𝔖 Bobbio Scriptorium
✦   LIBER   ✦

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

No coin nor oath required. For personal study only.

✦ 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


Stability of immobilized α-chymotrypsin
✍ Yasuko Kawamura; Kazuhiro Nakanishi; Ryuichi Matsuno; Tadashi Kamikubo 📂 Article 📅 1981 🏛 John Wiley and Sons 🌐 English ⚖ 829 KB
Thermal stability of immobilized α-chymo
✍ Anna A. Panova; V. Yu. Levitsky; Andrey V. Levashov; Vadim V. Mozhaev 📂 Article 📅 1995 🏛 Springer-Verlag 🌐 English ⚖ 447 KB

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