Authors:
B. Wang Chinese Academy of Sciences Center for Molecular Science, Institute of Chemistry Beijing 100080 China Beijing 100080 China

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B. Han Chinese Academy of Sciences Center for Molecular Science, Institute of Chemistry Beijing 100080 China Beijing 100080 China

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F. Tan Chinese Academy of Sciences Center for Molecular Science, Institute of Chemistry Beijing 100080 China Beijing 100080 China

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Abstract  

The influence of solution composition (pH, salts, and chelant) on the thermostability of horse liver alcohol dehydrogenase was studied by differential scanning calorimetry (DSC) in the pH range from7.51 to 9.50 and showing the enzyme catalytic activity. The experiments demonstrated that the effect of increasing pH on the heat denaturation temperature of the enzyme was slight, but the denaturation enthalpy was considerably increased, indicating the enzyme conformation alteration by changing pH and the presence of enthalpy-entropy compensation. The effect of ionic strength on thermostability was not noticeable, i.e., the electrostatic interactions were not a dominant factor for the thermostability. The anions Cl and SCN imposed diverse influence upon the enzyme thermostability, and SCNcan reduce the thermostability considerably. The chelant 1,10-phenanthroline, which can reversibly bind together with the zinc ions functioning the catalytic action in the enzyme molecules, increases the thermostability considerably. The hydration of the enzyme plays an important role to the thermostability.

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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