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Stability of immobilized α-chymotrypsin

✍ Scribed by Yasuko Kawamura; Kazuhiro Nakanishi; Ryuichi Matsuno; Tadashi Kamikubo

Publisher
John Wiley and Sons
Year
1981
Tongue
English
Weight
829 KB
Volume
23
Category
Article
ISSN
0006-3592

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Stability of immobilized α-chymotrypsin
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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

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## Abstract Electron paramagnetic resonance (EPR) spectroscopy has been applied in concert with measurements of catalytic activity and the quantity of active immobilized protein to study the deactivation in 50% __n__‐propanol of α‐chymotrypsin immobilized on CNBr–Sepharose 4B. These analyses focus