ISSN:
1573-6784
Source:
Springer Online Journal Archives 1860-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Summary Temperature dependence of the rate constant of irreversible thermal inactivation, kin, of immobilized α-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 plot (log kin versus reciprocal temperature). However, if the number of such bonds is moderate or small (six or two), the temperature dependence of kin, has a pronounced ‘zig-zag’ character. This difference in the inactivation behaviour is attributed to an ability of ‘moderately or mildly’ attached α-chymotrypsins to accomplish a transition into a less ordered, catalytically inactive conformation and to inability of ‘rigidly’ bound enzyme to pass such a transition. Chaotropic salts additionally stabilize this loose conformation of ‘mildly or moderately’ bound α-chymotrypsins against irreversible thermal inactivation but are without effect on the stability of ‘rigidly’ bound enzyme.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00152992
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