THERMAL DEACTIVATION OF IMMOBILIZED CATALASE

Authors

Sawsan A. Abdel-Halim, front Cbemistry Department, Faculty of Science, Helwan University

Article Type

Original Study

Abstract

The rates of enzyme catalyzed re­actions typically increase in Arrhenius fashion near the enzyme natural tem­perature, but increasing temperature eventually results in rapid decline in enzyme activity. Thermal deactivation of enzyme may involve both reversible and irreversible processes. When the temperature is kept constant.a num­ber of enzyme systems are found to be irreversibly denatured with time, of­ten following approximately a first-order decay law(l). If the heat stability of an enzyme is enhanced by immobil­ization, the potential utilization of such enzymes will be extensive(2,3). In this work the thermal deactivation rate measurements were reported for both the free and immobilized forms of cat-alase.

Recommended Citation

Abdel-Halim, Sawsan A. (1991) "THERMAL DEACTIVATION OF IMMOBILIZED CATALASE," Mansoura Medical Journal: Vol. 20 : Iss. 1 , Article 3.
Available at: https://doi.org/10.21608/mjmu.1991.139113

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