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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/435

Title: Thermal stability of alcohol dehydrogenase enzyme determined by activity assay and calorimetry
Authors: Nath, Sunil
Satpathy, Gyana R
Mantri, Rahul
Deep, Shashank
Ahluwalia, Jagdish C
Keywords: Activity assay
Alcohol dehydrogenase
Denaturation enthalpy
Denaturation temperature
Kinetic parameters
Thermal stability
Issue Date: 1998
Citation: Thermochimica acta, 309, 193-196
Abstract: The thermostability of pure yeast alcohol dehydrogenase was investigated at various temperatures, in the presence and absence of sucrose, by both activity assay and differential scanning calorimetry. The thermal inactivation exhibited nonlinear blphasic behavior. The thermal inactivation rate constants and the magnitude of the heat-stable and heat-labile fractions of the enzyme were quantified. The values of the denaturation temperature were experimentally measured by calorimetry. It was found that although activity assay and calorimetry are based on different principles, they yield results that agree well with each other. However, each technique provides unique data (e.g. enzyme activity vis-a-vis basic thermodynamic properties, such as the denaturation enthalpy) and the two techniques may be considered complementary to each other.
URI: http://eprint.iitd.ac.in/dspace/handle/2074/435
Appears in Collections:Biochemical Engg. and Biotechnology

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