Stability of immobilized α-chymotrypsin in supercritical carbon dioxide
✍ Scribed by Pedro Lozano; Antonio Avellaneda; Raphaël Pascual; José L. Iborra
- Publisher
- Springer Netherlands
- Year
- 1996
- Tongue
- English
- Weight
- 393 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0141-5492
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✦ Synopsis
Inactivation of immobilized c~-chymotrypsin in supercritical carbon dioxide was with a first-order kinetic behaviour. The increase in either the pressure or the temperature of the fluid enhanced the inactivation process of the enzyme. The fluid density was shown as a key parameter on the enzyme stability, enhancing the half-life time proportionally to the physical phase of CO2, as follows: liquid > supercritical > gas. However, the number of pressurization/depressurization cycles, and the water content of the derivative increased greatly the loss of activity.
📜 SIMILAR VOLUMES
The reaction rates in supercritical carbon dioxide at optimized conditions and in n-hexane were slmllar.
Temperature dependence of the rate constant of irreversible thermal inactivation, kin, of immobilized a-chymotrypsin depends markedly on the number of covalent bonds between the enzyme and support. When the number of bonds is big enough (thirteen), the dependence is linear as presented in Arrhenius