMMOBILIZED ALPHA-CHYMOTRYPSIN IN SUPERCRITICAL CARBON-DIOXIDE

Inactivation of immobilized alpha-chymotrypsin in supercritical carbon dioxide was with a first-order kinetic behaviour. The increase in eit her the pressure or the temperature of the fluid enhanced the inactiva tion process of the enzyme. The fluid density was shown as a key param eter on the enzyme stability, enhancing the half-life time proportiona lly to the physical phase of CO2, as follows: liquid > supercritical > gas. However, the number of pressurization/depressurization cycles, a nd the water content of the derivative increased greatly the loss of a ctivity.