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Journal of Solid Phase Biochemistry

, Volume 3, Issue 2, pp 119–131 | Cite as

A physico-chemical analysis of soluble and immobilized enzyme stabilization

  • N. N. Ugarova
  • G. D. Roshkova
  • I. V. Berezin
Article
  • 34 Downloads

Abstract

The literature and our experimental data on the effect of chemical modification and immobilization on the thermostability of enzymes are analyzed. The effect of various factors causing changes in the stability of enzymes after their modification or immobilization is demonstrated. It is shown that changes in the temperature dependence of the inactivation rate constant are associated with the change in the effective values of thermodynamic activation parameters for the inactivation processes. An increase in the activation energy of thermoinactivation, Ea, leads to the stabilization of a modified or immobilized enzyme at temperatures below the iso-kinetic temperature (“low-temperature” stabilization) and a decrease inE a entails a “high-temperature” stabilization of enzymes. It is shown that with immobilized enzymes the high-temperature stabilization is invariably observed.

Keywords

Immobilize Enzyme Chymotrypsin Succinic Anhydride Conformational Mobility Inactivation Rate Constant 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Humana Press Inc. 1979

Authors and Affiliations

  • N. N. Ugarova
    • 1
  • G. D. Roshkova
    • 1
  • I. V. Berezin
    • 1
  1. 1.Department of Chemical EnzymologyMoscow State UniversityMoscowUSSR

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