Enzyme-substrate interaction based approach for screening electroactive microorganisms for Microbial Fuel Cell applications
Alcohol dehydrogenase (ADH) of A. aceti is one of the potential enzyme for biological fuel cell applications. The modeled structure of ADH of A. aceti and its validation has been reported. The docking investigations have been made to assess the catalytic activity of the modeled ADH. The experimental results show that the modeled ADH of A. aceti has lowest binding affinity to its substrate when compared with the ADH structures of few other microorganisms. It indicates that the ADH of A. aceti has higher catalytic activity and better electrogenic activity. This study documents a computational procedure for screening electroactive microorganisms for biological fuel cell applications.
Alcohol dehydrogenase; Enzymes; Ethanol; Homology Modeling
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