Eastern Kentucky University

Poster Title

Thermophilic Enzyme Stability: Investigating the Stability of Alcohol Dehydrogenase in Bacillus Stearothermophilus

Institution

Eastern Kentucky University

Abstract

Alcohol dehydrogenases (ADH) are a group of enzymes occurring in many organisms that facilitate the conversion between alcohols and aldehydes or ketones. In humans, they serve to detoxify alcohols. Understanding the mechanisms of enzyme action continues to be an active field of research. Enzymes from thermophiles (organisms thriving at high temperatures) are stable under conditions destroying enzymes from mesophiles (organisms such as ourselves living at more normal temperatures). While several studies have been done in order to determine the nature of thermophilic enzyme stability, I have extended our understanding of this molecule. I have followed the activity of thermophilic ADH as a function of temperature changes and levels of denaturants, showing its stability relative to homologous enzymes from mesophiles. This work will help us to understand and control inherent instability in enzymes for therapeutic and industrial work.

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Thermophilic Enzyme Stability: Investigating the Stability of Alcohol Dehydrogenase in Bacillus Stearothermophilus

Alcohol dehydrogenases (ADH) are a group of enzymes occurring in many organisms that facilitate the conversion between alcohols and aldehydes or ketones. In humans, they serve to detoxify alcohols. Understanding the mechanisms of enzyme action continues to be an active field of research. Enzymes from thermophiles (organisms thriving at high temperatures) are stable under conditions destroying enzymes from mesophiles (organisms such as ourselves living at more normal temperatures). While several studies have been done in order to determine the nature of thermophilic enzyme stability, I have extended our understanding of this molecule. I have followed the activity of thermophilic ADH as a function of temperature changes and levels of denaturants, showing its stability relative to homologous enzymes from mesophiles. This work will help us to understand and control inherent instability in enzymes for therapeutic and industrial work.